HK40110597A - Silk coated synthetic fabrics - Google Patents

Description

Silk-coated synthetic fabrics

Cross-references to related applications

This application claims the benefit of U.S. Provisional Patent Application No. 63/161,929, filed March 16, 2021, and U.S. Provisional Patent Application No. 63/319,765, filed March 14, 2022, each of which is incorporated herein by reference in its entirety.

Technical Field

This disclosure pertains to the field of synthetic fabrics coated with silk core proteins and protein fragments.

Background Technology

Silk is a natural polymer produced by various insects and spiders, and consists of a core protein, a sericin, and a gelatinous coating composed of non-filamentous proteins and sericin. Silk fibers are lightweight, breathable, and hypoallergenic. Silk is comfortable to wear next to the skin and provides excellent insulation; it keeps the wearer warm in cold temperatures and is cooler than many other fabrics in warmer temperatures.

Summary of the Invention

This disclosure provides an article comprising a fabric and a coating, wherein the coating comprises a surfactant and/or emulsifier system, and silk core protein fragments having a molecular weight selected from about 1 kDa to about 5 kDa, about 5 kDa to about 10 kDa, about 6 kDa to about 17 kDa, about 10 kDa to about 15 kDa, about 14 kDa to about 30 kDa, about 15 kDa to about 20 kDa, about 17 kDa to about 39 kDa, about 20 kDa to about 25 kDa, and about 25 kDa. The average weight-average molecular weight is approximately 30 kDa to 30 kDa, approximately 30 kDa to 35 kDa, approximately 35 kDa to 40 kDa, approximately 39 kDa to 54 kDa, approximately 39 kDa to 80 kDa, approximately 40 kDa to 45 kDa, approximately 45 kDa to 50 kDa, approximately 50 kDa to 55 kDa, approximately 55 kDa to 60 kDa, approximately 60 kDa to 100 kDa, or approximately 80 kDa to 144 kDa, and the polydispersity ranges from 1 to 5. In some embodiments, the polydispersity of the fibroin fragment is 1 to 1.5, approximately 1.5 to 2.0, approximately 2.0 to 2.5, approximately 2.5 to 3.0, approximately 3.0 to 3.5, approximately 3.5 to 4.0, approximately 4.0 to 4.5, or approximately 4.5 to 5.0. In some embodiments, the polydispersity of the fibroin fragment is approximately 1.5 to 3.0. In some embodiments, the silk core protein fragments comprise one or more of low molecular weight silk core protein fragments and medium molecular weight silk core protein fragments. In some embodiments, the article further comprises about 0.01% (w/w) to about 10% (w/w) sericin relative to the silk core protein fragments. In some embodiments, the fabric comprises one or more of the following: polyester, polyamide, polyaramid, polytetrafluoroethylene, polyethylene, polypropylene, polyurethane, silicone, mixtures of polyurethane and polyethylene glycol, ultra-high molecular weight polyethylene, high-performance polyethylene, nylon, LYCRA (polyester-polyurethane copolymer, also known as SPANDEX and elastomer), or mixtures thereof. In some embodiments, the coating further comprises one or more of a wetting agent, defoamer, softener, wicking agent, and antimicrobial agent. In some embodiments, the w/w ratio of the silk core protein fragments in the coating to the surfactant and/or emulsifier system is about 99:1, about 98:2, about 97:3, about 96:4, about 95:5, about 94:6, about 93:7, about 92:8, about 91:9, about 90:10, about 89:11, about 88:12, about 87:13, about 86:14, about 85:15, about 84:16, about 83:17, about 82:18, about 81:19, about 80:20, or about 79:21. Approximately 78:22, 77:23, 76:24, 75:25, 74:26, 73:27, 72:28, 71:29, 70:30, 69:31, 68:32, 67:33, 66:34, 65:35, 64:36, 63:37, 62:38, 61:39, 60:40, 59:41, 58:42, 57:43, 56:44, 55:45, 54:46, 53: 47, Approx. 52:48, Approx. 51:49, Approx. 50:50, Approx. 49:51, Approx. 48:52, Approx. 47:53, Approx. 46:54, Approx. 45:55, Approx. 44:56, Approx. 43:57, Approx. 42:58, Approx. 41:59, Approx. 40:60, Approx. 39:61, Approx. 38:62, Approx. 37:63, Approx. 36:64, Approx. 35:65, Approx. 34:66, Approx. 33:67, Approx. 32:68, Approx. 31:69, Approx. 30:70, Approx. 29:71, Approx. 28:72, Approx. The ratios are approximately 27:73, 26:74, 25:75, 24:76, 23:77, 22:78, 21:79, 20:80, 19:81, 18:82, 17:83, 16:84, 15:85, 14:86, 13:87, 12:88, 11:89, 10:90, 9:91, 8:92, 7:93, 6:94, 5:95, 4:96, 3:97, 2:98, or 1:99. In some embodiments, the w/w ratio of the silk core protein fragments in the coating to the surfactant and/or emulsifier is approximately 1:1, 1:2, 1:4, 1:8, 1:16, or 1:32. In some embodiments, the w/w ratio of the silk core protein fragments in the coating to the surfactant and/or emulsifier system is about 1:1, about 1:2, about 1:3, about 1:4, about 1:5, about 1:6, about 1:7, about 1:8, about 1:9, about 1:10, about 1:11, about 1:12, about 1:13, about 1:14, about 1:15, about 1:16, about 1:17, about 1:18, about 1:19, about 1:20, about 1:21, about 1:22, about 1:23, about 1:24, about 1:25, about 1:26, about 1:27, about 1:28, about 1:29, about 1:30, about 1:31, or about 1:32. In some embodiments, the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene sorbitan monooleate, polyoxyethylene sorbitan trioleate, polyoxyethylene castor oil, and any combination thereof. In some embodiments, the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene (10-30) sorbitan monooleate, polyoxyethylene (10-30) sorbitan trioleate, polyoxyethylene (10-50) castor oil, and any combination thereof. In some embodiments, the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene (20) sorbitan monooleate, polyoxyethylene (20) sorbitan trioleate, polyoxyethylene (29) castor oil, and any combination thereof. In some embodiments, the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene (20) sorbitol monolaurate, polyoxyethylene (20) sorbitol monopalmitate, polyoxyethylene (20) sorbitol monostearate, polyoxyethylene (20) sorbitol tristearate, and any combination thereof. In some embodiments, the surfactant and/or emulsifier system comprises one or more of the following: sorbitol monofatty acid, sorbitol trifatty acid, castor oil, and any combination thereof. In some embodiments, the surfactant and/or emulsifier system comprises one or more of the following: cocoyl glucoside, decyl glucoside, lauryl glucoside, sucrose cocoate, octyl/octyl glucoside, octyl/octyl glucoside, and any combination thereof. In some embodiments, the HLB of the surfactant and/or emulsifier system is from about 11 to about 13.50. In some embodiments, the HLB of the surfactant and/or emulsifier system is about 11 to about 11.50, about 11.50 to about 12, about 12 to about 12.50, about 12.50 to about 13, or about 13 to about 13.50. In some embodiments, the article has improved moisture management compared to similar articles comprising similar fabrics but without a coating. In some embodiments, moisture management is evaluated by absorbency testing, vertical wicking testing, or drying rate testing. In some embodiments, the article has improved drape compared to similar articles comprising similar fabrics but without a coating. In some embodiments, the article has improved smoothness compared to similar articles comprising similar fabrics but without a coating. In some embodiments, the article has improved hand feel compared to similar articles comprising similar fabrics but without a coating. In some embodiments, the article has a lower charge density at a given pH value compared to similar articles comprising similar fabrics but without a coating.

This disclosure provides a method for preparing a silk core protein-coated fabric, the method comprising: applying a solution containing a surfactant and/or emulsifier system to the fabric; applying a silk core protein fragment solution to the fabric; and drying the fabric. This disclosure also provides a method for preparing a silk core protein-coated fabric, the method comprising: applying a solution containing a surfactant and/or emulsifier system and silk core protein fragments to the fabric; and drying the fabric. In some embodiments, the concentration of the silk core protein fragments in the solution ranges from 0.01 g/L to about 100 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier system in the solution ranges from 0.01 g/L to about 100 g/L. In some embodiments, the silk core protein fragment has an average weight-average molecular weight selected from about 1 kDa to about 5 kDa, about 5 kDa to about 10 kDa, about 6 kDa to about 17 kDa, about 10 kDa to about 15 kDa, about 14 kDa to about 30 kDa, about 15 kDa to about 20 kDa, about 17 kDa to about 39 kDa, about 20 kDa to about 25 kDa, about 25 kDa to about 30 kDa, about 30 kDa to about 35 kDa, about 35 kDa to about 40 kDa, about 39 kDa to about 54 kDa, about 39 kDa to about 80 kDa, about 40 kDa to about 45 kDa, about 45 kDa to about 50 kDa, about 50 kDa to about 55 kDa, about 55 kDa to about 60 kDa, about 60 kDa to about 100 kDa, or about 80 kDa to about 144 kDa, and a polydispersity ranging from 1 to about 5. In some embodiments, the polydispersity of the fibroin fragments is from 1 to about 1.5, from about 1.5 to about 2.0, from about 2.0 to about 2.5, from about 2.5 to about 3.0, from about 3.0 to about 3.5, from about 3.5 to about 4.0, from about 4.0 to about 4.5, or from about 4.5 to about 5.0. In some embodiments, the polydispersity of the fibroin fragments is from about 1.5 to about 3.0. In some embodiments, the fibroin fragments comprise one or more of low molecular weight fibroin fragments and medium molecular weight fibroin fragments. In some embodiments, the solution further comprises about 0.01% (w/w) to about 10% (w/w) of sericin relative to the fibroin fragments. In some embodiments, the fabric comprises one or more of the following: polyester, polyamide, polyaramid, polytetrafluoroethylene, polyethylene, polypropylene, polyurethane, silicone, a mixture of polyurethane and polyethylene glycol, ultra-high molecular weight polyethylene, high-performance polyethylene, nylon, LYCRA (polyester-polyurethane copolymer, also known as SPANDEX and elastomer), or mixtures thereof. In some embodiments, the solution also comprises one or more of a wetting agent, defoamer, softener, wicking agent, and antimicrobial agent. In some embodiments, the w/w ratio of the silk core protein fragment to the surfactant and/or emulsifier system is about 99:1, about 98:2, about 97:3, about 96:4, about 95:5, about 94:6, about 93:7, about 92:8, about 91:9, about 90:10, about 89:11, about 88:12, about 87:13, about 86:14, about 85:15, about 84:16, about 83:17, about 82:18, about 81:19, about 80:20, about 79:21, about 78... :22, 77:23, 76:24, 75:25, 74:26, 73:27, 72:28, 71:29, 70:30, 69:31, 68:32, 67:33, 66:34, 65:35, 64:36, 63:37, 62:38, 61:39, 60:40, 59:41, 58:42, 57:43, 56:44, 55:45, 54:46, 53:47 Approximately 52:48, Approximately 51:49, Approximately 50:50, Approximately 49:51, Approximately 48:52, Approximately 47:53, Approximately 46:54, Approximately 45:55, Approximately 44:56, Approximately 43:57, Approximately 42:58, Approximately 41:59, Approximately 40:60, Approximately 39:61, Approximately 38:62, Approximately 37:63, Approximately 36:64, Approximately 35:65, Approximately 34:66, Approximately 33:67, Approximately 32:68, Approximately 31:69, Approximately 30:70, Approximately 29:71, Approximately 28:72, Approximately 2 7:73, about 26:74, about 25:75, about 24:76, about 23:77, about 22:78, about 21:79, about 20:80, about 19:81, about 18:82, about 17:83, about 16:84, about 15:85, about 14:86, about 13:87, about 12:88, about 11:89, about 10:90, about 9:91, about 8:92, about 7:93, about 6:94, about 5:95, about 4:96, about 3:97, about 2:98, or about 1:99. In some embodiments, the w/w ratio of the silk core protein fragment to the surfactant and/or emulsifier system is about 1:1, about 1:2, about 1:4, about 1:8, about 1:16, or about 1:32. In some embodiments, the w/w ratio of the silk core protein fragment to the surfactant and/or emulsifier system is about 1:1, about 1:2, about 1:3, about 1:4, about 1:5, about 1:6, about 1:7, about 1:8, about 1:9, about 1:10, about 1:11, about 1:12, about 1:13, about 1:14, about 1:15, about 1:16, about 1:17, about 1:18, about 1:19, about 1:20, about 1:21, about 1:22, about 1:23, about 1:24, about 1:25, about 1:26, about 1:27, about 1:28, about 1:29, about 1:30, about 1:31, or about 1:32. In some embodiments, the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene sorbitan monooleate, polyoxyethylene sorbitan trioleate, polyoxyethylene castor oil, and any combination thereof. In some embodiments, the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene (10-30) sorbitan monooleate, polyoxyethylene (10-30) sorbitan trioleate, polyoxyethylene (10-50) castor oil, and any combination thereof. In some embodiments, the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene (20) sorbitan monooleate, polyoxyethylene (20) sorbitan trioleate, polyoxyethylene (29) castor oil, and any combination thereof. In some embodiments, the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene (20) sorbitol monolaurate, polyoxyethylene (20) sorbitol monopalmitate, polyoxyethylene (20) sorbitol monostearate, polyoxyethylene (20) sorbitol tristearate, and any combination thereof. In some embodiments, the surfactant and/or emulsifier system comprises one or more of the following: sorbitol monofatty acid, sorbitol trifatty acid, castor oil, and any combination thereof. In some embodiments, the surfactant and/or emulsifier system comprises one or more of the following: cocoyl glucoside, decyl glucoside, lauryl glucoside, sucrose cocoate, octyl/octyl glucoside, octyl/octyl glucoside, and any combination thereof. In some embodiments, the HLB of the surfactant and/or emulsifier system is from about 11 to about 13.50. In some embodiments, the HLB of the surfactant and/or emulsifier system is about 11 to about 11.50, about 11.50 to about 12, about 12 to about 12.50, about 12.50 to about 13, or about 13 to about 13.50. In some embodiments, the drying includes heating. In some embodiments, the pH of the solution is acidic. In some embodiments, the pH of the solution is about 3.5 to about 4, about 4 to about 4.5, about 4.5 to about 5, about 5 to about 5.5, or about 5.5 to about 6.

This disclosure also provides an article prepared by the method described herein, according to any one of claims 25 to 49. In some embodiments, the article has improved moisture management compared to similar articles comprising similar fabrics but without a coating. In some embodiments, moisture management is evaluated by an absorbency test, a vertical wicking test, or a drying rate test. In some embodiments, the article has improved drape compared to similar articles comprising similar fabrics but without a coating. In some embodiments, the article has improved smoothness compared to similar articles comprising similar fabrics but without a coating. In some embodiments, the article has improved hand feel compared to similar articles comprising similar fabrics but without a coating. In some embodiments, the article has a lower charge density at a given pH value compared to similar articles comprising similar fabrics but without a coating.

Attached Figure Description

Figure 1 is a flowchart showing various embodiments for producing the silk core protein fragment (SPF) of this disclosure.

Figure 2 is a flowchart showing various parameters that can be modified during the process of producing a silk protein fragment solution of this disclosure, in the extraction and dissolution steps.

Figure 3 is a graph showing the absorbency of ActivatedSilk ^™ with an octyl/octyl glucoside coating on various interlocking nylon fabrics; unfinished nylon interlocking fabrics cannot absorb moisture due to poor absorbency; after coating ActivatedSilk ^™ with an octyl/octyl glucoside coating, the absorbency of all nylon interlocking fabrics increased significantly.

Figure 4 is a graph showing the absorbency of Active Yarn ^™ with an octyl/octyl glucoside coating on various nylon fabrics, excluding the interlocking structure; untreated nylon fabrics have poor absorbency or no absorbency; after coating Active Yarn ^™ with an octyl/octyl glucoside coating, the absorbency of all nylon fabrics increases significantly.

Figure 5 is a graph showing the unwashed absorbency curves produced by varying the concentration of polyoxyethylene (29) castor oil in the emulsifier mixture (thus changing the HLB) before addition to the coating solution. In all samples, the filament concentration in the coating solution was 1 g/L.

Figure 6 is a graph showing the unwashed hand feel grade curves produced by varying the concentration of polyoxyethylene (29) castor oil in the emulsifier mixture (thus changing the HLB) before addition to the coating solution. In all samples, the silk concentration in the coating solution was 1 g/L.

Figures 7A-7D are graphs showing the moisture management data for unwashed (Figure 7A), 5-washed (Figure 7B), 10-washed (Figure 7C), and 25-washed (Figure 7D) samples produced by varying the concentration of the emulsion mixture (polyoxyethylene (20) dehydrated sorbitol monooleate, polyoxyethylene (20) dehydrated sorbitol trioleate, polyoxyethylene (29) castor oil, and water in a ratio of 2:4:8:10) in the final coating solution; in all samples, the filament concentration in the coating solution was 1 g/L.

Figures 8A-8D are graphs showing the results of unwashed (Figure 8A), 5-washed (Figure 8B), 10-washed (Figure 8C), and 25-washed (Figure 8D) hand feel grades produced by varying the concentration of the emulsion mixture (polyoxyethylene (20) dehydrated sorbitol monooleate, polyoxyethylene (20) dehydrated sorbitol trioleate, polyoxyethylene (29) castor oil, and water in a ratio of 2:4:8:10) in the final coating solution; 1 represents the best hand feel grade score, and 8 represents the worst hand feel grade score; in all samples, the silk concentration in the solution was 1 g/L.

Figures 9A-9D are graphs showing the hand feel grades obtained by varying the concentration of medium molecular weight yarns in the final coating solution for unwashed (Figure 9A), 5-wash (Figure 9B), 10-wash (Figure 9C), and 25-wash (Figure 9D) grades; 1 represents the best grade, and 8 represents the worst grade.

Figures 10A-10D are graphs showing the results of moisture management for unwashed (Figure 10A), 5-wash (Figure 10B), 10-wash (Figure 10C), and 25-wash (Figure 10D) results by varying the concentration of medium molecular weight filaments in the final coating solution.

Figures 11A-11D are graphs showing the quantitative UV/Vis experiment of fabrics coated with low molecular weight active yarns and polyoxyethylene (20) monooleate solution. Figure 11A: Graph showing the percentage of yarn loss relative to fiber surface area after five washes. Figure 11B: Graph showing the quantitative mass of yarn on the coated fabric relative to fiber surface area. Figure 11C: Graph showing the percentage of yarn loss relative to fabric type after five washes. Figure 11D: Graph showing the quantitative mass of yarn on each fabric before and after five washes according to fabric type.

Figure 12 is a graph showing the quantitative UV/Vis experiment of a fabric coated with low molecular weight active yarn and polyoxyethylene (20) monooleate solution. The figure shows the quantitative mass of the yarn on the coated fabric relative to the fabric mass (g/m² (GSM)). This mass depends on the weave type, fiber content, and filament denier.

Figures 13A-13C comprise a series of graphs showing the potentiometric titration curves of charge density at pH 5 for unfinished heavy double-knit nylon fabrics (Figure 13A), heavy double-knit nylon fabrics treated with reactive yarns (Figure 13B), and heavy double-knit nylon fabrics treated with Archroma RPU wetting agent (Figure 13C). Each fabric has titration curves obtained at unwashed (Figures 13A-13C, left) and after five washes (Figures 13A-13C, right). The change in charge density at pH 5 after washing is expressed as ΔC.

Detailed Implementation

This disclosure provides articles comprising coated fabrics and methods for preparing such articles, wherein the coating comprises a surfactant and/or emulsifier system and silk core protein fragments.

Silk is a natural polymer produced by various insects and spiders. The silk produced by the silkworm (Bombyx mori) consists of filamentin, sericin, and a gelatinous coating composed of non-filamentous proteins, sericin. Sericin is an FDA-approved, edible, non-toxic, and relatively inexpensive protein derived from silkworm cocoons. The structure and content of the amino acids in filamentin are very similar to those in human tissue.

Methods for preparing filamentin fragments are known and described, for example, in U.S. Patents 9,187,538, 9,511,012, 9,517,191, 9,522,107, 9,522,108, 9,545,369, and 10,166,177, all of which are incorporated herein by reference in their entirety.

Recent advances in silk materials technology include the emergence of top-down and bottom-up silk cocoon engineering, particularly aqueous solutions that regenerate cocoons into silk, and the use of genetic engineering to produce recombinant silks with molecularly defined compositions (Tran et al., A review of the emerging role of silk for the treatment of the eye, Pharm. Res., 2018, Vol. 35, pp. 1-16). In recent years, silk core proteins have been reported to be used in ocular tissue reconstruction, corneal tissue engineering, and ocular surface repair due to their biocompatibility, tunable properties, and transparency. It has been found that silk membranes support corneal cell growth and form layered epithelial cell sheets equivalent to the amniotic basal layer (Lawrence et al., Silk film biomaterials for cornea tissue engineering, Biomaterials, 2009; 30(7):1299-308; Harkin et al., Silk fibroin in ocular tissue reconstruction, Biomaterials, 2011; Chirtla et al., Bombyx mori silk fibroin membranes as potential substrate for epithelial constructs used in the management of ocular surface disorders. Tissue Engineering Pan A, 2008; 14(7):1203-11.). It has been demonstrated that filocene and hydrolyzed peptide fragments can inhibit the transcription and upstream activation of NF-κB protein subunits and pro-inflammatory molecules, which are normally controlled by NF-κB (Hayden et al., Cell Research, 2011.21(2):223-244; Chon et al., International Journal of Molecular Medicine, 2012.30(5):1203-1210; Kim et al., J. Neurosurg., 2011.114(2):485-90; J. Microbiol. Biotechnol., 2012.22(4):494-500).

definition

As used in the foregoing sections and throughout the remainder of this specification, unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this disclosure pertains. All patents and publications mentioned herein are incorporated herein by reference in their entirety.

Unless otherwise specified, all percentages, parts, and ratios are based on the total weight of the eye care compositions disclosed herein. All such weights relating to the listed ingredients are based on activity levels and therefore exclude solvents or byproducts that may be present in commercially available materials, unless otherwise specified. The term “percentage by weight” may be expressed herein as “% by weight” or % w/w.

As used herein, the terms “a”, “an”, or “the” are generally interpreted to encompass both the singular and plural forms.

As used herein, the term “about” generally refers to a specific numerical value that includes a range of variation and acceptable error as determined by one of ordinary skill in the art, depending in part on how the value is measured or determined, i.e., the limitations of the measurement system. For example, “about” can mean zero variation, and a range of ±20 percent, ±10 percent, or ±5 percent of a given value.

For example, as used herein, the term "dermatologically acceptable carrier" means a carrier suitable for use in contact with the keratinized tissue of mammals without causing any adverse reactions (such as excessive toxicity, incompatibility, instability, or allergic reactions). Dermatologically acceptable carriers may include, but are not limited to, water, liquid or solid emollients, humectants, solvents, etc.

As used herein, the term “hydrophilic-lipophilic balance” (HLB) for surfactants and/or emulsifiers is a measure of their degree of hydrophilicity or hydrophobicity, determined by calculating values for different regions of the molecule, as described in the Griffin method: HLB = 20 * _Mh / M, where _Mh is the molecular weight of the hydrophilic portion of the surfactant and/or emulsifier, and M is the molecular weight of the entire surfactant and/or emulsifier molecule, with results ranging from 0 to 20. An HLB value of 0 corresponds to a completely lipophilic molecule, and an HLB value of 20 corresponds to a completely hydrophilic molecule. HLB values can be used to predict the properties of surfactants and/or emulsifiers in molecules: HLB < 10: lipid-soluble (water-insoluble), HLB > 10: water-soluble (lipid-insoluble), HLB = 1-3: defoamer, 3-6: W/O (water-in-oil) emulsifier, 7-9: wetting and spreading agent, 8-16: O/W (oil-in-water) emulsifier, 13-16: detergent, 16-18: solubilizer or water-soluble growth promoter.

As used herein, “weight-average molecular weight” refers to the average of two or more values of the weight-average molecular weight of the same composition of fibroin or its fragments, determined by two or more separate experimental readings.

As used herein, the term polymer “polydispersity (PD)” is generally used as a measure of the width of a polymer’s molecular weight distribution and is defined by the following formula:

As used herein, the term "substantially homogeneous" can refer to a filamentin-based protein fragment distributed in a normal distribution with respect to the identified molecular weight. As used herein, the term "substantially homogeneous" can refer to the uniform distribution of components or additives such as filamentin fragments, dermatologically acceptable carriers, etc., in the overall composition of this disclosure.

As used herein, the terms “silk fibroin peptide,” “silk fibroin protein fragment,” and “silk fibroin fragment” are used interchangeably. When molecular size is an important parameter, the molecular weight or the number of amino acid units is defined.

As used herein, the term "rapidly dissolving solids form" refers to rapidly dissolving solids forms, including lyophilized forms (filter cakes, flakes, films) and compressed tablets.

As used in this article, the term "peptide" or "protein" refers to a chain of amino acids linked together by peptide bonds (also known as amide bonds). The fundamental differentiating factors between proteins and peptides are size and structure. Peptides are smaller than proteins. Traditionally, peptides are defined as molecules consisting of 2 to 50 amino acids, while proteins are composed of 50 or more amino acids. Furthermore, the structure of peptides is often less defined than that of proteins, which can take on complex conformations known as secondary, tertiary, and quaternary structures.

As used herein, the term "silkcore protein" or "silk protein" refers to a class of structural proteins produced by certain silk-producing spider and insect species (see the definition provided in the WIPO Pearl-WIPO’s Multilingual Terminology Portal database https://wipopearl.wipo.int/en/linguistic). Silkcore proteins can include silkworm silkcore proteins, insect or spider silk proteins (e.g., spider silk proteins), recombinant spider proteins, silk proteins present in other spider silk types such as tubular silk protein (TuSP), flagellated silk protein, minor ampulla silk protein, alveolar silk protein, piriform silk protein, and polymerized sericin), silkcore proteins produced by genetically modified silkworms, or recombinant silkcore proteins.

As used herein, the term "silk core protein" refers to silkworm fibroin, silk core protein produced by genetically modified silkworms, or recombinant silkworm fibroin (see (1) Narayan (ed.), Encyclopedia of Biomedical Engineering, Vol. 2, Elsevier, 2019; (2) Kobayashi et al. (eds.), Encyclopedia of Polymeric Nanomaterials, Springer, 2014, https://link.springer.com/referenceworkentry/10.1007％2F978-3-642-36199-9_323-1). In one embodiment, the silk core protein is obtained from domesticated silkworms.

As used herein, the term "solid solution" refers to an active agent dissolved in a solid excipient matrix (such as a hydrophobic polymer) in molecular form, wherein the active agent is miscible with the polymer matrix excipient.

As used herein, the term "solid dispersion" refers to an active agent dispersed as crystalline or amorphous particles, wherein the active agent is dispersed in an amorphous polymer and randomly distributed among the polymer matrix excipients.

As used herein, the term "substantially homogeneous" may refer to silk-core protein fragments distributed in a normal distribution with respect to the identified molecular weight. As used herein, the term "substantially homogeneous" may also refer to the uniform distribution of components or additives (e.g., silk-core protein fragments, dermatologically acceptable carriers, etc.) in the overall silk eye care composition.

As used herein, the term "surface tension" refers to the tendency of a fluid surface to contract to the smallest possible surface area. At the liquid-air interface, surface tension arises because the attractive forces between liquid molecules (due to cohesion) are greater than the attractive forces between molecules in air (due to adhesion). The net effect is the inward force on the liquid surface, causing the liquid to behave as if its surface were covered by a stretched elastic membrane. Water has a higher surface tension (72.8 mN/m at 20°C) than most other liquids because water molecules have relatively strong attractive forces to each other through a network of hydrogen bonds.

SPF Definition and Properties

As used herein, a “silk protein fragment” (SPF) includes, but is not limited to, one or more of the following: a “silicone protein fragment” as defined herein; a “recombinant silk fragment” as defined herein; a “spider silk fragment” as defined herein; a “silicone-like protein fragment” as defined herein; a “chemically modified silk fragment” as defined herein; and/or a “sericin or sericin fragment” as defined herein. An SPF may have any molecular weight value or range described herein, and any polydispersity value or range described herein. As used herein, in some embodiments, the term “silk protein fragment” also refers to a silk protein comprising or composed of at least two identical repeating units, each of which is independently selected from naturally occurring silk polypeptides or variants thereof, amino acid sequences of naturally occurring silk polypeptides, or combinations thereof.

SPF molecular weight and polydispersity

In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 1 kDa to about 5 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 5 kDa to about 10 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 10 kDa to about 15 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 15 kDa to about 20 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 14 kDa to about 30 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 20 kDa to about 25 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 25 kDa to about 30 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 30 kDa to about 35 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 35 kDa to about 40 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 39 kDa to about 54 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 40 kDa to about 45 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 45 kDa to about 50 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 50 kDa to about 55 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 55 kDa to about 60 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 60 kDa to about 65 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 65 kDa to about 70 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 70 kDa to about 75 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 75 kDa to about 80 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 80 kDa to about 85 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 85 kDa to about 90 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 90 kDa to about 95 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 95 kDa to about 100 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 100 kDa to about 105 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 105 kDa to about 110 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 110 kDa to about 115 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 115 kDa to about 120 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 120 kDa to about 125 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 125 kDa to about 130 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 130 kDa to about 135 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 135 kDa to about 140 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 140 kDa to about 145 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 145 kDa to about 150 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 150 kDa to about 155 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 155 kDa to about 160 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 160 kDa to about 165 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 165 kDa to about 170 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 170 kDa to about 175 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 175 kDa to about 180 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 180 kDa to about 185 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 185 kDa to about 190 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 190 kDa to about 195 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 195 kDa to about 200 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 200 kDa to about 205 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 205 kDa to about 210 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 210 kDa to about 215 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 215 kDa to about 220 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 220 kDa to about 225 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 225 kDa to about 230 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 230 kDa to about 235 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 235 kDa to about 240 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 240 kDa to about 245 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 245 kDa to about 250 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 250 kDa to about 255 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 255 kDa to about 260 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 260 kDa to about 265 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 265 kDa to about 270 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 270 kDa to about 275 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 275 kDa to about 280 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 280 kDa to about 285 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 285 kDa to about 290 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 290 kDa to about 295 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 295 kDa to about 300 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 300 kDa to about 305 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 305 kDa to about 310 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 310 kDa to about 315 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 315 kDa to about 320 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 320 kDa to about 325 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 325 kDa to about 330 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 330 kDa to about 335 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 335 kDa to about 340 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 340 kDa to about 345 kDa. In one embodiment, the composition of this disclosure comprises an SPF having an average weight-average molecular weight selected from about 345 kDa to about 350 kDa.

In some embodiments, the compositions disclosed herein include SPF compositions selected from compositions #1001 to #2450, having a weight-average molecular weight selected from about 1 kDa to about 145 kDa, and a polydispersity selected from 1 to about 5 (including but not limited to 1), 1 to about 1.5 (including but not limited to 1), about 1.5 to about 2, about 1.5 to about 3, about 2 to about 2.5, about 2.5 to about 3, about 3 to about 3.5, about 3.5 to about 4, about 4 to about 4.5, and about 4.5 to about 5.

As used herein, “low molecular weight,” “low MW,” or “low-MW” SPF may include SPFs having a weight-average molecular weight or average weight-average molecular weight selected from about 5 kDa to about 38 kDa, about 14 kDa to about 30 kDa, or about 6 kDa to about 17 kDa. In some implementations, the target low molecular weight of certain SPFs may be a weight-average molecular weight of about 5 kDa, about 6 kDa, about 7 kDa, about 8 kDa, about 9 kDa, about 10 kDa, about 11 kDa, about 12 kDa, about 13 kDa, about 14 kDa, about 15 kDa, about 16 kDa, about 17 kDa, about 18 kDa, about 19 kDa, about 20 kDa, about 21 kDa, about 22 kDa, about 23 kDa, about 24 kDa, about 25 kDa, about 26 kDa, about 27 kDa, about 28 kDa, about 29 kDa, about 30 kDa, about 31 kDa, about 32 kDa, about 33 kDa, about 34 kDa, about 35 kDa, about 36 kDa, about 37 kDa, or about 38 kDa.

As used herein, “medium molecular weight,” “medium MW,” or “medium-MW” SPF may include SPFs with a weight-average molecular weight or average weight-average molecular weight selected from about 31 kDa to about 55 kDa or about 39 kDa to about 54 kDa. In some embodiments, the target medium molecular weight of certain SPFs may be a weight-average molecular weight of about 31 kDa, about 32 kDa, about 33 kDa, about 34 kDa, about 35 kDa, about 36 kDa, about 37 kDa, about 38 kDa, about 39 kDa, about 40 kDa, about 41 kDa, about 42 kDa, about 43 kDa, about 44 kDa, about 45 kDa, about 46 kDa, about 47 kDa, about 48 kDa, about 49 kDa, about 50 kDa, about 51 kDa, about 52 kDa, about 53 kDa, about 54 kDa, or about 55 kDa.

As used herein, “high molecular weight,” “high MW,” or “high-MW” SPFs may include SPFs with a weight-average molecular weight or average weight-average molecular weight selected from about 55 kDa to about 150 kDa. In some embodiments, the target high molecular weight of certain SPFs may be about 55 kDa, about 56 kDa, about 57 kDa, about 58 kDa, about 59 kDa, about 60 kDa, about 61 kDa, about 62 kDa, about 63 kDa, about 64 kDa, about 65 kDa, about 66 kDa, about 67 kDa, about 68 kDa, about 69 kDa, about 70 kDa, about 71 kDa, about 72 kDa, about 73 kDa, about 74 kDa, about 75 kDa, about 76 kDa, about 77 kDa, about 78 kDa, about 79 kDa, or about 80 kDa.

In some embodiments, the molecular weights described herein (e.g., low molecular weight fibers, medium molecular weight fibers, high molecular weight fibers) can be converted into an approximate number of amino acids contained in the corresponding SPF, as understood by those skilled in the art. For example, the average weight of the amino acids can be about 110 Daltons (i.e., 110 g/mol). Therefore, in some embodiments, dividing the molecular weight of the linear protein by 110 Daltons can be used to approximate the number of amino acid residues contained therein.

In one embodiment, the SPF of the composition disclosed herein has a polydispersity selected from 1 to 5.0, including but not limited to a polydispersity of 1. In one embodiment, the SPF of the composition disclosed herein has a polydispersity selected from about 1.5 to about 3.0. In one embodiment, the SPF of the composition disclosed herein has a polydispersity selected from 1 to about 1.5, including but not limited to a polydispersity of 1. In one embodiment, the SPF of the composition disclosed herein has a polydispersity selected from about 1.5 to about 2.0. In one embodiment, the SPF of the composition disclosed herein has a polydispersity selected from about 2.0 to about 2.5. In one embodiment, the SPF of the composition disclosed herein has a polydispersity selected from about 2.5 to about 3.0. In one embodiment, the SPF of the composition disclosed herein has a polydispersity selected from about 3.0 to about 3.5. In one embodiment, the SPF of the composition disclosed herein has a polydispersity selected from about 3.5 to about 4.0. In one embodiment, the SPF of the composition disclosed herein has a polydispersity selected from about 4.0 to about 4.5. In one embodiment, the SPF of the compositions disclosed herein has a polydispersity selected from about 4.5 to about 5.0.

In one embodiment, the SPF of the composition disclosed herein has a polydispersity of 1. In one embodiment, the SPF of the composition disclosed herein has a polydispersity of about 1.1. In one embodiment, the SPF of the composition disclosed herein has a polydispersity of about 1.2. In one embodiment, the SPF of the composition disclosed herein has a polydispersity of about 1.3. In one embodiment, the SPF of the composition disclosed herein has a polydispersity of about 1.4. In one embodiment, the SPF of the composition disclosed herein has a polydispersity of about 1.5. In one embodiment, the SPF of the composition disclosed herein has a polydispersity of about 1.6. In one embodiment, the SPF of the composition disclosed herein has a polydispersity of about 1.7. In one embodiment, the SPF of the composition disclosed herein has a polydispersity of about 1.8. In one embodiment, the SPF of the composition disclosed herein has a polydispersity of about 1.9. In one embodiment, the SPF of the composition disclosed herein has a polydispersity of about 2.0. In one embodiment, the SPF of the composition disclosed herein has a polydispersity of about 2.1. In one embodiment, the SPF of the composition disclosed herein has a polydispersity of about 2.2. In one embodiment, the composition of the present disclosure has an SPF of about 2.3 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 2.4 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 2.5 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 2.6 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 2.7 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 2.8 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 2.9 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 3.0 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 3.1 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 3.2 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 3.3 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 3.4 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 3.5 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 3.6 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 3.7 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 3.8 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 3.9 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 4.0 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 4.1 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 4.2 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 4.3 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 4.4 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 4.5 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 4.6 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 4.7 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 4.8 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 4.9 polydispersity. In one embodiment, the composition of the present disclosure has an SPF of about 5.0 polydispersity.

In some embodiments, in the compositions described herein having a combination of low, medium, and/or high molecular weight SPFs, such low, medium, and/or high molecular weight SPFs may have the same or different polydispersity.

Silk heart protein fragments

Methods for preparing filamentin or filamentin fragments and their applications in various fields are known and described, for example, in U.S. Patents 9,187,538, 9,511,012, 9,517,191, 9,522,107, 9,522,108, 9,545,369 and 10,166,177, 10,287,728 and 10,301,768, all of which are incorporated herein by reference in their entirety. Raw silk from the silkworm (Bombyx mori) consists of two main proteins: filamentin (approximately 75%) and sericin (approximately 25%). Fiberin is a fibrous protein with a semi-crystalline structure that provides stiffness and strength. As used herein, the term "filamentin" refers to the fiber of the silkworm cocoon having a weight-average molecular weight of approximately 370,000 Da. Coarse silkworm fiber consists of double threads of filamentin. The adhesive substance that binds these bifidus together is sericin. Sericin consists of a heavy chain (H chain) with a weight-average molecular weight of approximately 350,000 Da and a light chain (L chain) with a weight-average molecular weight of approximately 25,000 Da. Sericin is an amphiphilic polymer with large hydrophobic domains (of high molecular weight) occupying the major components of the polymer. The hydrophobic regions are interrupted by small hydrophilic spacers, and the N- and C-termini of the chains are also highly hydrophilic. The hydrophobic domains of the H chain contain repeating hexapeptide sequences of Gly-Ala-Gly-Ala-Gly-Ser and repeating dipeptides of Gly-Ala/Ser/Tyr, which can form stable antiparallel-sheet microcrystals. The L chain has a non-repeating amino acid sequence, making it more hydrophilic and relatively flexible. The alternation of hydrophilic (Tyr, Ser) and hydrophobic (Gly, Ala) segments in the sericin molecule enables self-assembly of the sericin molecule.

This document provides methods for producing pure and highly scalable solutions of silk core protein fragment mixtures suitable for a wide range of applications across multiple industries. While not intended to be bound by any particular theory, it is believed that these methods are equally applicable to the fragmentation of any SPFs described herein, including but not limited to recombinant silk proteins and the fragmentation of silk-like or silk core protein fragments.

The term "silk core protein" as used herein includes silkworm silk core protein and insect or spider silk protein. In one embodiment, the silk core protein is obtained from silkworms. Raw silk from silkworms consists of two main proteins: silk core protein (approximately 75%) and sericin (approximately 25%). Silk core protein is a fibrous protein with a semi-crystalline structure that provides stiffness and strength. The term "silk core protein" as used herein refers to the fiber of the silkworm cocoon having a weight-average molecular weight of approximately 370,000 Da. Converting these insoluble silk core protein fibrils into water-soluble silk core protein fragments requires the addition of concentrated neutral salts (e.g., 8-10M lithium bromide), which interfere with the intermolecular and intramolecular ionic and hydrogen bonds that originally make silk core protein insoluble in water. Methods for preparing filamentin fragments and/or compositions thereof are known and described, for example, in U.S. Patents 9,187,538, 9,511,012, 9,517,191, 9,522,107, 9,522,108, 9,545,369, and 10,166,177.

Raw silk cocoons from silkworms are cut into fragments. The cocoon fragments are treated in an aqueous solution of _Na₂CO₃ at approximately ₁₀₀ °C for about 60 minutes to remove sericin (degumming). The volume of water used is approximately 0.4 times the weight of the raw silk, and the amount _{of Na₂CO₃} is approximately 0.848 times the weight of the raw silk cocoon fragments. The resulting degummed cocoon fragments are rinsed three times with deionized water at approximately 60°C (20 minutes each time). The volume of rinsing water for each cycle is 0.2 L x the weight of the raw silk cocoon fragments. Excess water is removed from the degummed cocoon fragments. After the deionized water washing step, the wet degummed cocoon fragments are dried at room temperature. The degummed cocoon fragments are mixed with a LiBr solution, and the mixture is heated to approximately 100°C. The heated mixture is placed in a drying oven and heated at approximately 100°C for about 60 minutes to achieve complete dissolution of the natural silk fibroin. The resulting silk protein solution was filtered through deionized water and dialyzed for 72 hours using tangential flow filtration (TFF) and a 10 kDa membrane. The resulting aqueous silk protein solution had a concentration of approximately 8.5% by weight. This 8.5% silk solution was then diluted with water to produce a 1.0% w/v silk solution. The TFF could then be used to further concentrate the pure silk solution to a concentration of 20.0% w/w silk/water.

Fiber dialysis, involving a series of water replacements, is a manual and time-intensive process that can be accelerated by altering certain parameters, such as diluting the fiber solution before dialysis. The dialysis process can be scaled up using semi-automated equipment, such as tangential flow filtration systems.

In some embodiments, the silk solution is prepared under various preparation conditions, such as 90°C for 30 minutes, 90°C for 60 minutes, 100°C for 30 minutes, and 100°C for 60 minutes. Briefly, 9.3M LiBr is prepared and allowed to stand at room temperature for at least 30 minutes. 5 mL of LiBr solution is added to 1.25 g of silk and placed in a 60°C oven. Samples are taken from each group at 4, 6, 8, 12, 24, 168, and 192 hours.

In some embodiments, the silk solution is prepared under various preparation conditions, such as 90°C for 30 minutes, 90°C for 60 minutes, 100°C for 30 minutes, and 100°C for 60 minutes. In short, a 9.3M LiBr solution is heated to one of four temperatures: 60°C, 80°C, 100°C, or boiling. 5 mL of hot LiBr solution is added to 1.25 g of silk and placed in a 60°C oven. Samples are removed from each group at 1, 4, and 6 hours.

In some embodiments, the silk solution is prepared under various preparation conditions, such as using four different silk extraction combinations: 90°C for 30 minutes, 90°C for 60 minutes, 100°C for 30 minutes, and 100°C for 60 minutes. In short, the 9.3M LiBr solution is heated to one of four temperatures: 60°C, 80°C, 100°C, or boiling. 5 mL of the hot LiBr solution is added to 1.25 g of silk and placed in an oven at the same temperature as LiBr. Samples are removed from each group at 1, 4, and 6 hours. 1 mL of each sample is added to 7.5 mL of 9.3M LiBr and refrigerated for viscosity testing.

In some embodiments, SPF is obtained by dissolving raw, undegummed, partially degummed, or degummed silkworm fibers with a neutral lithium bromide salt. The raw silk is processed under selected temperatures and other conditions to remove any sericin and achieve the desired weight-average molecular weight ( _MW ) and polydispersity (PD) of the fragment mixture. The choice of process parameters can be varied to achieve different final silk fibroin fragment properties depending on the intended use. The resulting final fragment solution is a mixture of silk fibroin fragments and water with parts per million (ppm) to undetectable levels of process contaminants, levels acceptable in the pharmaceutical, medical, and consumer eye care markets. The concentration, size, and polydispersity of the SPF can be further modified according to the desired application and performance requirements.

Figure 1 is a flowchart illustrating various embodiments for producing pure silk core protein fragments (SPF) of this disclosure. It should be understood that not all illustrated steps are necessary for preparing all silk solutions of this disclosure. As shown in Figure 2, step A, cocoons (heat-treated or untreated), silk fibers, silk powder, spider silk, or reconstituted spider silk can be used as the silk source. If starting with raw silk cocoons from silkworms, the cocoons can be cut into small pieces, such as pieces of approximately equal size, step B1. Then, in step C1a, the raw silk is extracted and rinsed to remove any sericin. This produces raw silk that _is essentially sericin-free. In one embodiment, water is heated to a temperature of 84°C to 100°C (ideally boiling), and then _Na₂CO₃ (sodium carbonate) is added to the boiling water until _{the Na₂CO₃} is completely dissolved. The raw silk is added to the boiling water/ _Na₂CO₃ (100° _C ) and immersed for approximately 15–90 minutes, where a longer boiling time produces smaller silk protein fragments. In one embodiment, the water volume is equal to approximately 0.4 times the weight of the raw silk, and the _{Na₂CO₃ volume} is equal to approximately 0.848 times the weight of the raw silk. In another embodiment, the water volume is equal to 0.1 times the weight of the raw silk, and _{the Na₂CO₃} volume is maintained at 2.12 g/L.

Subsequently, the water- _{dissolved Na₂CO₃} solution is drained, and excess water/ _Na₂CO₃ is removed from the sericin fibers (e.g., by hand to form the sericin extract into rings, using a rotating circulation machine _, etc.). The resulting sericin extract is rinsed with warm to hot water, typically in the temperature range of about 40°C to about 80°C, to remove any residual adsorbed sericin or contaminants, changing the water volume at least once (repeated as needed). The resulting sericin extract is essentially sericin-free. In one embodiment, the resulting sericin extract is rinsed with water at a temperature of about 60°C. In one embodiment, the volume of rinsing water per cycle is equal to 0.1 L to 0.2 L × the weight of the raw silk. It may be advantageous to agitate, tumble, or circulate the rinsing water to maximize the rinsing effect. After rinsing, excess water is removed from the extracted sericin fibers (e.g., by hand or by machine to squeeze the sericin extract). Alternatively, methods known to those skilled in the art, such as pressure, temperature, or other reagents or combinations thereof, can be used for sericin extraction. Alternatively, the silk glands (100% sericin-free silk protein) can be extracted directly from the insect. This will yield sericin-free liquid silk protein with no alteration to the protein structure.

The extracted silk core fibers are then completely dried. Once dried, the extracted silk core fibers are dissolved in a solvent added to the silk core fibers at a temperature from ambient to boiling point, step C1b. In one embodiment, the solvent is a lithium bromide (LiBr) solution (LiBr has a boiling point of 140°C). Alternatively, the extracted silk core fibers are not dried but placed wet in a solvent; the solvent concentration can then be varied to achieve a concentration similar to that when the dried fibers are added to the solvent. The final concentration of the LiBr solvent can be in the range of 0.1M to 9.3M. Complete dissolution of the extracted silk core fibers can be achieved by varying the treatment time and temperature as well as the concentration of the dissolving solvent. Other solvents can be used, including but not limited to phosphate, calcium nitrate, calcium chloride solution, or other concentrated aqueous solutions of inorganic salts. To ensure complete dissolution, the silk fibers should be completely immersed in the heated solvent solution and then maintained at a temperature of about 60°C to about 140°C for 1–168 hours. In one embodiment, the silk fibers should be completely immersed in the solvent solution and then placed in a drying oven at a temperature of about 100°C for about 1 hour.

The temperature at which silk core protein extract is added to the LiBr solution (and vice versa) affects the time required for complete dissolution of the silk core protein, as well as the resulting molecular weight and polydispersity of the SPF mixture solution. In one embodiment, the silk solvent solution concentration is less than or equal to 20% w/v, and stirring during introduction or dissolution can be used to promote dissolution at different temperatures and concentrations. The temperature of the LiBr solution provides control over the molecular weight and polydispersity of the resulting silk core protein fragment mixture. In one embodiment, higher temperatures dissolve the silk more quickly to provide enhanced process scalability and large-scale production of the silk solution. In one embodiment, using a LiBr solution heated to 80°C–140°C reduces the time required to achieve complete dissolution in an oven. Variations in time and dissolution solvent at temperatures of 60°C or above will alter and control the molecular weight (MW) and polydispersity of the SPF mixture solution formed from natural silk core protein at its original molecular weight.

Alternatively, extraction can be bypassed by placing the entire cocoon directly in a solvent, such as LiBr, step B2. This requires subsequent filtration of the silk and solvent solution from the silk particles and removal of sericin using methods known in the art for separating hydrophobic and hydrophilic proteins (such as column separation and/or chromatography, ion exchange, chemical precipitation with salt and/or pH, and/or enzymatic digestion and filtration or extraction), all of which are common examples of standard protein separation methods and not limitations, step C2. Alternatively, extraction can be bypassed by placing the untreated, untreated cocoon, after removing the silkworm particles, in a solvent, such as LiBr. The above methods can be used for sericin separation, with the advantage that the untreated cocoon contains significantly less insect debris.

The dissolving solvent can be removed from the resulting dissolved silk protein fragment solution by dialysis relative to a certain volume of water, step E1. Pre-filtration prior to dialysis helps remove any debris (i.e., silkworm residue) from the silk and LiBr solution, step D. In one example, a 0.1% to 1.0% silk-LiBr solution is filtered at a flow rate of 200-300 mL/min using a 3 μm or 5 μm filter before dialysis and, if necessary, concentration. The methods disclosed herein, as described above, utilize time and/or temperature to reduce the concentration from 9.3 M LiBr to the range of 0.1 M to 9.3 M to facilitate filtration and downstream dialysis, particularly when considering establishing a scalable process. Alternatively, without using additional time or temperature, the 9.3 M LiBr-silk protein fragment solution can be diluted with water to facilitate debris filtration and dialysis. Dissolution at the desired time and temperature results in a translucent, particle-free, room-temperature-stable silk protein fragment-LiBr solution with known MW and polydispersity. It is advantageous to change the dialysis water periodically until the solvent is removed (e.g., change the water after 1 hour, 4 hours, and then every 12 hours, for a total of 6 water changes). The total number of water changes can be varied based on the resulting concentration of the solvent used for silk protein dissolution and fragmentation. After dialysis, the final silk solution can be further filtered to remove any residual debris (i.e., silkworm residue).

Alternatively, tangential flow filtration (TFF), a rapid and efficient method for separating and purifying biomolecules, can be used to remove solvent from the resulting dissolved silk protein solution, step E2. TFF provides a high-purity aqueous solution of silk protein fragments and ensures that the method can be scalable to produce large quantities of solutions in a controlled and reproducible manner. The silk-LiBr solution can be diluted prior to TFF (from 20% to 0.1% silk in water or LiBr). Pre-filtration as described above prior to TFF treatment maintains filtration efficiency and potentially avoids the formation of a silk gel boundary layer on the filter surface due to the presence of debris particles. Pre-filtration prior to TFF also helps remove any residual debris (i.e., silkworm residue) from the silk and LiBr solution, which may cause spontaneous or prolonged gelation of the resulting water-only solution, step D. Recycled or single-pass TFF can be used to produce an aqueous-silk protein fragment solution of 0.1% to 30.0% silk (more preferably, 0.1%–6.0% silk). Depending on the desired concentration, molecular weight, and polydispersity of the silk protein fragment mixture in solution, TFF membranes of different cutoff sizes may be required. For example, for silk solutions of different molecular weights prepared by varying the length of the extraction boiling time or the time and temperature in the dissolving solvent (e.g., LiBr), membranes of 1–100 kDa may be necessary. In one embodiment, a 5 or 10 kDa TFF membrane is used to purify the silk protein fragment mixture solution and produce the final desired silk-to-water ratio. After removal of the dissolving solvent (e.g., LiBr), the solution can also be concentrated using single-pass TFF, TFF, and other methods known in the art, such as falling film evaporators (resulting in desired concentrations of 0.1% to 30% silk). This can be used as an alternative to standard HFIP concentration methods known in the art for preparing water-based solutions. Larger pore membranes can also be used to filter out small silk protein fragments and produce solutions of higher molecular weight silk with and/or without narrow polydispersity values.

Determination methods for detecting LiBr and _Na₂CO₃ can be performed using an HPLC system equipped with an evaporative light scattering detector (ELSD). Calculations are performed by linear regression of _the resulting peak areas of the analytes plotted relative to concentration. Multiple samples of many formulations disclosed herein are used for sample preparation and analysis. Typically, four samples of different formulations are weighed directly into 10 mL volumetric flasks. The samples are suspended in 5 mL of 20 mM ammonium formate (pH 3.0) and maintained at 2 to 8 °C for 2 hours, occasionally agitated to extract the analytes from the membrane. After 2 hours, the solution is diluted with 20 mM ammonium formate (pH 3.0). The sample solution from the volumetric flasks is transferred to an HPLC vial and injected into an HPLC-ELSD system to estimate sodium carbonate and lithium bromide.

The analytical method developed for the quantification of _Na₂CO₃ and LiBr in silk _fibroin formulations was found to be linear in the range of 10–165 μg/mL, with an RSD of 2% for injection precision and 1% for area, and retention times of 0.38% and 0.19% for sodium carbonate and lithium bromide, respectively. This analytical method can be used for the quantitative determination of sodium carbonate and lithium bromide in silk fibroin formulations.

Figure 2 is a flowchart showing various parameters that can be modified during the process of producing the silk protein fragment solutions of this disclosure, specifically during the extraction and dissolution steps. The selected method parameters can be varied to achieve different final solution properties, such as molecular weight and polydispersity, depending on the intended use. It should be understood that not all illustrated steps are necessary for preparing all silk solutions of this disclosure.

In one embodiment, a silk fibroin fragment solution suitable for diverse applications is prepared according to the following steps: silk cocoon fragments are formed from silkworms; the fragments are extracted in an _{aqueous Na₂CO₃} solution at approximately 100°C for approximately 60 minutes, wherein the water volume is equal to approximately 0.4 × the weight of the raw silk and the _Na₂CO₃ solution is... The following steps are performed: _1. A silk core protein extract is prepared by rinsing approximately 0.848 × fragment weight in a volume of rinsing water at approximately 60°C three times, each rinse lasting approximately 20 minutes, with each cycle using approximately 0.2 L × fragment weight of rinsing water. 2. Excess water is removed from the silk core protein extract. 3. The silk core protein extract is dried. 4. The dried silk core protein extract is dissolved in a LiBr solution, wherein the LiBr solution is first heated to approximately 100°C to produce a silk-LiBr solution and held. 5. The silk-LiBr solution is placed in a drying oven at approximately 100°C for approximately 60 minutes to achieve complete dissolution of the natural silk protein structure and further fragmentation into a mixture with the desired molecular weight and polydispersity. 6. The solution is filtered to remove any residual debris from the silkworm. 7. The solution is diluted with water to obtain a 1.0 wt% silk solution. 8. The solvent is removed from the solution using tangential flow filtration (TFF). In one embodiment, a 10 kDa membrane is used to purify the silk solution and produce the desired final silk-to-water ratio. TFF can then be used to further concentrate the silk solution to a concentration of 2.0% by weight of silk in water.

While it is undesirable to be bound by any particular theory, varying the extraction (i.e., time and temperature), LiBr (i.e., the temperature of the LiBr solution when added to the silk core extract (or vice versa), and dissolution (i.e., time and temperature) parameters yields solvent-silk solutions with different viscosities, homogeneity, and colors. Similarly, it is undesirable to be bound by any particular theory, but increasing the extraction temperature, extending the extraction time, using a higher temperature LiBr solution initially and over time during silk dissolution, and increasing the time at a given temperature (e.g., in an oven or alternative heat source as shown here) all result in solvent-silk solutions with lower viscosity and greater homogeneity.

The extraction step can be performed in a larger container, such as an industrial washer that can maintain temperatures between 60°C and 100°C or higher. The rinsing step can also be performed in an industrial washer to eliminate manual rinsing cycles. Dissolution of the silk in the LiBr solution can be carried out in a container other than a convection oven, such as a stirred tank reactor. Silk dialysis via a series of water replacements is a manual and time-intensive process, which can be accelerated by changing certain parameters, such as diluting the silk solution before dialysis. The dialysis process can be scaled up using semi-automated equipment, such as tangential flow filtration systems.

Varying the extraction (i.e., time and temperature), LiBr (i.e., the temperature of the LiBr solution when added to the silk core extract (or vice versa), and dissolution (i.e., time and temperature) parameters yields solvent-silk solutions with varying viscosities, homogeneity, and colors. Increasing the extraction temperature, extending the extraction time, using a higher temperature LiBr solution initially and over time during silk dissolution, and increasing the time at a given temperature (e.g., in an oven or alternative heat source as shown here) all result in solvent-silk solutions with lower viscosity and greater homogeneity. Although almost all parameters yield viable silk solutions, methods that achieve complete dissolution in less than 4 to 6 hours are preferred for process scaling.

In one embodiment, a solution of silk core protein fragments having a weight-average molecular weight selected from about 6 kDa to about 17 kDa is prepared according to the following steps: degumming the silk source by adding it to a boiling (100°C) aqueous sodium carbonate solution for about 30 minutes to about 60 minutes; removing sericin from the solution to produce a silk core protein extract containing an undetectable amount of sericin; draining the solution from the silk core protein extract; dissolving the silk core protein extract in a lithium bromide solution having an initial temperature of about 60°C to about 140°C when the silk core protein extract is placed in the lithium bromide solution; maintaining the silk core protein-lithium bromide solution in an oven at a temperature of about 140°C for a period of up to 1 hour; removing lithium bromide from the silk core protein extract; and preparing an aqueous solution of silk protein fragments comprising fragments having a weight-average molecular weight selected from about 6 kDa to about 17 kDa and a polydispersity of 1 to about 5 or about 1.5 to about 3.0. The method may further include drying the silk core protein extract prior to the dissolution step. The aqueous solution of the silk core protein fragment may contain less than 300 ppm of lithium bromide residue, as determined by high-performance liquid chromatography (HPLC) for lithium bromide. The aqueous solution of the silk core protein fragment may contain less than 100 ppm of sodium carbonate residue, as determined by HPLC for sodium carbonate. The aqueous solution of the silk core protein fragment may be lyophilized. In some embodiments, the silk core protein fragment solution may be further processed into various forms, including gels, powders, and nanofibers.

In one embodiment, a solution having sericin fragments with a weight-average molecular weight selected from about 17 kDa to about 39 kDa is prepared according to the following steps: adding a sericin source to a boiling (100°C) aqueous sodium carbonate solution for a treatment time of about 30 minutes to about 60 minutes to result in degumming; removing sericin from the solution to produce a sericin extract containing undetectable levels of sericin; draining the solution from the sericin extract; and dissolving the sericin extract in a lithium bromide solution having an initial temperature of about 80°C to about 140°C when the sericin extract is placed in the lithium bromide solution. Temperature; holding the silk core protein-lithium bromide solution in a drying oven at a temperature of about 60°C to about 100°C for a period of up to 1 hour; removing lithium bromide from the silk core protein extract; and preparing an aqueous solution of silk core protein fragments, wherein the aqueous solution of silk core protein fragments contains about 10 ppm to about 300 ppm of lithium bromide residue, wherein the aqueous solution of silk core protein fragments contains about 10 ppm to about 100 ppm of sodium carbonate residue, and wherein the aqueous solution of silk core protein fragments contains fragments having a weight-average molecular weight selected from about 17 kDa to about 39 kDa and a polydispersity of 1 to about 5 or about 1.5 to about 3.0. The method may further include drying the silk core protein extract prior to the dissolution step. The aqueous solution of silk core protein fragments may contain less than 300 ppm of lithium bromide residue as determined by high performance liquid chromatography (HPLC). The aqueous solution of silk core protein fragments may contain less than 100 ppm of sodium carbonate residue as determined by HPLC.

In some embodiments, a method for preparing an aqueous solution of silk core protein fragments having an average weight-average molecular weight selected from about 6 kDa to about 17 kDa includes the following steps: degumming the silk source by adding it to a boiling (100°C) aqueous sodium carbonate solution for a treatment time of about 30 minutes to about 60 minutes; removing sericin from the solution to produce a silk core protein extract containing undetectable levels of sericin; draining the solution from the silk core protein extract; dissolving the silk core protein extract in a lithium bromide solution having an initial temperature of about 60°C to about 140°C when the silk core protein extract is placed in the lithium bromide solution; maintaining the silk core protein-lithium bromide solution in an oven at a temperature of about 140°C for at least 1 hour; removing lithium bromide from the silk core protein extract; and preparing an aqueous solution of silk core protein fragments comprising fragments having an average weight-average molecular weight selected from about 6 kDa to about 17 kDa and a polydispersity of 1 to about 5 or about 1.5 to about 3.0. The method may further include drying the silk core protein extract prior to the dissolution step. The aqueous solution of the pure silk-core protein fragment may contain less than 300 ppm of lithium bromide residue, as determined by high-performance liquid chromatography (HPLC) for lithium bromide. The aqueous solution of the pure silk-core protein fragment may contain less than 100 ppm of sodium carbonate residue, as determined by HPLC for sodium carbonate. The method may further include adding a therapeutic agent to the aqueous solution of the pure silk-core protein fragment. The method may further include adding a molecule selected from antioxidants or enzymes to the aqueous solution of the pure silk-core protein fragment. The method may further include adding a vitamin to the aqueous solution of the pure silk-core protein fragment. The vitamin may be vitamin C or a derivative thereof. The aqueous solution of the pure silk-core protein fragment may be lyophilized. The method may further include adding an α-hydroxy acid to the aqueous solution of the pure silk-core protein fragment. The α-hydroxy acid may be selected from glycolic acid, lactic acid, tartaric acid, and citric acid. The method may further include adding hyaluronic acid or a salt thereof to the aqueous solution of the pure silk-core protein fragment at a concentration of about 0.5% to about 10.0%. The method may further include adding at least one of zinc oxide or titanium dioxide. A membrane can be prepared from an aqueous solution of pure silk core protein fragments produced by this method. The membrane may contain about 1.0 wt% to about 50.0 wt% vitamin C or a derivative thereof. The membrane may have a water content of about 2.0 wt% to about 20.0 wt%. The membrane may contain about 30.0 wt% to about 99.5 wt% pure silk core protein fragments. A gel can be prepared from an aqueous solution of pure silk core protein fragments produced by this method. The gel may contain about 0.5 wt% to about 20.0 wt% vitamin C or a derivative thereof. The gel may have a silk content of at least 2% and a vitamin content of at least 20%.

In some embodiments, a method for preparing an aqueous solution of sericin fragments having an average weight-average molecular weight selected from about 17 kDa to about 39 kDa includes the following steps: adding a sericin source to a boiling (100°C) aqueous sodium carbonate solution for a treatment time of about 30 minutes to about 60 minutes to result in degumming; removing sericin from the solution to produce a sericin extract containing undetectable levels of sericin; draining the solution from the sericin extract; and dissolving the sericin extract in a lithium bromide solution having a temperature of about 80°C to about 140°C when the sericin extract is placed in the lithium bromide solution. The method involves: setting the initial temperature; maintaining the silk protein-lithium bromide solution in a drying oven at a temperature of about 60°C to about 100°C for at least 1 hour; removing lithium bromide from the silk protein extract; and preparing an aqueous solution of pure silk protein fragments, wherein the aqueous solution of pure silk protein fragments contains about 10 ppm to about 300 ppm of lithium bromide residue, wherein the aqueous solution of silk protein fragments contains about 10 ppm to about 100 ppm of sodium carbonate residue, and wherein the aqueous solution of pure silk protein fragments contains fragments having an average weight-average molecular weight selected from about 17 kDa to about 39 kDa and a polydispersity of 1 to about 5 or about 1.5 to about 3.0. The method may further include drying the silk protein extract prior to the dissolution step. The aqueous solution of pure silk protein fragments may contain less than 300 ppm of lithium bromide residue as determined by high performance liquid chromatography (HPLC). The aqueous solution of pure silk protein fragments may contain less than 100 ppm of sodium carbonate residue as determined by HPLC. The method may further include adding a therapeutic agent to an aqueous solution of pure silk-core protein fragments. The method may further include adding a molecule selected from antioxidants or enzymes to the aqueous solution of pure silk-core protein fragments. The method may further include adding a vitamin to the aqueous solution of pure silk-core protein fragments. The vitamin may be vitamin C or a derivative thereof. The aqueous solution of pure silk-core protein fragments may be lyophilized. The method may further include adding an α-hydroxy acid to the aqueous solution of pure silk-core protein fragments. The α-hydroxy acid may be selected from glycolic acid, lactic acid, tartaric acid, and citric acid. The method may further include adding hyaluronic acid or a salt thereof to the aqueous solution of pure silk-core protein fragments at a concentration of about 0.5% to about 10.0%. The method may further include adding at least one of zinc oxide or titanium dioxide. A membrane may be prepared from the aqueous solution of pure silk-core protein fragments prepared by this method. The membrane may contain about 1.0% by weight to about 50.0% by weight of vitamin C or a derivative thereof. The membrane may have a water content of about 2.0% by weight to about 20.0% by weight. The membrane may contain about 30.0% to about 99.5% by weight of pure silk core protein fragments. A gel may be prepared from an aqueous solution of the pure silk core protein fragments prepared by this method. The gel may contain about 0.5% to about 20.0% by weight of vitamin C or a derivative thereof. The gel may have a silk content of at least 2% and a vitamin content of at least 20%.

In one embodiment, a solution having sericin fragments with a weight-average molecular weight selected from about 39 kDa to about 80 kDa is prepared according to the following steps: adding a sericin source to a boiling (100°C) aqueous sodium carbonate solution for about 30 minutes to cause degumming; removing sericin from the solution to produce a sericin extract containing undetectable levels of sericin; draining the solution from the sericin extract; and dissolving the sericin extract in a lithium bromide solution having a temperature of about 80°C to about 140°C when the sericin extract is placed... The method includes: an initial temperature in a lithium bromide solution; maintaining the silk-core protein-lithium bromide solution in a drying oven at a temperature of about 60°C to about 100°C for up to 1 hour; removing lithium bromide from the silk-core protein extract; and preparing an aqueous solution of silk-core protein fragments, wherein the aqueous solution of silk-core protein fragments contains about 10 ppm to about 300 ppm of lithium bromide residue, about 10 ppm to about 100 ppm of sodium carbonate residue, and fragments having a weight-average molecular weight selected from about 39 kDa to about 80 kDa and a polydispersity of 1 to about 5 or about 1.5 to about 3.0. The method may further include drying the silk-core protein extract prior to the dissolution step. The aqueous solution of silk-core protein fragments may contain less than 300 ppm of lithium bromide residue as determined by high-performance liquid chromatography (HPLC). The aqueous solution of silk-core protein fragments may contain less than 100 ppm of sodium carbonate residue as determined by HPLC. In some embodiments, the method may further include adding an active agent (e.g., a therapeutic agent) to the aqueous solution of pure silk-core protein fragments. The method may further include adding an activator selected from antioxidants or enzymes to an aqueous solution of pure silk protein fragments. The method may further include adding a vitamin to the aqueous solution of pure silk protein fragments. The vitamin may be vitamin C or a derivative thereof. The aqueous solution of pure silk protein fragments may be lyophilized. The method may further include adding an α-hydroxy acid to the aqueous solution of pure silk protein fragments. The α-hydroxy acid may be selected from glycolic acid, lactic acid, tartaric acid, and citric acid. The method may further include adding hyaluronic acid or a salt thereof to the aqueous solution of pure silk protein fragments at a concentration of about 0.5% to about 10.0%. A membrane may be prepared from the aqueous solution of pure silk protein fragments prepared by this method. The membrane may contain about 1.0 wt% to about 50.0 wt% vitamin C or a derivative thereof. The membrane may have a water content of about 2.0 wt% to about 20.0 wt%. The membrane may contain about 30.0 wt% to about 99.5 wt% pure silk protein fragments. A gel may be prepared from the aqueous solution of pure silk protein fragments prepared by this method. The gel may contain about 0.5% by weight to about 20.0% by weight of vitamin C or its derivatives. The gel may have at least 2% by weight of silk content and at least 20% by weight of vitamin content.

The molecular weight of silk protein fragments can be controlled based on specific parameters used in the extraction step, including extraction time and temperature; specific parameters used in the dissolution step, including the LiBr temperature when immersing the silk in lithium bromide and the time the solution is held at a specific temperature; and specific parameters used in the filtration step. By controlling the process parameters using the disclosed method, silk protein fragment solutions with polydispersity equal to or less than 2.5 at various molecular weights selected from 5 kDa to 200 kDa or 10 kDa to 80 kDa can be prepared. By changing the process parameters to obtain silk solutions with different molecular weights, a final product of a fragment mixture with a desired range of polydispersity equal to or less than 2.5 can be obtained based on the desired performance requirements. For example, higher molecular weight silk membranes containing ophthalmic drugs can have a controlled slow release rate compared to lower molecular weight membranes, making them ideal for use as a presentation carrier in eye care products. Additionally, silk protein fragment solutions with polydispersity greater than 2.5 can be obtained. Furthermore, two solutions with different average molecular weights and polydispersities can be mixed to produce combined solutions. Alternatively, liquid silk glands (100% sericin-free silk protein) extracted directly from the insect can be used in combination with any filamentin fragment solution of this disclosure. The molecular weight of the pure filamentin fragment composition was determined using high-performance liquid chromatography (HPLC) with a refractive index detector (RID). Polydispersity was calculated using Cirrus GPConline GPC/SEC software version 3.3 (Agilent).

Differences in processing parameters can result in regenerated fibroin with varying molecular weights and peptide chain size distributions (polydispersity, PD). This, in turn, affects the properties of regenerated fibroin, including mechanical strength and water solubility.

Parameters were varied during the processing of raw silk cocoons into a silk solution. These variations affected the molecular weight (MW) of the resulting silk solution. The manipulated parameters included (i) extraction time and temperature, (ii) LiBr temperature, (iii) dissolution oven temperature, and (iv) dissolution time. Experiments were conducted to determine the effect of varying the extraction time. Tables A-G summarize the results. The following is a summary:

A 30-minute extraction time for sericin results in a larger molecular weight compared to a 60-minute extraction time.

-Molecular weight decreases with time spent in the oven.

-140℃ LiBr and an oven caused the lower limit of the confidence interval to be below the molecular weight of 9500 Da.

– Extraction of undigested silk at 1 hour and 4 hours time points within 30 minutes.

– Extraction at 30 minutes resulted in a significantly higher molecular weight at the 1-hour time point, with a lower limit of the confidence interval of 35,000 Da.

– The range of molecular weights reached at the upper limit of the confidence interval is 18,000 to 216,000 Da (important for providing solutions with a specified upper limit).

Experiments were conducted to determine the effect of changing the extraction temperature. Table G summarizes the results. The following is a summary:

– Extraction of sericin at 90°C resulted in a higher molecular weight (MW) than extraction at 100°C.

Both -90°C and 100°C showed a decrease in MW with time spent in the oven.

Experiments were conducted to determine the effect of changing the temperature of lithium bromide (LiBr) when added to the wire. Table H-I summarizes the results. The following is a summary:

– No effect on molecular weight or confidence interval (all CI ~ 10500-6500 Da)

Studies have shown that, since most of the substances are filaments at room temperature, when LiBr is added and begins to dissolve, the dissolution temperature of the LiBr-filaments rapidly drops below the original LiBr temperature.

Experiments were conducted to determine the effect of oven/melting temperature. Table J-N summarizes the results. The following is a summary:

– The effect of oven temperature on filaments extracted at 60 minutes is less than that on filaments extracted at 30 minutes. Not wanting to be bound by theory, it is believed that filaments extracted at 30 minutes undergo less degradation during extraction, and therefore oven temperature has a greater impact on the larger MW (measuring capacity) and less degraded portions of the filaments.

– For the 60°C vs. 140°C oven, the fibers extracted for 30 minutes showed a very significant effect of lower MW at the higher oven temperature, while the fibers extracted for 60 minutes had a much smaller effect.

The -140℃ oven results in a lower limit of the confidence interval of ~6000Da.

Raw silk cocoons from silkworms are cut into pieces. The raw silk cocoon pieces are boiled in an aqueous solution _{of Na₂CO₃} (approximately 100°C) for approximately 30 to 60 minutes to remove sericin (degumming). The volume of water used is approximately 0.4 times the weight of the raw silk, and the amount _{of Na₂CO₃} is approximately 0.848 times the weight of the raw silk cocoon pieces. The resulting degummed silk cocoon pieces are rinsed three times with deionized water at approximately 60°C (20 minutes each time). The volume of rinsing water for each cycle is 0.2 L x the weight of the raw silk cocoon pieces. Excess water is removed from the degummed silk cocoon pieces. After the deionized water washing step, the wet degummed silk cocoon pieces are dried at room temperature. The degummed silk cocoon pieces are mixed with a LiBr solution, and the mixture is heated to approximately 100°C. The heated mixture is placed in a drying oven and heated at approximately 60°C to approximately 140°C for approximately 60 minutes to achieve complete dissolution of the natural silk fibroin. The resulting solution was cooled to room temperature and then dialyzed using a 3,500 Da MWCO membrane to remove LiBr salts. Multiple exchanges were performed in deionized water until the Br⁻ ^ion concentration in the hydrolyzed silk core protein solution was less than 1 ppm, as read on an Oakton Bromide ( ^Br⁻ ) double-junction ion-selective electrode.

The resulting filamentin aqueous solution has a concentration of about 8.0% w/v and contains pure filamentin fragments having an average weight-average molecular weight selected from about 6 kDa to about 16 kDa, about 17 kDa to about 39 kDa, and about 39 kDa to about 80 kDa, and a polydispersity of about 1.5 to about 3.0. The 8.0% w/v solution is diluted with deionized water to provide 1.0% w/v, 2.0% w/v, 3.0% w/v, 4.0% w/v, and 5.0% w/v solutions, based on the coating solution.

Various filament concentration percentages (%) were prepared using tangential flow filtration (TFF). In all cases, a 1% filament solution was used as the input feed. A starting volume of 750–18,000 mL of 1% filament solution was used. The solution was percolated in the TFF to remove lithium bromide. Once below the specified residual LiBr level, the solution underwent ultrafiltration to increase the concentration by removing water. See the examples below.

Six (6) filament solutions were used in the standard filament structure, and the results are as follows:

Solution #1 had a filament concentration of 5.9 wt%, an average molecular weight of 19.8 kDa, and a PDI of 2.2 (prepared by boiling for 60 minutes and dissolving in LiBr at 100°C for 1 hour).

The concentration of the filament in solution #2 was 6.4% by weight (prepared by boiling for 30 minutes and dissolving in LiBr at 60°C for 4 hours).

The concentration of the filament in solution #3 was 6.17% by weight (prepared by boiling for 30 minutes and dissolving in LiBr at 100°C for 1 hour).

Solution #4 had a silk concentration of 7.30% by weight: A 7.30% silk solution was produced by extracting 100g of silk cocoons per batch over 30 minutes. The extracted silk fibers were then dissolved in 9.3M LiBr at 100°C for 1 hour in a 100°C oven. 100g of silk fibers were dissolved per batch to produce 20% silk in LiBr. The silk dissolved in LiBr was then diluted to 1% silk and filtered through a 5μm filter to remove large debris. 15,500mL of the 1% filtered silk solution was used as the starting volume/percolation volume for TFF. Once LiBr was removed, the solution was ultrafiltered to approximately 1300mL. 1262mL of 7.30% silk was then collected. Water was added to the feed to aid in the removal of residual solution, and then 547mL of 3.91% silk was collected.

Solution #5 had a silk concentration of 6.44% by weight: A 6.44% by weight silk solution was produced by extracting batches of 25, 33, 50, 75, and 100 g silk cocoons over 60 minutes. The extracted silk fibers were then dissolved in 9.3 M LiBr at 100°C for 1 hour in a 100°C oven. 35, 42, 50, and 71 g silk fibers were dissolved in each batch to prepare 20% silk in LiBr and combined. The silk dissolved in LiBr was then diluted to 1% silk and filtered through a 5 μm filter to remove large debris. 17,000 mL of the 1% filtered silk solution was used as the starting volume/percolation volume for TFF. Once LiBr was removed, the solution was ultrafiltered to approximately 3000 mL. 1490 mL of 6.44% silk was then collected. Water was added to the feed to aid in the removal of residual solution, and then 1454 mL of 4.88% silk was collected.

Solution #6 had a silk concentration of 2.70% by weight: a 2.70% silk solution was produced starting with a 60-minute extraction batch of 25g silk cocoons per batch. The extracted silk fibers were then dissolved in 9.3M LiBr at 100°C for 1 hour in a 100°C oven. 35.48g of silk fibers were dissolved per batch to prepare 20% silk in LiBr. The silk dissolved in LiBr was then diluted to 1% silk and filtered through a 5μm filter to remove large debris. 1000mL of the 1% filtered silk solution was used as the starting volume/percolation volume for TFF. Once LiBr was removed, the solution was ultrafiltered to approximately 300mL. 312mL of 2.7% silk was then collected.

Table O shows the preparation of a silk core protein solution with a higher molecular weight.

Table O. Preparation and properties of silk protein solution.

The water-based coating compositions for application to fabrics are given in Tables P and Q below.

Three (3) filament solutions were used in membrane preparation, and the results are as follows:

Solution #1 had a filament concentration of 5.9%, an average MW of 19.8 kDa, and a PD of 2.2 (prepared by boiling extraction for 60 minutes and dissolution in LiBr at 100 °C for 1 hour).

° Solution #2 is a 6.4% filament concentration (prepared by boiling for 30 minutes and dissolving in LiBr at 60°C for 4 hours).

° Solution #3 is a filament concentration of 6.17% (prepared by boiling for 30 minutes and dissolving in LiBr at 100°C for 1 hour).

Membranes were prepared according to Rockwood et al. (Nature Protocols; Vol. 6; No. 10; Published online September 22, 2011; doi:10.1038/nprot.2011.379). 4 mL of an aqueous solution of 1% or 2% (wt/vol) filaments was added to a 100 mm Petit-Blanc dish (the filament volume can be varied for thicker or thinner membranes and is not important) and left to dry open overnight. The bottom of a vacuum desiccator was filled with water. The dried membrane was placed in the desiccator and a vacuum was applied to allow it to undergo water annealing for 4 hours before being removed from the dish. The membrane cast from solution #1 did not yield a structurally continuous membrane; it fractured into several pieces. Despite the water annealing treatment, these membrane fragments dissolved in the water.

Silk solutions of various molecular weights and/or combinations thereof can be optimized for gel applications. An example of this approach is provided below, but it is not intended to be limiting in application or formulation. Three (3) silk solutions were used in gel preparation, with the following results:

Solution #1 had a filament concentration of 5.9%, an average MW of 19.8 kDa, and a PD of 2.2 (prepared by boiling extraction for 60 minutes and dissolution in LiBr at 100 °C for 1 hour).

° Solution #2 is a 6.4% filament concentration (prepared by boiling for 30 minutes and dissolving in LiBr at 60°C for 4 hours).

° Solution #3 is a filament concentration of 6.17% (prepared by boiling for 30 minutes and dissolving in LiBr at 100°C for 1 hour).

"Egel" refers to the electrogelation method described by Rockwood et al. In short, 10 ml of an aqueous solution of wire is added to a 50 ml conical tube, and a pair of platinum wire electrodes are immersed in the wire solution. A 20-volt potential is applied to the platinum electrodes for 5 minutes, the power supply is cut off, and the gel is collected. Solution #1 did not form an EGEL during the 5-minute current application.

Solutions #2 and #3 were gelled according to the disclosed horseradish peroxidase (HRP) procedure. The properties appear to be typical of the disclosed solutions.

Materials and Methods: The following equipment and materials were used in the determination of the molecular weight of the silk: ChemStation software; Agilent 1100 version 10.01; Refractive index detector (RID); Analytical balance; Volumetric flasks (1000 mL, 10 mL, and 5 mL); HPLC grade water; ACS grade sodium chloride; ACS grade disodium hydrogen phosphate heptahydrate; Phosphoric acid; Dextran MW standards - nominal molecular weights of 5 kDa, 11.6 kDa, 23.8 kDa, 48.6 kDa, and 148 kDa; 50 mL disposable PET or polypropylene centrifuge tubes; Graduated pipettes; Amber glass HPLC vials with Teflon caps; Phenomenex PolySep GFC P-4000 column (size: 7.8 mm × 300 mm).

Procedure steps:

A) Preparation of 1 L mobile phase (0.1 M sodium chloride solution in 0.0125 M sodium phosphate buffer)

Take a clean, dry 250 mL beaker, place it on a balance, and tare it. Add approximately 3.3509 g of disodium hydrogen phosphate heptahydrate to the beaker. Record the exact weight of the weighed disodium hydrogen phosphate. Dissolve the weighed sodium phosphate by adding 100 mL of HPLC-grade water to the beaker. Be careful not to spill any contents of the beaker. Carefully transfer the solution to a clean, dry 1000 mL volumetric flask. Rinse the beaker and transfer the rinse solution to the volumetric flask. Repeat rinsing 4–5 times. In a separate clean, dry 250 mL beaker, accurately weigh approximately 5.8440 g of sodium chloride. Dissolve the weighed sodium chloride in 50 mL of water and transfer this solution to the sodium phosphate solution in the volumetric flask. Rinse the beaker and transfer the rinse solution to the volumetric flask. Adjust the pH of the solution to 7.0 ± 0.2 with phosphoric acid. Make up the volume in the volumetric flask to 1000 mL with HPLC-grade water and shake vigorously to mix the solution thoroughly. Filter the solution through a 0.45 μm polyamide membrane filter. Transfer the solution to a clean, dry solvent bottle and label the bottle. The volume of the solution can be changed as needed by adjusting the amounts of disodium hydrogen phosphate heptahydrate and sodium chloride.

B) Preparation of dextran molecular weight standard solution

At least five different molecular weight standards are used for each batch of samples in the run to ensure that the expected values of the test samples are encompassed by the values of the standards used. Six 20 mL scintillation glass vials are labeled as molecular weight standards. Each dextran molecular weight standard is accurately weighed to approximately 5 mg and the weight is recorded. The dextran molecular weight standard is dissolved in 5 mL of mobile phase to prepare a 1 mg/mL standard solution.

C) Preparation of sample solution

When preparing sample solutions, if there is a limitation on the amount of sample available, preparation can be scaled up as long as the ratio is maintained. Weigh sufficient sample into 50 mL disposable centrifuge tubes on an analytical balance to prepare a 1 mg/mL sample solution for analysis, depending on the sample type and silk protein content. Dissolve the sample in an equal volume of mobile phase to prepare a 1 mg/mL solution. Tightly cap the tubes and mix the sample (in solution). Incubate the sample solution at room temperature for 30 minutes. Gently mix the sample solution for 1 minute and centrifuge at 4000 RPM for 10 minutes.

D) HPLC analysis of the sample

Transfer 1.0 mL of all standards and sample solutions to separate HPLC vials. Inject the molecular weight standards (one injection each) and each sample in duplicate. Analyze all standards and sample solutions using the following HPLC conditions:

column PolySep GFC P-4000(7.8×300mm) Column temperature 25℃ detector Refractive index detector (temperature at 35℃) Injection volume 25.0μL mobile phase 0.1M sodium chloride solution in 0.0125M sodium phosphate buffer Flow rate 1.0 mL/min runtime 20.0min

Data Analysis and Calculation - Calculating Average Molecular Weight using Cirrus Software

Upload the chromatographic data files of the standard and analytical samples to the Cirrus SEC data collection and molecular weight analysis software. Calculate the weight-average molecular weight ( _Mw ), number-average molecular weight ( _Mn ), peak-average molecular weight ( _Mp ), and polydispersity of each injection.

Spider silk fragments

Spider silk is a natural polymer composed of three domains: a repetitive central core domain that dominates the protein chain, and non-repetitive N-terminal and C-terminal domains. The large core domain is organized in a block copolymer-like arrangement, where two basic sequences—a crystalline polypeptide [poly(A) or poly(GA)] and a less crystalline polypeptide (GGX or GPGXX (SEQ ID NO: 6))—alternate within the core domain. Dragline silk is a protein complex composed of ampulla of Vater dragline 1 (MaSp1) and ampulla of Vater dragline 2 (MaSp2). Both silks are approximately 3500 amino acids long. MaSp1 is found in the core and periphery, while MaSp2 forms clusters in certain core regions. The large central domains of MaSp1 and MaSp2 are organized in a block copolymer-like arrangement, in which two basic sequences—a crystalline polypeptide [poly(A) or poly(GA)] and a less crystalline polypeptide (GGX or GPGXX (SEQ ID NO:6))—alternate within the core domain. Specific secondary structures are attributed to the poly(A)/(GA), GGX, and GPGXX (SEQ ID NO:6) motifs, comprising β-sheets, α-helices, and β-helices, respectively. The primary sequence, composition, and secondary structure elements of the repeating core domain determine the mechanical properties of the spider silk; while the non-repeating N-terminal and C-terminal domains are crucial for storing the liquid silk dope in the lumen and for fiber formation within the spinning vessel.

The main difference between MaSp1 and MaSp2 is that MaSp2 contains proline (P) residues, accounting for 15% of the total amino acid content, while MaSp1 contains no proline. The presence of these two proteins in the fibers can be estimated by counting the number of proline residues in the drag silk of the spider *N. clavipes*: 81% MaSp1 and 19% MaSp2. Different spiders have different MaSp1 and MaSp2 ratios. For example, drag silk fibers from the orb-weaver spider *Argiope aurantia* contain 41% MaSp1 and 59% MaSp2. This variation in the ratio of large ampulla gland silk can determine the properties of the silk fibers.

For a single species of orb-weaver spider, at least seven different types of silk proteins are known. Silks differ in their primary sequence, physical properties, and function. For example, the drag silk used to construct the framework, radii, and lifelines is renowned for its excellent mechanical properties, including strength, toughness, and elasticity. Spider silk is tougher than steel and Kevlar on an equal weight basis. Flageliform silk, found in capture spirals, has a stretchability of up to 500%. Small urn-shaped glandular silk, found in auxiliary spirals of orb-webs and prey wrapping, has almost the same high toughness and strength as large urn-shaped glandular silk, but does not over-contract in water.

Spider silk is renowned for its high tensile strength and toughness. Recombinant silk proteins also impart favorable properties to cosmetic or dermatological compositions, particularly improving hydration or softening effects, good film-forming properties, and low surface density. The diverse and unique biomechanical properties, along with biocompatibility and a slow degradation rate, make spider silk an excellent candidate for biomaterials in tissue engineering, guided tissue repair and drug delivery, cosmetic products (e.g., nail and hair strengtheners, skin care products), and industrial materials (e.g., nanowires, nanofibers, surface coatings).

In one embodiment, the silk protein may include a polypeptide derived from natural spider silk protein. The polypeptide is not particularly limited, as long as it is derived from natural spider silk protein, and examples of polypeptides include natural spider silk protein and recombinant spider silk protein, such as variants, analogs, derivatives, etc., of natural spider silk protein. For superior toughness, the polypeptide may be derived from the major drag silk protein produced in the ampullae gland of spiders. Examples of major drag silk proteins include the ampullae gland spider silk proteins MaSp1 and MaSp2 from the genus *Nephilaclavipes* and ADF3 and ADF4 from the spider *Araneus diadematus*. Examples of polypeptides derived from major drag silk proteins include variants, analogs, derivatives, etc. Furthermore, the polypeptide may be derived from the flagellate gland silk protein produced in the flagellate gland of spiders. Examples of flagellate gland silk proteins include the flagellate gland silk protein derived from the genus *Nephilaclavipes*.

Examples of polypeptides derived from major filament proteins include polypeptides containing two or more units of the amino acid sequence represented by Formula 1: REP1-REP2 (1), preferably polypeptides containing five or more such units, more preferably polypeptides containing ten or more such units. Alternatively, a polypeptide derived from a major filament protein may be a polypeptide containing units of the amino acid sequence represented by Formula 1: REP1-REP2 (1) and having at its C-terminus an amino acid sequence represented by any one of SEQ ID NO: 52 to 54 (also described in U.S. Patent 9,051,453, which is incorporated herein by reference in its entirety), or an amino acid sequence having 90% or more homology with any one of the amino acid sequences represented by SEQ ID NO: 52 to 54 (also described in U.S. Patent 9,051,453, which is incorporated herein by reference in its entirety). In polypeptides derived from major filament proteins, units of the amino acid sequence represented by Formula 1: REP1-REP2 (1) may be identical to or different from each other. When using microorganisms such as Escherichia coli as a host to produce recombinant proteins, the molecular weight of polypeptides derived from the main drag silk protein is 500 kDa or less, or 300 kDa or less, or 200 kDa or less, taking productivity into consideration.

In formula (1), REP1 refers to polyalanine. In REP1, the number of consecutively arranged alanine residues is preferably 2 or more, more preferably 3 or more, further preferably 4 or more, and particularly preferably 5 or more. Furthermore, in REP1, the number of consecutively arranged alanine residues is preferably 20 or less, more preferably 16 or less, further preferably 12 or less, and particularly preferably 10 or less. In formula (1), REP2 is an amino acid sequence consisting of 10 to 200 amino acid residues. The total number of glycine, serine, glutamine, and alanine residues contained in the amino acid sequence is 40% or more, preferably 60% or more, and more preferably 70% or more, relative to the total number of amino acid residues contained therein.

In the main drag filaments, REP1 corresponds to the crystalline region in the fiber, where crystalline β-sheets are formed, and REP2 corresponds to the amorphous region in the fiber, where most of the portions lack a regular conformation and have greater flexibility. Furthermore, [REP1-REP2] corresponds to the repeating region (repetitive sequence) composed of the crystalline and amorphous regions, which is the characteristic sequence of drag filament proteins.

Reconstituted fiber fragments

In some embodiments, recombinant silk protein refers to recombinant spider silk polypeptides, recombinant insect silk polypeptides, or recombinant shell silk polypeptides. In some embodiments, the recombinant silk protein fragments disclosed herein include recombinant spider silk polypeptides from the family Araneidae or Araneoids, or recombinant insect silk polypeptides from the silkworm (Bombyx mori). In some embodiments, the recombinant silk protein fragments disclosed herein include recombinant spider silk polypeptides from the family Araneidae or Araneoids. In some embodiments, the recombinant silk protein fragments disclosed herein include block copolymers having repeating units of natural spider silk polypeptides derived from the family Araneidae or Araneoids. In some embodiments, the recombinant silk protein fragments disclosed herein include block copolymers having synthetic repeating units of spider silk polypeptides derived from the family Araneidae or Araneoids and non-repeating units of natural repeating units of spider silk polypeptides derived from the family Araneidae or Araneoids.

Recent advances in genetic engineering have provided routes for producing various types of recombinant silk proteins. Recombinant DNA technology has been used to provide more practical sources of silk proteins. As used in this article, "recombinant silk proteins" refers to synthetic proteins produced heterologously in prokaryotic or eukaryotic expression systems using genetic engineering methods.

Various methods for synthesizing recombinant silk peptides are known and described by Ausubel et al., Current Protocols in Molecular Biology, §8 (John Wiley & Sons 1987, (1990)), which are incorporated herein by reference. The Gram-negative rod-shaped bacterium *Escherichia coli* (E. coli) is the recognized host for industrial-scale protein production. Therefore, most recombinant silk peptides have been produced in *E. coli*. *E. coli* is easy to manipulate, has a short generation time, is relatively low-cost, and can be scaled up for larger quantities of protein production.

Recombinant silk proteins can be generated through a transformation system containing cDNA encoding a silk protein, a fragment of such a protein, or an analogue of such a protein. The recombinant DNA pathway enables the production of recombinant silks with programmed sequences, secondary structures, configurations, and precise molecular weights. This method involves four main steps: (i) designing and assembling the synthesized silk-like gene into a gene "cassette," (ii) inserting this fragment into a recombinant DNA vector, (iii) transforming this recombinant DNA molecule into host cells, and (iv) expression and purification of the selected clone.

As used herein, the term "recombinant vector" includes any vector known to those skilled in the art, including plasmid vectors, granular vectors, bacteriophage vectors such as λ phage, viral vectors such as adenovirus or baculovirus vectors, or artificial chromosome vectors such as bacterial artificial chromosomes (BAC), yeast artificial chromosomes (YAC), or P1 artificial chromosomes (PAC). These vectors include expression vectors and cloning vectors. Expression vectors contain plasmids and viral vectors and typically contain the desired coding sequence and the appropriate DNA sequence necessary to express the operably linked coding sequence in a specific host organism (e.g., bacteria, yeast, or plant) or in an in vitro expression system. Cloning vectors are typically used for the engineering and amplification of a specific desired DNA fragment and may lack the functional sequence required to express the desired DNA fragment.

Prokaryotic systems include Gram-negative or Gram-positive bacteria. Prokaryotic expression vectors may include a host-recognizable origin of replication, a homologous or heterologous promoter functional in the host, a spider silk protein, a fragment of such a protein, or a DNA sequence encoding a similar protein. Non-limiting examples of prokaryotic expression organisms include *Escherichia coli*, *Bacillus subtilis*, *Bacillus megaterium*, *Corynebacterium glutamicum*, *Anabaena*, *Stemycetes*, *Staphylococcus*, *Rhodophyta*, *Pseudomonas*, *Paracococcus*, *Bacillus* (e.g., *Bacillus subtilis*), *Bryophytes*, *Corynebacterium*, *Rhizobium sinense*, *Flavobacterium*, *Klebsiella*, *Enterobacter*, *Lactobacillus*, *Lactococcus*, *Methylobacterium*, *Propionibacterium*, *Staphylococcus*, or *Streptomyces* cells.

Eukaryotic systems include yeast and insect, mammalian, or plant cells. In this case, expression vectors may include a yeast plasmid origin of replication or autonomous replication sequence, a promoter, a DNA sequence encoding a spider silk protein, a fragment, or a similar protein, a polyadenylated sequence, a transcription termination site, and finally, a selected gene. Non-limiting examples of eukaryotic expression organisms include yeasts such as *Saccharomyces cerevisiae*, *Pichia pastoris*, *basidiosporogenous*, and *ascosporogenous*; filamentous fungi such as *Aspergillus niger*, *Aspergillus oryzae*, *Aspergillus nidus*, *Trichoderma reesei*, and *Acremonium chrysogenum*; *Candida*, *Hansenula*, *Kluyveromyces*; *Saccharomyces* (e.g., *Saccharomyces cerevisiae*); *Schizostomyces*; and *Pichia pastoris*. Cells such as Pichia pastoris or Yersinia genus, mammalian cells such as HeLa cells, COS cells, CHO cells, etc., insect cells such as Sf9 cells, MEL cells, etc., "insect host cells" such as fall armyworm or white armyworm cells, SF9 cells, SF-21 cells or High-Five cells, of which SF-9 and SF-21 are derived from fall armyworm ovarian cells and High-Five cells are derived from white armyworm egg cells, "plant host cells" such as tobacco, potato or pea cells.

Various heterologous host systems have been developed for the production of different types of recombinant silk. Recombinant spider silk proteins and engineered silks have been cloned and expressed in bacteria (Escherichia coli), yeast (Pichia pastoris), insects (silkworm larvae), plants (tobacco, soybean, potato, Arabidopsis thaliana), mammalian cell lines (BHT/hamster), and transgenic animals (mice, goats). Most of the silk proteins produced have N-terminal or C-terminal His tags to facilitate purification and produce sufficient protein yields.

In some embodiments, suitable hosts for expressing recombinant spider silk proteins using a heterologous system may include transgenic animals and plants. In some embodiments, suitable hosts for expressing recombinant spider silk proteins using a heterologous system include bacteria, yeast, and mammalian cell lines. In some embodiments, suitable hosts for expressing recombinant spider silk proteins using a heterologous system include *Escherichia coli*. In some embodiments, suitable hosts for expressing recombinant spider silk proteins using a heterologous system include transgenic silkworms (*B. mori*) generated using genome editing technologies (e.g., CRISPR).

The recombinant silk proteins in this disclosure comprise synthetic proteins based on repeating units of natural silk proteins. In addition to the synthetic repeating silk protein sequences, these may additionally comprise one or more natural non-repetitive silk protein sequences.

In some implementations, "recombinant silk fibroin" refers to recombinant silk fibroin or fragments thereof. Recombinant production of fibroin and sericin has been reported. Various hosts have been used for this production, including *Escherichia coli*, *Saccharomyces cerevisiae*, *Pseudomonas*, *Rhodopseudomonas*, *Bacillus*, and *Streptomyces*. See EP 0230702, which is incorporated herein by reference in its entirety.

This article also provides the design and biosynthesis of a silk-core protein-like multiblock polymer containing a repeating domain derived from the heavy chain (H chain) of silkworm silk, namely GAGAGX (SEQ ID NO:1) hexapeptide (X is A, Y, V or S).

In some embodiments, this disclosure provides silk protein-like multiblock polymers derived from repeating domains of the heavy chain (H chain) of silkworm silk containing repeating units of the GAGAGS (SEQ ID NO:2) hexapeptide. The GAGAGS (SEQ ID NO:2) hexapeptide is the core unit of the H chain and plays an important role in the formation of the crystalline domains. The silk protein-like multiblock polymers containing repeating units of the GAGAGS (SEQ ID NO:2) hexapeptide spontaneously aggregate into a β-sheet structure similar to that of natural silk core proteins, wherein the silk protein-like multiblock polymer has any of the weight-average molecular weights described herein.

In some embodiments, this disclosure provides a silk peptide-like multiblock copolymer composed of a GAGAGS (SEQ ID NO:2) hexapeptide repeat fragment derived from the H chain of the silkworm heavy chain and a mammalian elastin VPGVG (SEQ ID NO:3) motif generated by *E. coli*. In some embodiments, this disclosure provides a fused silk core protein composed of a GAGAGS (SEQ ID NO:2) hexapeptide repeat fragment derived from the H chain of the silkworm heavy chain and a GVGVP (SEQ ID NO:4) generated by *E. coli*, wherein the silk protein-like multiblock polymer has any of the weight-average molecular weights described herein.

In some embodiments, this disclosure provides a recombinant silkworm protein consisting of a (GAGAGS) ₁₆ (SEQ ID NO:55) repeating fragment. In some embodiments, this disclosure provides a recombinant protein composed of a repeating fragment of (GAGAGS) ₁₆ (SEQ ID NO:55) and non-repetitive (GAGAGS) ₁₆ -F-COOH (SEQ ID NO:56), (GAGAGS) ₁₆ -FF-COOH (SEQ ID NO:57), (GAGAGS) _16- FFF-COOH (SEQ ID NO:58), (GAGAGS) _16- FFFF-COOH (SEQ ID NO:59), (GAGAGS) _16- FFFFFFFF-COOH (SEQ ID NO:60), and (GAGAGS) ₁₆ -FFFF–FFFFFFFF-COOH (SEQ ID NO:61) generated from E. coli, wherein F has the following amino acid sequence SGFGPVANGGSGEASSESDFGSSGFGPVANASSGEASSESDFAG (SEQ ID NO:5), and wherein the silk-like multiblock polymer has any of the weight-average molecular weights described herein.

In some implementations, “recombinant silk protein” refers to recombinant spider silk protein or fragments thereof. Production of recombinant spider silk proteins based on partial cDNA clones has been reported. The recombinant spider silk proteins thus produced contain a portion of a repeating sequence derived from the spider filament Spidroin 1, which is from the spider *Nematocera*. See Xu et al. (Proc. Natl. Acad. Sci. U.S.A., 87:7120–7124 (1990). The cDNA clone encoding a portion of a repeating sequence of Spidroin 2, a second silk protein from *Nematocera* spiders, and its recombinant synthesis are described in J. Biol. Chem., 1992, volume 267, pp. 19320–19324. Spider silk proteins containing protein fragments and variants recombinantly synthesized by transformation of *E. coli* are described in the U.S. Patent and Trademark Office. U.S. Patents 5,728,810 and 5,989,894 describe the cDNA clone encoding a small urticaria gland silk protein and its expression. U.S. Patents 5,733,771 and 5,756,677 describe the cDNA clone encoding a whip-like gland silk protein from orb-webspinning spiders. U.S. Patent 5,994,099 describes the recombinant synthesis of a natural spider drag silk derived from *Nematocera* spiders using a recombinant expression system of *E. coli*, *Bacillus subtilis*, and *Pichia pastoris*. Spider silk-like proteins with repetitive peptide sequences. WO 03/020916 describes the cDNA cloning and recombinant production of spider silk proteins with repetitive sequences derived from the large ampullae glands of *Nephila madagascariensis*, *Nephila senegalensis*, *Tetragnathakauaiensis*, *Tetragnatha versicolor*, *Argiope aurantia*, *Argiope trifasciata*, *Gasteracantha mammosa*, and *Latrodectus geometricus*, the whip-like glands of *Argiope trifasciata*, the ampullae glands of *Dolomedes tenebrosus*, the two sets of silk glands of *Plectreurys tristis*, and the silk glands of *mygalomorph Euagrus chisoseus*. All of the above references are incorporated herein by reference in their entirety.

In some embodiments, the recombinant spider silk protein is a hybrid protein of spider silk protein and insect silk protein, spider silk protein and collagen, spider silk protein and arthropod elastin, or spider silk protein and keratin. The spider silk repeating unit comprises or consists of an amino acid sequence comprising or consisting of at least one repeating peptide motif within a naturally occurring ampullae gland polypeptide, such as a dragnet spider silk polypeptide, a small ampullae gland polypeptide, a whip-like gland polypeptide, an aggregated spider silk polypeptide, a varicella-like gland spider silk polypeptide, or a pyriform spider silk polypeptide.

In some embodiments, the recombinant spider silk protein of this disclosure comprises a repeating unit derived from natural spider silk protein, a common sequence, and optionally one or more natural non-repetitive spider silk protein sequences of synthetic spider silk protein. The repeating unit of the natural spider silk polypeptide may include drag-web spider silk polypeptides or whip-gland spider silk polypeptides from Araneidae or Araneoids.

As used herein, a spider silk “repetitive unit” comprises or consists of at least one repeating peptide motif found in naturally occurring ampullae gland polypeptides, such as tufted spider silk polypeptide, ampullae gland polypeptide, whip-like gland polypeptide, polymorphic spider silk polypeptide, variegata spider silk polypeptide, or piriformis spider silk polypeptide. A “repetitive unit” refers to a region in the amino acid sequence corresponding to or consisting of at least one repeating peptide motif (e.g., AAAAAA (SEQ ID NO: 20) or GPGQQ (SEQ ID NO: 15)) found in naturally occurring silk polypeptides (e.g., MaSpI, ADF-3, ADF-4, or Flag) (i.e., the same amino acid sequence) or a region corresponding to a substantially similar amino acid sequence (i.e., a varied amino acid sequence). “Repetitive units” having an amino acid sequence that is “substantially similar” to the corresponding amino acid sequence in naturally occurring silk polypeptides (i.e., wild-type repeat units) are also similar in properties; for example, silk proteins containing “substantially similar repeat units” remain insoluble and retain their insolubility. A "repetitive unit" having an amino acid sequence "identical" to that of a naturally occurring silk polypeptide can be, for example, a portion of a silk polypeptide corresponding to one or more peptide motifs of MaSpI (SEQ ID NO:48), MaSpII (SEQ ID NO:49), ADF-3 (SEQ ID NO:50), and/or ADF-4 (SEQ ID NO:51). A "repetitive unit" having an amino acid sequence "substantially similar" to that of a naturally occurring silk polypeptide can be, for example, a portion of a silk polypeptide corresponding to one or more peptide motifs of MaSpI (SEQ ID NO:48), MaSpII (SEQ ID NO:49), ADF-3 (SEQ ID NO:50), and/or ADF-4 (SEQ ID NO:51) but having one or more amino acid substitutions at specific amino acid positions.

As used herein, the term "common peptide sequence" refers to an amino acid sequence containing an amino acid that occurs frequently at a position (e.g., "G") and in which no other amino acid is further identified is replaced by a placeholder "X". In some embodiments, the common sequence is at least one of the following: (i) GPGXX (SEQ ID NO:6), wherein X is an amino acid selected from A, S, G, Y, P and Q; (ii) GGX, wherein X is an amino acid selected from Y, P, R, S, A, T, N and Q, preferably Y, P and Q; (iii) A _x , wherein x is an integer from 5 to 10.

The shared peptide sequence of GPGXX (SEQ ID NO:6) and GGX, namely the glycine-rich motif, provides flexibility to the silk polypeptide and thus to the thread formed from silk proteins containing said motif. Specifically, the iterative GPGXX (SEQ ID NO:6) motif forms a spiral helical structure, which imparts elasticity to the silk polypeptide. Both ampullary and flagellate gland filaments possess the GPGXX (SEQ ID NO:6) motif. The iterative GGX motif is associated with a helical structure having three amino acids per turn and is present in most spider silks. The GGX motif provides additional elasticity to the silk. The iterative polyalanine Ax (peptide) motif forms a crystalline β-sheet structure to provide strength to the silk polypeptide, as described, for example, in WO 03/057727.

In some embodiments, the recombinant spider silk protein of this disclosure comprises two identical repeating units, each containing at least one, preferably one, amino acid sequence selected from: GGRPSDTYG (SEQ ID NO:7) and GGRPSSSYG (SEQ ID NO:8) derived from arthropod elastin. Arthropod elastin is an elastomeric protein found in most arthropods, providing low stiffness and high strength.

As used herein, "non-repeating unit" refers to an amino acid sequence that is "substantially similar" to the corresponding non-repeating (C-terminal) amino acid sequence (i.e., wild-type non-repeating (C-terminal) unit) within naturally occurring drag silk polypeptides, preferably within the 16-repeating C16 peptide (spider silk protein eADF4, molecular weight 47.7 kDa, AMSilk) of the spider *A. cruciformis*, including ADF-3 (SEQ ID NO: 50), ADF-4 (SEQ ID NO: 51), NR3 (SEQ ID NO: 62), NR4 (SEQ ID NO: 63) (also described in U.S. Patent 9,217,017, which is incorporated herein by reference in its entirety), comprising the sequence GSSAAAAAAAASGPGGYGPENQGPSGPGGYGPGGP (SEQ ID NO: 9). Non-repeating ADF-4 and its variants exhibit highly efficient assembly properties.

In synthetic spider silk proteins, the recombinant silk proteins of this disclosure, in some embodiments, comprise a C16 protein having the polypeptide sequence SEQ ID NO:64 (also described in U.S. Patent 8,288,512, which is incorporated herein by reference in its entirety). In addition to the polypeptide sequence shown in SEQ ID NO:64, functional equivalents, functional derivatives, and salts of such sequences are also specifically included.

The term "functional equivalent" as used in this article refers to a mutant that has an amino acid at at least one sequence position in the amino acid sequence mentioned above that is different from the amino acid specifically mentioned.

In some embodiments, the recombinant spider silk protein of this disclosure comprises an effective amount of at least one natural or recombinant silk protein, including spider silk protein corresponding to Spidroin major 1 described in Xu et al., PNAS, USA, 87, 7120, (1990), Spidroin major 2 described in Hinman and Lewis, J. Biol. Chem., 267, 19320, (1922), and as in U.S. Patent Application 2016/02. The recombinant spider silk proteins described in U.S. Patents 22174 and 9,051,453, 9,617,315, 9,689,089, 8,173,772, 8,642,734, 8,367,803, 8,097,583, 8,030,024, 7,754,851, 7,148,039, and 7,060,260, or the minor spider silk proteins described in patent application WO 95/25165, are all incorporated herein by reference. Additional recombinant spider silk proteins applicable to the recombinant RSPF of this disclosure include ADF3 and ADF4 from the "large ampulla" of the spider *Archaeopteryx*.

Reconstituted fibers are also described in other patents and patent applications incorporated herein by reference: US 2004590196, US7,754,851, US2007654470, US 7,951,908, US2010785960, US 8,034,897, US20090263430, US2008226854, US20090123967, US 2005712095, US2007991037, US20090162896, US200885266, US 8,372,436, US2007989907, US20092675 96. US2010319542, US2009265344, US2012684607, US2004583227, US 8,030,024, US 2006643569, US 7,868,146, US2007991916, US 8,097,5 83. US2006643200, US 8,729,238, US 8,877,903, US20190062557, US20160280960, US 20110201783, US2008991916, US2011986662, US20126 97729, US 20150328363, US 9,034,816, US20130172478, US 9,217,017, US20170202995, US 8,721,991, US2008227498, US 9,233,067, US 8,288,512, US2008161364, US 7,148,039, US1999247806, US2001861597, US 2004887100, US 9,481,719, US 8,765,688, US200880705, US20 10809102, US 8,367,803, US2010664902, US 7,569,660, US1999138833, US 2000591632, US20120065126, US20100278882, US2008161352, US 20100015070, US2009513709, US20090194317, US2004559286, US 200589551, US2008187824, US20050266242, US20050227322 and US 20044418.

Reconstituted fibers are also described in other patents and patent applications incorporated herein by reference: US 20190062557, US20150284565, US20130225476, US20130172478, US 20130136779, US20130109762, US20120252294, US20110230911, US 20110201783, US20100298877, US10,478,520 , US10,253,213, US 10,072,152, US 9,233,067, US 9,217,017, US 9,034,816, US 8,877,903, US8,729,238 , US 8,721,991, US 8,097,583, US 8,034,897, US 8,030,024, US 7,951,908, US 7,868,146 and US 7,754,851.

In some embodiments, the recombinant spider silk protein of this disclosure comprises or consists of 2 to 80 repeating units, each of which is independently selected from GPGXX (SEQ ID NO:6), GGX and _Ax as defined herein.

In some embodiments, the recombinant spider silk protein of this disclosure comprises or is composed of repeating units, each of which is selected from the group consisting of: GPGAS (SEQ ID NO:10), GPGSG (SEQ ID NO:11), GPGGY (SEQ ID NO:12), GPGGP (SEQ ID NO:13), GPGGA (SEQ ID NO:14), GPGQQ (SEQ ID NO:15), GPGGG (SEQ ID NO:16), GPGQG (SEQ ID NO:17), GPGGS (SEQ ID NO:18), GGY, GGP, GGA, GGR, GGS, GGT, GGN, GGQ, AAAAA (SEQ ID NO:19), AAAAAA (SEQ ID NO:20), AAAAAAA (SEQ ID NO:21), AAAAAA AA(SEQ ID NO:22), AAAAAAAAA(SEQ ID NO:23), AAAAAAAAAA(SEQ ID NO:24), GGRPSDTYG(SEQ ID NO:7) and GGRPSSSYG(SEQ ID NO:8), (i)GPYGPGASAAAAAAGGYGPSGGQQ(SEQ ID NO:25), (ii)GSSAAAAAAAA SGPGGYGPENQGSGPGGYGPGGP(SEQ ID NO:9), (iii)GPGQQGPGQQGPGQQGPGQQ(SEQ ID NO:26), (iv)GPGGAGGPYGPGGAGGPYGPGGAGGPY(SEQ ID NO:27), (v)GGTTIIEDLDITIDGADGPITISEELTI(SEQ ID NO:28) , (vi)PGSSAAAAAAAAASGPGQGQGQGQGQGGRPSDTYG(SEQ ID NO:29), (vii)SAAAAAAAAGPGGGNGGRPSDTYGAPGGGNGGRPSSSYG(SEQ ID NO:30), (viii)GGAGGAGGAGGSGGAGGS(SEQ IDNO:31), (ix)GPGGAGPGGYGP GGSGPGGYGPPGGSGPGGY(SEQ ID NO:32), (x)GPYGPGASAAAAAAGGYGPGCGQQ(SEQ ID NO:33), (xi)GPYGPGASAAAAAAGGYGPGKGQQ(SEQ ID NO:34), (xii)GSSAAAAAAAASGPGGYGPENQGPCGPGGYGPGGP(SEQ ID NO: 35), (xiii)GSSAAAAAAAASGPGGYGPKNQGPSGPGGYGPGGP (SEQ ID NO:36), (xiv)GSSAAAAAAAASGPGGYGPKNQGPCGPGGYGPGGP (SEQ ID NO:37), or variants thereof as described in U.S. Patent 8,877,903, such as synthetic spider peptides having the sequence sequence GPGAS (SEQ ID NO:10), GGY, GPGSG (SEQ ID NO:11) in the peptide chain or having the sequence sequence AAAAAAAA (SEQ ID NO:22), GPGGY (SEQ ID NO:12), GPGGP (SEQ ID NO:13) in the peptide chain, or having the sequence sequence AAAAAAAA (SEQ ID NO:22), GPGQG (SEQ ID NO:17), GGR in the peptide chain.

In some embodiments, this disclosure provides silk-like multi-block peptides that mimic repeating units of amino acids derived from natural spider silk, such as a Spidroin major 1 domain, a Spidroin major 2 domain, or a Spidroin minor 1 domain, and a profile of variation among the repeating units without altering their three-dimensional conformation, wherein these silk-like multi-block peptides contain amino acid repeating units corresponding to one of the following sequences (I), (II), (III), and/or (IV).

[(XGG) _w (XGA)(GXG) _x (AGA) _y (G) _z AG] _p (SEQ ID NO:38) Formula (I), where: X corresponds to tyrosine or glutamine, w is an integer equal to 2 or 3, x is an integer from 1 to 3, y is an integer from 5 to 7, z is an integer equal to 1 or 2, and p is an integer having any weight-average molecular weight as described herein, and/or

[(GPG ₂ YGPGQ ₂ ) _a (X') ₂ S(A) _b ] _p (SEQ ID NO:39) Formula (II), where: X' corresponds to the amino acid sequence GPS or GPG, a equals 2 or 3, b is an integer from 7 to 10, p is an integer and has any weight-average molecular weight as described herein, and/or

[(GR)(GA) _l (A) _m (GGX) _n (GA) _l (A) _m ] _p (SEQ ID NO:40) formula (III) and/or [(GGX”) _n (GA) _m (A) _l ] _p (SEQ ID NO:41) formula (IV), where: X” corresponds to tyrosine, glutamine or alanine, L is an integer from 1 to 6, m is an integer from 0 to 4, n is an integer from 1 to 4, and p is an integer.

In some embodiments, recombinant spider silk protein or spider silk protein analogs comprise an amino acid repeating unit of sequence (V):

[(Xaa Gly Gly) _w (Xaa Gly Ala)(Gly Xaa Gly) _x (Ala Gly Ala) _y (Gly) _z Ala Gly] _p (V), where Xaa is tyrosine or glutamine, w is an integer equal to 2 or 3, x is an integer from 1 to 3, y is an integer from 5 to 7, z is an integer equal to 1 or 2, and p is an integer.

In some embodiments, the recombinant spider silk protein of this disclosure is selected from ADF-3 or variants thereof, ADF-4 or variants thereof, MaSpI or variants thereof, MaSpII or variants thereof, as described in U.S. Patent 9,217,017.

In some embodiments, this disclosure provides water-soluble recombinant spider silk proteins prepared in mammalian cells. The solubility of spider silk proteins prepared in mammalian cells can be attributed to the presence of COOH terminals in these proteins, making them more hydrophilic. These COOH-terminal amino acids are absent in spider silk proteins expressed in microbial hosts.

In some embodiments, the recombinant spider silk protein of this disclosure comprises a water-soluble recombinant spider silk protein C16 modified with an amino or carboxyl terminus selected from the amino acid sequences: GCGGGGGG (SEQ ID NO:42), GKGGGGGG (SEQ ID NO:43), GCGGSGGGGGSGGGG (SEQ ID NO:44), GKGGGGGGGSGGGG (SEQ ID NO:45), and GCGGGGGGSGGGG (SEQ ID NO:46). In some embodiments, the recombinant spider silk protein of this disclosure comprises _C16 NR4, _C32 NR4, C16, C32, _NR4C16 NR4, _NR4C32 NR4, _NR3C16 NR3, or _NR3C32 NR3, such that the molecular weight of the protein is within the range described herein.

In some embodiments, the recombinant spider silk protein of this disclosure comprises a recombinant spider silk protein having a synthetic repeating peptide segment and an amino acid sequence modified from the natural sequence of ADF4 from the spider *Ardisia cruciformis*, as described in U.S. Patent 8,877,903. In some embodiments, the RSPF of this disclosure comprises a recombinant spider silk protein having repeating peptide units derived from natural spider silk proteins, such as a Spidroin major 1 domain, a Spidroin major 2 domain, or a Spidroin minor 1 domain, wherein the repeating peptide sequence is GSSAAAAAAAASGPGQGQGQGQGQGRPSDTYG (SEQ ID NO: 47) or SAAAAAAAAGPGGGNGGRPSDTYGAPGGGNGGRPSSSYG (SEQ ID NO: 30), as described in U.S. Patent 8,367,803, which is incorporated herein by reference in its entirety.

In some embodiments, this disclosure provides a recombinant spider silk protein consisting of a repeating fragment of GPGGAGPGGYGPGGSGPGGYGPGGSGPGGY (SEQ ID NO: 32) and having the molecular weight as described herein.

As used herein, the term "recombinant silk" refers to recombinant spider silk and/or silk protein or fragments thereof. In one embodiment, the spider silk protein is selected from swathing silk (achniform glandular silk), eggsac silk (cylindriform glandular silk), egg case silk (tubuliform glandular silk), ampullate glandular silk, pear-shaped glandular silk, flagelliform glandular silk, and plexiform glandular silk. For example, the recombinant spider silk protein described herein includes proteins described in U.S. Patent Application 2016/0222174 and U.S. Patents 9,051,453, 9,617,315, 9,689,089, 8,173,772, and 8,642,734.

Some organisms produce a variety of silk fibers with unique sequences, structural elements, and mechanical properties. For example, the orb-weaving spider possesses six distinct types of glands that produce different silk polypeptide sequences, which aggregate into fibers adapted to their environment or lifecycle niche. These fibers are named after the glands from which they originate, and the polypeptides are labeled with gland abbreviations (e.g., "Ma") and "Sp," short for spider silk protein (abbreviation for spider silk heart protein). In the orb-weaving spider, these types include the large ampulla (MaSp, also known as the drag silk), the small ampulla (MiSp), the flagellate (Flag), the variegated (AcSp), the tubular (TuSp), and the piriform (PySp). This combination of polypeptide sequences across fiber types, domains, and variations across different genera and species of organisms yields a large range of potential properties that can be controlled through the commercial production of recombinant fibers. To date, the vast majority of work on recombinant silk has focused on the large ampulla (MaSp) spider silk protein.

Gracilaria (AcSp) filaments tend to have high toughness, a result of a combination of medium-to-high strength and medium-to-high ductility. AcSp filaments are characterized by large block ("overall repeat") sizes, which typically contain polyserine and GPX motifs. Tubular (TuSp or Cylindrical) filaments tend to have large diameters, as well as moderate strength and high ductility. TuSp filaments are characterized by their polyserine and polythreonine content, and short segments of polyalanine. Macroambulatory (MaSp) filaments tend to have high strength and moderate ductility. MaSp filaments can be one of two subtypes: MaSp1 and MaSp2. MaSp1 filaments are generally less ductile than MaSp2 filaments and are characterized by polyalanine, GX, and GGX motifs. MaSp2 filaments are characterized by polyalanine, GGX, and GPX motifs. Microambulatory (MiSp) filaments tend to have moderate strength and moderate ductility. MiSp filaments are characterized by GGX, GA, and poly A motifs and typically contain spacer units of about 100 amino acids. Flag filaments tend to have extremely high elongation and moderate strength. Flag filaments are typically characterized by GPG, GGX, and short-spacer motifs.

Silk polypeptides are uniquely composed of repeating domains (REPs) and non-repeating regions flanking them (e.g., C-terminal and N-terminal domains). In one embodiment, both the C-terminal and N-terminal domains are 75–350 amino acids in length. The repeating domains exhibit a hierarchical structure. Each repeating domain contains a series of blocks (also called repeating units). These blocks are repeated within the silk repeating domain, sometimes perfectly and sometimes imperfectly (forming quasi-repeating domains). The length and composition of the blocks vary between different silk types and between different species. Table 1 of U.S. Publication Application 2016/0222174 (in its entirety incorporated herein by reference) lists examples of block sequences from selected species and silk types, further illustrated in Rising, A. et al., Spider silk proteins: recent advances in recombinant production, structure-function relationships and biomedical applications, Cell Mol. Life Sci., 68:2, pg 169-184 (2011); and Gatesy, J. et al., Extreme diversity, conservation, and convergence of spider silk fibroin sequences, Science, 291:5513, pg.2603-2605 (2001). In some cases, blocks can be arranged in a regular pattern to form larger macro-repeats that appear multiple times (typically 2-8 times) in the repeating domains of the silk sequence. Repeating segments within repeating structural domains or large repeats, and repeating large repeats within repeating structural domains, can be separated by spacing units.

U.S. Patent Application Publication 2016/0222174 describes certain embodiments of spider silk block copolymer peptides constructed from these blocks and/or large repeating domains according to this disclosure.

Recombinant block copolymer peptides based on spider silk sequences, prepared by gene expression in recombinant prokaryotic or eukaryotic systems, can be purified according to methods known in the art. In a preferred embodiment, a commercially available expression/secretion system can be used to express the recombinant peptide, which is then secreted from a host cell for easy purification from the surrounding medium. If an expression/secretion vector is not used, alternative methods involve purifying the recombinant block copolymer peptide from cell lysates (cell remnants after disruption of cell integrity) derived from prokaryotic or eukaryotic cells expressing the peptide. Methods for generating such cell lysates are known to those skilled in the art. In some embodiments, the recombinant block copolymer peptide is isolated from cell culture supernatant.

Recombinant block copolymer peptides can be purified by affinity separation, for example, through immune interactions with antibodies that specifically bind to the recombinant peptide, or by using a nickel column to separate the recombinant peptide labeled with 6-8 histidine residues at its N-terminus or C-terminus. Alternative tags may include FLAG epitopes or hemagglutinin epitopes. Skilled practitioners commonly use such methods.

Solutions of such polypeptides (i.e., recombinant silk proteins) can then be prepared and used as described herein.

In another embodiment, the recombinant silk fibroin may be prepared according to the method described in U.S. Patent 8,642,734 (which is incorporated herein by reference in its entirety) and used as described herein.

In one embodiment, a recombinant spider silk protein is provided. This spider silk protein typically consists of 170 to 760 amino acid residues, such as 170 to 600 amino acid residues, preferably 280 to 600 amino acid residues, such as 300 to 400 amino acid residues, and more preferably 340 to 380 amino acid residues. Smaller size is advantageous because longer spider silk proteins tend to form amorphous aggregates, requiring the use of harsh solvents for dissolution and polymerization. The recombinant spider silk protein may contain more than 760 residues, particularly in cases where the spider silk protein comprises more than two fragments derived from the N-terminal portion of the spider silk protein, the spider silk protein comprising an N-terminal fragment consisting of at least one fragment (NT) derived from the corresponding portion of the spider silk protein, and a repeating fragment (REP) derived from the corresponding internal fragment of the spider silk protein. Optionally, the spider silk protein comprises a C-terminal fragment (CT) derived from the corresponding fragment of the spider silk protein. The spider silk protein typically comprises a single fragment (NT) derived from the N-terminal portion of the spider silk protein, but in a preferred embodiment, the N-terminal fragment comprises at least two, such as two fragments (NT) derived from the N-terminal portion of the spider silk protein. Thus, the spider silk protein can be schematically represented by the formula NT _m -REP or NT _m -REP-CT, where m is 1 or higher, such as 2 or higher, preferably an integer in the range of 1-2, 1-4, 1-6, 2-4, or 2-6. Preferred spider silk proteins can be schematically represented by the formula NT ₂ -REP or NT-REP, or NT ₂ -REP-CT or NT-REP-CT. Protein fragments are typically covalently coupled via peptide bonds. In one embodiment, the spider silk protein consists of one or more NT fragments coupled to a REP fragment, which is optionally coupled to a CT fragment.

In one embodiment, the first step of the method for producing a polymer of isolated spider silk protein involves expressing a polynucleotide molecule encoding the spider silk protein in a suitable host, such as *E. coli*. The resulting protein is then isolated using a standard procedure. Optionally, lipopolysaccharides and other pyrogens are actively removed at this stage.

In the second step of the method for producing a polymer of isolated spider silk protein, a solution of the spider silk protein in a liquid medium is provided. The terms "soluble" and "in solution" mean that the protein does not show significant aggregation at 60,000 × g and does not precipitate from the solvent. The liquid medium can be any suitable medium, such as an aqueous medium, preferably a physiological medium, typically a buffered aqueous medium, such as 10-50 mM Tris-HCl buffer or phosphate buffer. The liquid medium has a pH of 6.4 or higher and/or an ionic composition that prevents spider silk protein polymerization. That is, the liquid medium has a pH of 6.4 or higher or an ionic composition that prevents spider silk protein polymerization, or both.

Those skilled in the art can readily prepare ionic compositions that prevent the polymerization of spider silk proteins using the methods disclosed herein. Preferred ionic compositions for preventing spider silk protein polymerization have an ionic strength greater than 300 mM. Specific examples of ionic compositions for preventing spider silk protein polymerization include combinations of ions greater than 300 mM NaCl, 100 mM phosphate, and ions that have the desired preventative effect against spider silk protein polymerization, such as a combination of 10 mM phosphate and 300 mM NaCl.

The presence of the NT fragment improves solution stability and prevents polymer formation under these conditions. This is advantageous when immediate polymerization may not be ideal, such as during protein purification, in large-scale preparations, or when other conditions need to be optimized. Preferably, the pH of the liquid medium is adjusted to 6.7 or higher, such as 7.0 or higher, or even 8.0 or higher, such as up to 10.5, to achieve high solubility of spider silk proteins. It is also advantageous to adjust the pH of the liquid medium to the range of 6.4–6.8, which provides sufficient solubility for spider silk proteins, but it is beneficial to subsequently adjust the pH to 6.3 or lower.

In the third step, the properties of the liquid medium are adjusted to a pH of 6.3 or lower and an ionic composition that allows polymerization. That is, if the liquid medium for dissolving spider silk has a pH of 6.4 or higher, the pH is lowered to 6.3 or lower. Various methods of achieving this are well known to those skilled in the art, typically involving the addition of a strong or weak acid. If the liquid medium for dissolving spider silk has an ionic composition that prevents polymerization, the ionic composition is altered to allow polymerization. Various methods of achieving this are well known to those skilled in the art, such as dilution, dialysis, or gel filtration. If desired, this step involves lowering the pH of the liquid medium to 6.3 or lower and altering the ionic composition to allow polymerization. Preferably, the pH of the liquid medium is adjusted to 6.2 or lower, such as 6.0 or lower. In particular, it may be advantageous from a practical standpoint to limit the pH reduction from 6.4 or 6.4-6.8 in the previous step to 6.3 or 6.0-6.3 in this step, such as 6.2. In a preferred embodiment, the pH of the liquid medium in this step is 3 or higher, such as 4.2 or higher. The resulting pH range, for example, 4.2–6.3, promotes rapid polymerization.

In the fourth step, spider silk is polymerized in a liquid medium having a pH of 6.3 or lower and an ionic composition that allows for spider silk polymerization. While the presence of the NT fragment improves the solubility of spider silk at pH 6.4 or higher and/or at an ionic composition that prevents spider silk polymerization, it accelerates polymer formation at pH 6.3 or lower when the ionic composition allows for spider silk polymerization. The resulting polymers are preferably solid and macroscopic, and they are formed in a liquid medium having a pH of 6.3 or lower and an ionic composition that allows for spider silk polymerization. In a preferred embodiment, the pH of the liquid medium in this step is 3 or higher, such as 4.2 or higher. The resulting pH range, for example 4.2–6.3, promotes rapid polymerization, and the resulting polymers can be provided at the molecular weights described herein and prepared in solution form, which may be used for article coating if necessary.

Those skilled in the art can readily prepare ionic compositions that allow spider silk protein polymerization using the methods disclosed herein. Preferred ionic compositions allowing spider silk protein polymerization have an ionic strength of less than 300 mM. Specific examples of ionic compositions allowing spider silk protein polymerization include 150 mM NaCl, 10 mM phosphate, 20 mM phosphate, and combinations of these ions that lack preventative effect against spider silk protein polymerization, such as a combination of 10 mM phosphate or 20 mM phosphate and 150 mM NaCl. Preferably, the ionic strength of this liquid medium is adjusted to the range of 1-250 mM.

We do not wish to be confined to any particular theory, but we believe that the NT fragment has two oppositely charged poles, and that changes in environmental pH affect the charge balance on the surface of the protein, which subsequently polymerizes, while salt inhibits the same event.

At neutral pH, the energy expenditure of excess negative charge buried at the acidic pole is expected to prevent polymerization. However, as the dimer approaches its isoelectric point at lower pH, attractive electrostatic forces eventually dominate, explaining the salt- and pH-dependent polymerization characteristics of NTs and NT-containing minispidroins. It has been proposed that, in some embodiments, pH-induced NT polymerization and the enhanced fiber assembly efficiency of NT-minispidroins are attributed to changes in surface electrostatic potential and alterations in the charge balance of acidic residue clusters at one pole of the NT, leading to a polymerization transition at pH 6.3 or lower.

In the fifth step, the preferred solid spider silk protein polymer is separated from the liquid medium. Optionally, this step involves the active removal of lipopolysaccharides and other pyrogens from the spider silk protein polymer.

While not intended to be limited to any particular theory, it has been observed that the formation of spider silk protein polymers proceeds via the formation of water-soluble spider silk protein dimers. This disclosure therefore also provides a method for producing isolated spider silk protein dimers, wherein the first two method steps are as described above. The spider silk protein exists as a dimer in a liquid medium having a pH of 6.4 or higher and/or an ionic composition that prevents said spider silk protein from polymerizing. The third step involves separating the dimer obtained in the second step, and optionally removing lipopolysaccharides and other pyrogens. In a preferred embodiment, the spider silk protein polymer of this disclosure consists of polymerized protein dimers. This disclosure therefore provides novel uses of spider silk protein, preferably those disclosed herein, for the production of spider silk protein dimers.

According to another aspect, this disclosure provides polymers of spider silk proteins as disclosed herein. In one embodiment, such polymers of proteins can be obtained by any of the methods used therein according to this disclosure. Therefore, this disclosure provides recombinant spider silk proteins, preferably those disclosed herein, for various uses in the production of spider silk protein polymers as recombinant silk-based coatings. According to one embodiment, this disclosure provides dimers of spider silk proteins, preferably those disclosed herein, for novel uses in the production of isolated spider silk protein polymers as recombinant silk-based coatings. Among these uses, it is preferred that the polymer be prepared in a liquid medium having a pH of 6.3 or lower and an ionic composition that allows the spider silk proteins to polymerize. In one embodiment, the pH of the liquid medium is 3 or higher, such as 4.2 or higher. The resulting pH range, for example 4.2–6.3, promotes rapid polymerization.

Using one or more methods disclosed herein, the polymerization process can be controlled, and this enables the optimization of parameters to obtain filament polymers with desired properties and shapes.

In one embodiment, the recombinant silk proteins described herein include those described in U.S. Patent 8,642,734, which is incorporated herein by reference in its entirety.

In another embodiment, the recombinant silk fibroin described herein may be prepared according to the method described in U.S. Patent 9,051,453, which is incorporated herein by reference in its entirety.

The amino acid sequence represented by SEQ ID NO:52, also described in U.S. Patent 9,051,453, is equivalent to the amino acid sequence consisting of 50 amino acid residues at the C-terminus of the ADF3 amino acid sequence (NCBI Registry No.: AAC47010, GI: 1263287). The amino acid sequence represented by SEQ ID NO:53, also described in U.S. Patent 9,051,453, is equivalent to the amino acid sequence represented by SEQ ID NO:52, also described in U.S. Patent 9,051,453, with 20 residues removed from the C-terminus. The amino acid sequence represented by SEQ ID NO:54, also described in U.S. Patent 9,051,453, is equivalent to the amino acid sequence represented by SEQ ID NO:52, with 29 residues removed from the C-terminus.

An example of a polypeptide containing a unit of the amino acid sequence represented by Formula 1: REP1-REP2 (1) and having at its C-terminus an amino acid sequence represented by any one of SEQ ID NO: 52 to 54 or an amino acid sequence having 90% or greater homology with any one of the amino acid sequences represented by SEQ ID NO: 52 to 54 (also described in U.S. Patent 9,051,453) is a polypeptide having the amino acid sequence represented by SEQ ID NO: 65 (also described in U.S. Patent 9,051,453, which is incorporated herein by reference in its entirety). The polypeptide having the amino acid sequence represented by SEQ ID NO:65, also described in U.S. Patent 9,051,453, was obtained through the following mutation: In the amino acid sequence of ADF3 (NCBI Accession No.: AAC47010, GI: 1263287)—an amino acid sequence consisting of a start codon, a His 10 tag, and an HRV3C protease (human rhinovirus 3C protease) recognition site (SEQ ID NO:66, also described in U.S. Patent 9,051,453) was added to its N-terminus, substantially doubling the repeat regions from the 1st to the 13th and ending translation at the 1154th amino acid residue. In the polypeptide having the amino acid sequence represented by SEQ ID NO:65, also described in U.S. Patent 9,051,453, the C-terminal sequence is equivalent to the amino acid sequence represented by SEQ ID NO:54.

Furthermore, a polypeptide containing a unit of the amino acid sequence represented by Formula 1:REP1-REP2 (1) and having at its C-terminus an amino acid sequence represented by any one of SEQ ID NO:52 to 54, also described in U.S. Patent 9,051,453, or an amino acid sequence having 90% or greater homology with any one of the amino acid sequences represented by SEQ ID NO:52 to 54, also described in U.S. Patent 9,051,453, may be a protein having an amino acid sequence represented by SEQ ID NO:65, also described in U.S. Patent 9,051,453, wherein one or more amino acids have been substituted, deleted, inserted, and/or added and has a repeating region consisting of crystalline and amorphous regions.

Furthermore, an example of a polypeptide containing two or more units of the amino acid sequence represented by Formula 1:REP1-REP2 (1) is a recombinant protein derived from ADF4 having the amino acid sequence represented by SEQ ID NO:67 (also described in U.S. Patent 9,051,453, which is incorporated herein by reference in its entirety). The amino acid sequence represented by SEQ ID NO:67, also described in U.S. Patent 9,051,453, is an amino acid sequence obtained by adding an amino acid sequence consisting of a start codon, a His 10 tag, and an HRV3C protease (human rhinovirus 3C protease) recognition site (SEQ ID NO:66, also described in U.S. Patent 9,051,453) to the N-terminus of a portion of the amino acid sequence of ADF4 (NCBI Accession No.: AAC47011, GI:1263289) obtained from the NCBI database. Furthermore, a polypeptide containing two or more units of the amino acid sequence represented by Formula 1:REP1-REP2 (1) can be a polypeptide having the amino acid sequence represented by SEQ ID NO:67, also described in U.S. Patent 9,051,453, wherein one or more amino acids have been substituted, deleted, inserted, and/or added and have repeating regions consisting of crystalline and amorphous regions. Additionally, an example of a polypeptide containing two or more units of the amino acid sequence represented by Formula 1:REP1-REP2 (1) is a recombinant protein derived from MaSp2 having the amino acid sequence represented by SEQ ID NO:68 (also described in U.S. Patent 9,051,453, which is incorporated herein by reference in its entirety). The amino acid sequence represented by SEQ ID NO:68, also described in U.S. Patent 9,051,453, is an amino acid sequence obtained by adding an amino acid sequence consisting of a start codon, a His 10 tag, and an HRV3C protease (human rhinovirus 3C protease) recognition site (SEQ ID NO:66, also described in U.S. Patent 9,051,453) to the N-terminus of a partial sequence of MaSp2 (NCBI accession number: AAT75313, GI:50363147) obtained from the NCBI online database. Furthermore, a polypeptide containing two or more units of the amino acid sequence represented by Formula 1: REP1-REP2 (1) can be a polypeptide having the amino acid sequence represented by SEQ ID NO:68, also described in U.S. Patent 9,051,453, wherein one or more amino acids have been substituted, deleted, inserted, and/or added, and it has repeating regions consisting of crystalline and amorphous regions.

Examples of peptides derived from flagellate filament protein include peptides containing 10 or more units of the amino acid sequence represented by Formula 2:REP3(2), preferably peptides containing 20 or more such units, more preferably peptides containing 30 or more such units. When using microorganisms such as *Escherichia coli* as a host to produce recombinant proteins, the molecular weight of the peptides derived from flagellate filament protein is preferably 500 kDa or less, more preferably 300 kDa or less, and even more preferably 200 kDa or less, taking productivity into consideration.

In formula (2), REP 3 refers to the amino acid sequence consisting of Gly-Pro-Gly-Gly-X (SEQ ID NO:69), where X refers to an amino acid selected from Ala, Ser, Tyr and Val.

The main characteristic of spider silk is that whip-like glandular filaments lack crystalline regions but possess repeating regions composed of amorphous areas. Because major drag filaments and the like have repeating regions composed of crystalline and amorphous areas, they are expected to have high stress and tensile strength. Meanwhile, regarding whip-like glandular filaments, although their stress is not as high as that of major drag filaments, their tensile strength is high. This is believed to be because most whip-like glandular filaments are composed of amorphous regions.

Examples of polypeptides containing 10 or more units of the amino acid sequence represented by Formula 2:REP3(2) are recombinant proteins derived from flagellar filament protein having the amino acid sequence represented by SEQ ID NO:70 (also described in U.S. Patent 9,051,453, which is incorporated herein by reference in its entirety). The amino acid sequence represented by SEQ ID NO:70, also described in U.S. Patent 9,051,453, is obtained by combining a partial sequence of the whip-like glandular filament protein from the NCBI database (NCBI accession number: AAF36090, GI:7106224), particularly the amino acid sequence from residue 1220 to 1659 (corresponding to the repeat region and motif) (referred to as the PR1 sequence), with a partial sequence of the whip-like glandular filament protein from the NCBI database (NCBI accession number: AAC38847, GI:2833649), particularly the C-terminal amino acid sequence from residue 816 to 907, and then adding an amino acid sequence consisting of the start codon, His 10 tag, and HRV3C protease recognition site (SEQ ID NO:66, also described in U.S. Patent 9,051,453) to the N-terminus of the combined sequence. In addition, a polypeptide containing 10 or more units of the amino acid sequence represented by Formula 2: REP3(2) may be a polypeptide having the amino acid sequence represented by SEQ ID NO:70, which is also described in U.S. Patent 9,051,453, wherein one or more amino acids have been substituted, deleted, inserted and/or added and have repeating regions composed of amorphous regions.

The polypeptide can be produced using a host transformed with an expression vector containing a gene encoding the polypeptide. The method of gene production is not particularly limited, and it can be cloned by amplifying a gene encoding a natural spider silk protein derived from spider cells using polymerase chain reaction (PCR), or it can be chemically synthesized. The method of chemically synthesizing the gene is also not particularly limited, and it can be synthesized, for example, by ligating oligonucleotides automatically synthesized using AKTA oligopilot plus 10/100 (GE Healthcare Japan) via PCR based on information such as the amino acid sequence of a natural spider silk protein obtained from the NCBI online database. In this case, to facilitate protein purification and observation, a gene encoding a protein with the aforementioned amino acid sequence, having an amino acid sequence with a start codon and a His 10 tag added to its N-terminus, can be synthesized.

Examples of expression vectors include plasmids, bacteriophages, and viruses that can express proteins based on DNA sequences. Plasmid-type expression vectors are not particularly limited, as long as they allow expression of the target gene in the host cell and can amplify themselves. For example, when using *E. coli* Rosetta(DE3) as a host, pET22b(+) plasmid vectors, pCold plasmid vectors, etc., can be used. Among these, the pET22b(+) plasmid vector is preferred considering protein productivity. Examples of hosts include animal cells, plant cells, and microorganisms.

The polypeptides used in this disclosure are preferably polypeptides derived from ADF3, one of the two main silk-dragging proteins of the Orb-weaver spider. The advantages of this polypeptide are that it generally possesses high strength, elongation, and toughness, and is easy to synthesize.

Therefore, the recombinant silk proteins (e.g., recombinant spider silk-based proteins) used according to the embodiments, articles, and/or methods described herein may include one or more of the proteins described above or in U.S. Patents 8,173,772, 8,278,416, 8,618,255, 8,642,734, 8,691,581, 8,729,235, 9,115,204, 9,157,070, 9,309,299, 9,644,012, 9,708,376, 9,051,453, 9,617,315, 9,968,682, 9,689,089, 9,732,125, 9,856,308, 9,926,348, 10,065,997, 10,316,069, and 10, 329,332; and U.S. Patent Publications 2009/0226969, 2011/0281273, 2012/0041177, 2013/0065278, 2013/0115698, 2013/0316376, 2014/0058066, 2014/0079674, 2014/0245923, 20 15/0087046, 2015/0119554, 2015/0141618, 2015/0291673, 2015/0291674, 2015/0239587, 2015/0344542, 2015/0361144, 2015/0374833, 2015/0376247, 2016/0 024464, 2017/0066804, 2017/0066805, 2015/0293076, 2016/0222174, 2017/0283474, 2017/0088675, 2019/0135880, 2015/0329587, 2019/0040109, 2019/01358 81, 2019/0177363, 2019/0225646, 2019/0233481, 2019/0031842, 2018/0355120, 2019/0186050, 2019/0002644, 2020/0031887, 2018/0273590, 20191/094403, 2 019/0031843, 2018/0251501, 2017/0066805, 2018/0127553, 2019/0329526, 2020/0031886, 2018/0080147, 2019/0352349, 2020/0043085, 2019/0144819, 2019/ The recombinant silk proteins listed in 0228449, 2019/0340666, 2020/0000091, 2019/0194710, 2019/0151505, 2018/0265555, 2019/0352330, 2019/0248847 and 2019/0378191 (which are incorporated herein by reference in their entirety) are recombinant silk proteins.

Silk core protein-like protein fragments

The recombinant silk proteins in this disclosure comprise synthetic proteins based on repeating units of natural silk proteins. In addition to the synthetic repeating silk protein sequences, these may additionally comprise one or more natural non-repetitive silk protein sequences. As used herein, a “silkcore-like protein fragment” refers to a protein fragment having the molecular weight and polydispersity as defined herein and a degree of homology to a protein selected from natural silk proteins, silkcore heavy chains, silkcore light chains, or any protein containing one or more six-amino acid repeating units of GAGAGS (SEQ ID NO: 2). In some implementations, the degree of homology is selected from about 99%, about 98%, about 97%, about 96%, about 95%, about 94%, about 93%, about 92%, about 91%, about 90%, about 89%, about 88%, about 87%, about 86%, about 85%, about 84%, about 83%, about 82%, about 81%, about 80%, about 79%, about 78%, about 77%, about 76%, about 75%, or less than 75%.

As described herein, proteins such as natural silk fibroin, silken protein heavy chain, silken protein light chain, or any protein containing one or more six-amino acid repeating units of GAGAGS (SEQ ID NO:2) contain about 9% to about 45% glycine, or about 9% glycine, or about 10% glycine, about 43% glycine, about 44% glycine, about 45% glycine, or about 46% glycine. As described herein, proteins such as natural silk fibroin, silken protein heavy chain, silken protein light chain, or any protein containing one or more six-amino acid repeating units of GAGAGS (SEQ ID NO:2) contain about 13% to about 30% alanine, or about 13% alanine, or about 28% alanine, or about 29% alanine, or about 30% alanine, or about 31% alanine. As described herein, proteins such as natural silk proteins, silken protein heavy chains, silken protein light chains, or any protein containing one or more GAGAGS (SEQ ID NO:2) six-amino acid repeating units contain 9% to about 12% serine, or about 9% serine, or about 10% serine, or about 11% serine, or about 12% serine.

In some embodiments, the filamentous protein-like protein described herein comprises about 5%, about 6%, about 7%, about 8%, about 9%, about 10%, about 11%, about 12%, about 13%, about 14%, about 15%, about 16%, about 17%, about 18%, about 19%, about 20%, about 21%, about 22%, about 23%, about 24%, about 25%, about 26%, about 27%, about 28%, etc. Glycine at approximately 29%, 30%, 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, 41%, 42%, 43%, 44%, 45%, 46%, 47%, 48%, 49%, 50%, 51%, 52%, 53%, 54%, or 55%. In some embodiments, the silken protein-like protein described herein comprises about 13%, about 14%, about 15%, about 16%, about 17%, about 18%, about 19%, about 20%, about 21%, about 22%, about 23%, about 24%, about 25%, about 26%, about 27%, about 28%, about 29%, about 30%, about 31%, about 32%, about 33%, about 34%, about 35%, about 36%, about 37%, about 38%, or about 39% alanine. In some embodiments, the silken protein-like protein described herein comprises about 2%, about 3%, about 4%, about 5%, about 6%, about 7%, about 8%, about 9%, about 10%, about 11%, about 12%, about 13%, about 14%, about 15%, about 16%, about 17%, about 18%, about 19%, about 20%, about 21%, or about 22% serine. In some embodiments, the silken protein-like protein described herein may independently contain any amino acid known to be contained in natural silken protein. In some embodiments, the silken protein-like protein described herein may independently not contain any amino acid known to be contained in natural silken protein. In some embodiments, an average of 2/6, 3/6, or 4/6 of the amino acids in the silken protein-like protein described herein are glycine. In some embodiments, an average of 1/6, 2/6, or 3/6 of the amino acids in the silken protein-like protein described herein are alanine. In some embodiments, an average of 0/6, 1/6, or 2/6 of the amino acids in the filamentous protein-like protein described herein are serine.

Sericin or sericin fragments

The main body of raw silk is sericin fiber, which is coated with sericin, an adhesive substance. Sericin is a gelatinous silk protein that covers the surface of the silk thread and is composed of chemically reactive, sterically hindered amino acids (such as serine, threonine, aspartic acid, glycine, and alanine). In the various processes of producing silk from raw silk, sericin plays a crucial role in controlling the dissolution of the silk and producing high-quality silk. Furthermore, it plays an extremely important role as an adhesive functional protein. When silk fibers are used as clothing materials, most of the sericin covering the thread is removed and discarded, thus sericin is a valuable untapped resource.

In some embodiments, the silk fibroin fragments described herein include sericin or sericin fragments. Methods for preparing sericin or sericin fragments and their applications in various fields are known and described herein, and are also described, for example, in U.S. Patents 7,115,388, 7,157,273, and 9,187,538, all of which are incorporated herein by reference in their entirety.

In some embodiments, sericin, such as that removed from raw silk cocoons during a degumming step, can be collected and used in the methods described herein. Sericin can also be reconstituted from powder and used in the compositions and methods disclosed herein.

Other properties of SPF

The composition of this disclosure is "biocompatible" or exhibits "biocompatibility" meaning that the composition is compatible with living tissue or living systems because it is non-toxic, harmless, or physiologically non-reactive and does not cause immune rejection or inflammatory response. Such biocompatibility can be demonstrated by the duration of topical application of the composition of this disclosure to the skin by participants for an extended period of time. In one embodiment, the extended period of time is about 3 days. In one embodiment, the extended period of time is about 7 days. In one embodiment, the extended period of time is about 14 days. In one embodiment, the extended period of time is about 21 days. In one embodiment, the extended period of time is about 30 days. In one embodiment, the extended period of time is selected from the group consisting of about 1 month, about 2 months, about 3 months, about 4 months, about 5 months, about 6 months, about 7 months, about 8 months, about 9 months, about 10 months, about 11 months, about 12 months, and indefinite. For example, in some embodiments, the coating described herein is a biocompatible coating.

In some embodiments, the compositions described herein (which may be biocompatible compositions) (e.g., biocompatible coatings containing filaments) can be evaluated in accordance with the international standard ISO 10993-1 entitled "Biological evaluation of medical devices – Part 1: Evaluation and testing within a risk management process". In some embodiments, the compositions described herein (which may be biocompatible compositions) can be evaluated according to ISO 106993-1 for one or more of the following: cytotoxicity, sensitization, blood compatibility, pyrogenicity, implantation, genotoxicity, carcinogenicity, reproductive and developmental toxicity, and degradation.

The compositions disclosed herein are "hypoallergenic," meaning they are relatively unlikely to cause allergic reactions. This hypoallergenicity can be demonstrated by the extended period of time for which participants have topically applied the compositions of this disclosure to their skin. In one embodiment, the extended period is about 3 days. In one embodiment, the extended period is about 7 days. In one embodiment, the extended period is about 14 days. In one embodiment, the extended period is about 21 days. In one embodiment, the extended period is about 30 days. In one embodiment, the extended period is selected from the group consisting of: about 1 month, about 2 months, about 3 months, about 4 months, about 5 months, about 6 months, about 7 months, about 8 months, about 9 months, about 10 months, about 11 months, about 12 months, and indefinite.

In one embodiment, the stability of the composition of this disclosure is about 1 day. In one embodiment, the stability of the composition of this disclosure is about 2 days. In one embodiment, the stability of the composition of this disclosure is about 3 days. In one embodiment, the stability of the composition of this disclosure is about 4 days. In one embodiment, the stability of the composition of this disclosure is about 5 days. In one embodiment, the stability of the composition of this disclosure is about 6 days. In one embodiment, the stability of the composition of this disclosure is about 7 days. In one embodiment, the stability of the composition of this disclosure is about 8 days. In one embodiment, the stability of the composition of this disclosure is about 9 days. In one embodiment, the stability of the composition of this disclosure is about 10 days.

In one embodiment, the stability of the composition disclosed herein is about 11 days, about 12 days, about 13 days, about 14 days, about 15 days, about 16 days, about 17 days, about 18 days, about 19 days, about 20 days, about 21 days, about 22 days, about 23 days, about 24 days, about 25 days, about 26 days, about 27 days, about 28 days, about 29 days, or about 30 days.

In one embodiment, the stability of the disclosed composition is from 10 days to 6 months. In one embodiment, the stability of the disclosed composition is from 6 months to 12 months. In one embodiment, the stability of the disclosed composition is from 12 months to 18 months. In one embodiment, the stability of the disclosed composition is from 18 months to 24 months. In one embodiment, the stability of the disclosed composition is from 24 months to 30 months. In one embodiment, the stability of the disclosed composition is from 30 months to 36 months. In one embodiment, the stability of the disclosed composition is from 36 months to 48 months. In one embodiment, the stability of the disclosed composition is from 48 months to 60 months.

In one embodiment, the SPF composition of this disclosure is insoluble in aqueous solution due to the crystallinity of the protein. In one embodiment, the SPF composition of this disclosure is soluble in aqueous solution. In one embodiment, the SPF of the composition of this disclosure comprises about 2/3 crystalline portion and about 1/3 amorphous region. In one embodiment, the SPF of the composition of this disclosure comprises about half crystalline portion and about half amorphous region. In one embodiment, the SPF of the composition of this disclosure comprises 99% crystalline portion and 1% amorphous region. In one embodiment, the SPF of the composition of this disclosure comprises 95% crystalline portion and 5% amorphous region. In one embodiment, the SPF of the composition of this disclosure comprises 90% crystalline portion and 10% amorphous region. In one embodiment, the SPF of the composition of this disclosure comprises 85% crystalline portion and 15% amorphous region. In one embodiment, the SPF of the composition of this disclosure comprises 80% crystalline portion and 20% amorphous region. In one embodiment, the SPF of the composition of this disclosure comprises 75% crystalline portion and 25% amorphous region. In one embodiment, the SPF of the disclosed composition comprises 70% crystalline portion and 30% amorphous region. In one embodiment, the SPF of the disclosed composition comprises 65% crystalline portion and 35% amorphous region. In one embodiment, the SPF of the disclosed composition comprises 60% crystalline portion and 40% amorphous region. In one embodiment, the SPF of the disclosed composition comprises 50% crystalline portion and 50% amorphous region. In one embodiment, the SPF of the disclosed composition comprises 40% crystalline portion and 60% amorphous region. In one embodiment, the SPF of the disclosed composition comprises 35% crystalline portion and 65% amorphous region. In one embodiment, the SPF of the disclosed composition comprises 30% crystalline portion and 70% amorphous region. In one embodiment, the SPF of the disclosed composition comprises 25% crystalline portion and 75% amorphous region. In one embodiment, the SPF of the disclosed composition comprises 20% crystalline portion and 80% amorphous region. In one embodiment, the SPF of the disclosed composition comprises 15% crystalline portion and 85% amorphous region. In one embodiment, the SPF of the compositions disclosed herein comprises 10% crystalline portion and 90% amorphous portion. In one embodiment, the SPF of the compositions disclosed herein comprises 5% crystalline portion and 90% amorphous portion. In one embodiment, the SPF of the compositions disclosed herein comprises 1% crystalline portion and 99% amorphous portion.

As used herein, the term "substantially free of inorganic residues" means that the composition exhibits 0.1% (w/w) or less of residues. In one embodiment, substantially free of inorganic residues means a composition exhibiting 0.05% (w/w) or less of residues. In one embodiment, substantially free of inorganic residues means a composition exhibiting 0.01% (w/w) or less of residues. In one embodiment, the amount of inorganic residue is from 0 ppm ("undetectable" or "ND") to 1000 ppm. In one embodiment, the amount of inorganic residue is from ND to about 500 ppm. In one embodiment, the amount of inorganic residue is from ND to about 400 ppm. In one embodiment, the amount of inorganic residue is from ND to about 300 ppm. In one embodiment, the amount of inorganic residue is from ND to about 200 ppm. In one embodiment, the amount of inorganic residue is from ND to about 100 ppm. In one embodiment, the amount of inorganic residue is from 10 ppm to 1000 ppm.

As used herein, the term "substantially free of inorganic residues" means that the composition exhibits 0.1% (w/w) or less of residues. In one embodiment, substantially free of inorganic residues means that the composition exhibits 0.05% (w/w) or less of residues. In one embodiment, substantially free of organic residues means that the composition exhibits 0.01% (w/w) or less of residues. In one embodiment, the amount of organic residues is from 0 ppm ("undetectable" or "ND") to 1000 ppm. In one embodiment, the amount of organic residues is from ND to about 500 ppm. In one embodiment, the amount of organic residues is from ND to about 400 ppm. In one embodiment, the amount of organic residues is from ND to about 300 ppm. In one embodiment, the amount of organic residues is from ND to about 200 ppm. In one embodiment, the amount of organic residues is from ND to about 100 ppm. In one embodiment, the amount of organic residues is from 10 ppm to 1000 ppm.

The compositions disclosed herein exhibit "biocompatibility," meaning that they are compatible with living tissues or living systems because they are non-toxic, harmless, or physiologically non-reactive and do not cause immune rejection. Such biocompatibility can be demonstrated by the duration of topical application of the compositions disclosed herein to the skin by participants. In one embodiment, the duration of extension is about 3 days. In one embodiment, the duration of extension is about 7 days; in another embodiment, about 14 days; in yet another embodiment, about 21 days; and in one embodiment, about 30 days. In one embodiment, the duration of extension is selected from the group consisting of about 1 month, about 2 months, about 3 months, about 4 months, about 5 months, about 6 months, about 7 months, about 8 months, about 9 months, about 10 months, about 11 months, about 12 months, and indefinite.

The compositions disclosed herein are "hypoallergenic," meaning they are relatively unlikely to cause allergic reactions. This hypoallergenicity can be demonstrated by the extended period of time for which participants have topically applied the compositions of this disclosure to their skin. In one embodiment, the extended period is about 3 days. In one embodiment, the extended period is about 7 days. In one embodiment, the extended period is about 14 days. In one embodiment, the extended period is about 21 days. In one embodiment, the extended period is about 30 days. In one embodiment, the extended period is selected from the group consisting of: about 1 month, about 2 months, about 3 months, about 4 months, about 5 months, about 6 months, about 7 months, about 8 months, about 9 months, about 10 months, about 11 months, about 12 months, and indefinite.

The following are non-limiting examples of suitable ranges of parameters used in the preparation of the silk solutions of this disclosure. The silk solutions of this disclosure may include one or more, but not all, of these parameters, and may be prepared using various combinations of such ranges of parameters.

In one embodiment, the SPF percentage in the solution is less than 30.0% by weight. In one embodiment, the SPF percentage in the solution is less than 25.0% by weight. In one embodiment, the SPF percentage in the solution is less than 20.0% by weight. In one embodiment, the SPF percentage in the solution is less than 19.0% by weight. In one embodiment, the SPF percentage in the solution is less than 18.0% by weight. In one embodiment, the SPF percentage in the solution is less than 17.0% by weight. In one embodiment, the SPF percentage in the solution is less than 16.0% by weight. In one embodiment, the SPF percentage in the solution is less than 15.0% by weight. In one embodiment, the SPF percentage in the solution is less than 14.0% by weight. In one embodiment, the SPF percentage in the solution is less than 13.0% by weight. In one embodiment, the SPF percentage in the solution is less than 12.0% by weight. In one embodiment, the SPF percentage in the solution is less than 11.0% by weight. In one embodiment, the SPF percentage in the solution is less than 10.0% by weight. In one embodiment, the SPF percentage in the solution is less than 9.0% by weight. In one embodiment, the SPF percentage in the solution is less than 8.0% by weight. In one embodiment, the SPF percentage in the solution is less than 7.0% by weight. In one embodiment, the SPF percentage in the solution is less than 6.0% by weight. In one embodiment, the SPF percentage in the solution is less than 5.0% by weight. In one embodiment, the SPF percentage in the solution is less than 4.0% by weight. In one embodiment, the SPF percentage in the solution is less than 3.0% by weight. In one embodiment, the SPF percentage in the solution is less than 2.0% by weight. In one embodiment, the SPF percentage in the solution is less than 1.0% by weight. In one embodiment, the SPF percentage in the solution is less than 0.9% by weight. In one embodiment, the SPF percentage in the solution is less than 0.8% by weight. In one embodiment, the SPF percentage in the solution is less than 0.7% by weight. In one embodiment, the SPF percentage in the solution is less than 0.6% by weight. In one embodiment, the SPF percentage in the solution is less than 0.5% by weight. In one embodiment, the SPF percentage in the solution is less than 0.4% by weight. In one embodiment, the SPF percentage in the solution is less than 0.3% by weight. In one embodiment, the SPF percentage in the solution is less than 0.2% by weight. In one embodiment, the SPF percentage in the solution is less than 0.1% by weight.

In one embodiment, the SPF percentage in the solution is greater than 0.1 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.2 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.3 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.4 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.5 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.6 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.7 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.8 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.9 wt%. In one embodiment, the SPF percentage in the solution is greater than 1.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 2.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 3.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 4.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 5.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 6.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 7.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 8.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 9.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 10.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 11.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 12.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 13.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 14.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 15.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 16.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 17.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 18.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 19.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 20.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 25.0% by weight.

In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 30.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 25.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 20.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 15.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 10.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 9.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 8.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 7.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 6.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 6.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 5.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 5.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 4.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 4.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 3.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 3.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 2.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 2.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 2.4 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.5 wt% to about 5.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.5 wt% to about 4.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.5 wt% to about 4.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.5 wt% to about 3.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.5 wt% to about 3.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.5 wt% to about 2.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 1.0 wt% to about 4.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 1.0 wt% to about 3.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 1.0 wt% to about 3.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 1.0 wt% to about 2.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 1.0 wt% to about 2.4 wt%. In one embodiment, the SPF percentage in the solution ranges from about 1.0 wt% to about 2.0 wt%.

In one embodiment, the SPF percentage in the solution ranges from about 20.0 wt% to about 30.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 10.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 1.0 wt% to about 10.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 2 wt% to about 10.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 6.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 6.0 wt% to about 10.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 6.0 wt% to about 8.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 6.0 wt% to about 9.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 10.0 wt% to about 20.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 11.0 wt% to about 19.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 12.0 wt% to about 18.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 13.0 wt% to about 17.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 14.0 wt% to about 16.0 wt%. In one embodiment, the SPF percentage in the solution is about 1.0 wt%. In one embodiment, the SPF percentage in the solution is about 0.5 wt%. In one embodiment, the SPF percentage in the solution is about 1.5 wt%. In one embodiment, the SPF percentage in the solution is about 2.0 wt%. In one embodiment, the SPF percentage in the solution is about 2.4 wt%. In one embodiment, the SPF percentage in the solution is 3.0 wt%. In one embodiment, the SPF percentage in the solution is 3.5 wt%. In one embodiment, the SPF percentage in the solution is about 4.0 wt%. In one embodiment, the SPF percentage in the solution is about 4.5 wt%. In one embodiment, the SPF percentage in the solution is about 5.0 wt%. In one embodiment, the SPF percentage in the solution is about 5.5 wt%. In one embodiment, the SPF percentage in the solution is about 6.0% by weight. In one embodiment, the SPF percentage in the solution is about 6.5% by weight. In one embodiment, the SPF percentage in the solution is about 7.0% by weight. In one embodiment, the SPF percentage in the solution is about 7.5% by weight. In one embodiment, the SPF percentage in the solution is about 8.0% by weight. In one embodiment, the SPF percentage in the solution is about 8.5% by weight. In one embodiment, the SPF percentage in the solution is about 9.0% by weight. In one embodiment, the SPF percentage in the solution is about 9.5% by weight. In one embodiment, the SPF percentage in the solution is about 10.0% by weight.

In one embodiment, the percentage of sericin in the solution is less than detectable to 25.0% by weight. In one embodiment, the percentage of sericin in the solution is less than detectable to 5.0% by weight. In one embodiment, the percentage of sericin in the solution is 1.0% by weight. In one embodiment, the percentage of sericin in the solution is 2.0% by weight. In one embodiment, the percentage of sericin in the solution is 3.0% by weight. In one embodiment, the percentage of sericin in the solution is 4.0% by weight. In one embodiment, the percentage of sericin in the solution is 5.0% by weight. In one embodiment, the percentage of sericin in the solution is 10.0% by weight. In one embodiment, the percentage of sericin in the solution is 25.0% by weight.

In some embodiments, the filament protein fragments of this disclosure are storage stable (they do not slowly or spontaneously gel when stored in aqueous solution and do not aggregate over time, thus the molecular weight does not increase) for 10 days to 3 years, depending on storage conditions, SPF percentage, and number and shipping conditions. Additionally, the pH can be altered to extend shelf life and/or support shipping conditions by preventing premature folding and aggregation of the filaments. In one embodiment, the stability of the LiBr-filament fragment solution is 0 to 1 year. In one embodiment, the stability of the LiBr-filament fragment solution is 0 to 2 years. In one embodiment, the stability of the LiBr-filament fragment solution is 0 to 3 years. In one embodiment, the stability of the LiBr-filament fragment solution is 0 to 4 years. In one embodiment, the stability of the LiBr-filament fragment solution is 0 to 5 years. In one embodiment, the stability of the LiBr-filament fragment solution is 1 to 2 years. In one embodiment, the stability of the LiBr-filament fragment solution is 1 to 3 years. In one embodiment, the stability of the LiBr-filament fragment solution is 1 to 4 years. In one embodiment, the stability of the LiBr-filament fragment solution is 1 to 5 years. In one embodiment, the stability of the LiBr-filament fragment solution is 2 to 3 years. In another embodiment, the stability of the LiBr-filament fragment solution is 2 to 4 years. In another embodiment, the stability of the LiBr-filament fragment solution is 2 to 5 years. In another embodiment, the stability of the LiBr-filament fragment solution is 3 to 4 years. In yet another embodiment, the stability of the LiBr-filament fragment solution is 3 to 5 years. In yet another embodiment, the stability of the LiBr-filament fragment solution is 4 to 5 years.

In one embodiment, the stability of the disclosed composition is from 10 days to 6 months. In one embodiment, the stability of the disclosed composition is from 6 months to 12 months. In one embodiment, the stability of the disclosed composition is from 12 months to 18 months. In one embodiment, the stability of the disclosed composition is from 18 months to 24 months. In one embodiment, the stability of the disclosed composition is from 24 months to 30 months. In one embodiment, the stability of the disclosed composition is from 30 months to 36 months. In one embodiment, the stability of the disclosed composition is from 36 months to 48 months. In one embodiment, the stability of the disclosed composition is from 48 months to 60 months.

In one embodiment, the composition of this disclosure having an SPF has an undetectable level of LiBr residue. In one embodiment, the amount of LiBr residue in the composition of this disclosure is from 10 ppm to 1000 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is from 10 ppm to 300 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is less than 25 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is less than 50 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is less than 75 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is less than 100 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is less than 200 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is less than 300 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is less than 400 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is less than 500 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is less than 600 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is less than 700 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is less than 800 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is less than 900 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is less than 1000 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is undetectable to 500 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is undetectable to 450 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is undetectable to 400 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is undetectable to 350 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is undetectable to 300 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is undetectable to 250 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is undetectable to 200 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is undetectable to 150 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is undetectable to 100 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is 100 ppm to 200 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is 200 ppm to 300 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is 300 ppm to 400 ppm. In one embodiment, the amount of LiBr residue in the composition of this disclosure is 400 ppm to 500 ppm.

In one embodiment, the composition of this disclosure having an SPF has an undetectable level of _Na₂CO₃ residue. In one embodiment, the amount of _Na₂CO₃ residue in the composition of this disclosure is less than 100 ppm. In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure _is less than 200 ppm. In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is less than 300 _ppm . In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is less than 400 ppm. In one embodiment, the amount of _Na₂CO₃ residue in the composition of this disclosure is less than 500 _ppm . In one embodiment, the amount of _Na₂CO₃ residue in the composition of this disclosure is less than 600 ppm. In one embodiment, the amount of _Na₂CO₃ residue in the composition of this disclosure is less than 700 ppm. In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is less than 800 ppm. In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure _is less than 900 _ppm . In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is less than 1000 ppm. In one embodiment, the amount of _Na₂CO₃ residue in _the composition of this disclosure is undetectable to 500 ppm. In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is undetectable to 450 ppm. In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is undetectable to 400 ppm. In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is undetectable to 350 ppm. In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is undetectable to 300 ppm. In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is undetectable to 250 ppm. In one embodiment, the amount of _Na₂CO₃ residue in the composition of this disclosure is undetectable to 200 ppm. In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is undetectable to 150 _ppm . In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is undetectable to 100 ppm. In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is 100 ppm to 200 ppm. In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is 200 ppm to 300 ppm. In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is 300 ppm to 400 ppm. In one embodiment, the amount of _{Na₂CO₃ residue} in the composition of this disclosure is 400 ppm to 500 ppm.

A unique feature of the SPF compositions disclosed herein is their storage stability from 10 days to 3 years (they do not slowly or spontaneously gel when stored in aqueous solutions and do not aggregate over time, thus the molecular weight does not increase), depending on storage conditions, filament percentage, and number and shipping conditions. Additionally, the pH can be altered to extend shelf life and/or support shipping conditions by preventing premature folding and aggregation of the filaments. In one embodiment, the SPF solution compositions of this disclosure have storage stability for up to 2 weeks at room temperature (RT). In one embodiment, the SPF solution compositions of this disclosure have storage stability for up to 4 weeks at room temperature. In one embodiment, the SPF solution compositions of this disclosure have storage stability for up to 6 weeks at room temperature. In one embodiment, the SPF solution compositions of this disclosure have storage stability for up to 8 weeks at room temperature. In one embodiment, the SPF solution compositions of this disclosure have storage stability for up to 10 weeks at room temperature. In one embodiment, the SPF solution compositions of this disclosure have storage stability for up to 12 weeks at room temperature. In one embodiment, the SPF solution compositions of this disclosure have storage stability for about 4 weeks to about 52 weeks at room temperature.

Table R below shows the storage stability test results of embodiments of the SPF compositions of this disclosure.

In some implementations, the water solubility of silk membranes derived from the silk core protein fragments described herein can be altered by solvent annealing (water annealing or methanol annealing), chemical crosslinking, enzymatic crosslinking, and heat treatment.

In some embodiments, the annealing process may involve initiating β-sheet formation in a solution of fibrous protein fragments used as a coating material. Techniques for annealing (e.g., increasing crystallinity) or otherwise promoting the “molecular stacking” of fibrous protein-based fragments have been described. In some embodiments, amorphous fibrous membranes are annealed in the presence of a solvent selected from water or organic solvents to introduce β-sheets. In some embodiments, amorphous fibrous membranes are annealed in the presence of water to introduce β-sheets (water annealing). In some embodiments, amorphous fibrous protein fragment membranes are annealed in the presence of methanol to introduce β-sheets. In some embodiments, annealing (e.g., β-sheet formation) is initiated by adding an organic solvent. Suitable organic solvents include, but are not limited to, methanol, ethanol, acetone, isopropanol, or combinations thereof.

In some embodiments, annealing is performed via so-called “water annealing” or “vapor annealing,” in which steam is used as an intermediate plasticizer or catalyst to promote the stacking of β-sheets. In some embodiments, water annealing can be performed under vacuum. Suitable methods of this kind have been described in Jin H-J et al. (2005), Water-stable Silk Films with Reduced Beta-Sheet Content, Advanced Functional Materials, 15:1241-1247; Xiao H et al. (2011), Regulation of Silk Material Structure by Temperature-Controlled Water Vapor Annealing, Biomacromolecules, 12(5):1686-1696.

A key feature of water annealing is the driving formation of crystalline β-sheets in the filamentin fragment peptide chains, enabling the filamentin to self-assemble into a continuous membrane. In some embodiments, the crystallinity of the filamentin fragment membrane is controlled by adjusting the temperature of the water vapor and the annealing duration. In some embodiments, annealing is performed at a temperature of about 65°C to about 110°C. In some embodiments, the water temperature is maintained at about 80°C, and annealing is performed at a temperature selected from about 65°C, about 70°C, about 75°C, about 80°C, about 85°C, about 90°C, about 95°C, about 100°C, about 105°C, and about 110°C.

In some embodiments, the annealing process lasts for a duration selected from the following time periods: approximately 1 minute to approximately 40 minutes, approximately 1 minute to approximately 50 minutes, approximately 1 minute to approximately 60 minutes, approximately 1 minute to approximately 70 minutes, approximately 1 minute to approximately 80 minutes, approximately 1 minute to approximately 90 minutes, approximately 1 minute to approximately 100 minutes, approximately 1 minute to approximately 110 minutes, approximately 1 minute to approximately 120 minutes, approximately 1 minute to approximately 130 minutes, approximately 5 minutes to approximately 40 minutes, approximately 5 minutes to approximately 50 minutes, approximately 5 minutes to approximately 60 minutes, approximately 5 minutes to approximately 70 minutes, approximately 5 minutes to approximately 80 minutes, approximately 5 minutes to approximately 90 minutes, approximately 5 minutes to approximately 100 minutes, approximately 5 minutes to approximately 110 minutes, approximately 5 minutes to approximately 120 minutes, approximately 5 minutes to approximately 130 minutes, approximately 10 minutes to approximately 40 minutes, approximately 10 minutes to approximately 50 minutes, approximately 10 minutes to approximately 60 minutes, approximately 10 minutes to approximately 70 minutes. Clock, approximately 10 minutes to approximately 80 minutes, approximately 10 minutes to approximately 90 minutes, approximately 10 minutes to approximately 100 minutes, approximately 10 minutes to approximately 110 minutes, approximately 10 minutes to approximately 120 minutes, approximately 10 minutes to approximately 130 minutes, approximately 15 minutes to approximately 40 minutes, approximately 15 minutes to approximately 50 minutes, approximately 15 minutes to approximately 60 minutes, approximately 15 minutes to approximately 70 minutes, approximately 15 minutes to approximately 80 minutes, approximately 15 minutes to approximately 90 minutes, approximately 15 minutes to approximately 100 minutes, approximately 15 minutes to approximately 110 minutes, approximately 15 minutes to approximately 120 minutes, approximately 15 minutes to approximately 130 minutes, approximately 20 minutes to approximately 40 minutes, approximately 20 minutes to approximately 50 minutes, approximately 20 minutes to approximately 60 minutes, approximately 20 minutes to approximately 70 minutes, approximately 20 minutes to approximately 80 minutes, approximately 20 minutes to approximately 90 minutes, approximately 20 minutes to approximately 100 minutes, approximately 20 minutes to approximately 110 minutes, approximately 20 minutes to approximately 120 minutes, approximately 20 minutes to approximately 130 minutes, approximately 25 minutes to approximately 40 minutes, approximately 25 minutes to approximately 50 minutes, approximately 25 minutes to approximately 60 minutes, approximately 25 minutes to approximately 70 minutes, approximately 25 minutes to approximately 80 minutes, approximately 25 minutes to approximately 90 minutes, approximately 25 minutes to approximately 100 minutes, approximately 25 minutes to approximately 110 minutes, approximately 25 minutes to approximately 120 minutes, approximately 25 minutes to approximately 130 minutes, approximately 30 minutes to approximately 40 minutes, approximately 30 minutes to approximately 50 minutes, approximately 30 minutes to approximately 60 minutes, approximately 30 minutes to approximately 70 minutes, approximately 30 minutes to approximately 80 minutes, approximately 30 minutes to approximately 90 minutes, approximately 30 minutes to approximately 100 minutes, approximately 30 minutes to approximately 110 minutes, approximately 30 minutes to approximately 120 minutes, approximately 30 minutes to approximately 130 minutes, approximately 35 minutes to approximately 40 minutes, approximately 35 minutes to approximately 50 minutes, approximately 35 minutes to approximately 60 minutes, approximately 35 minutes Approximately 70 minutes, approximately 35 minutes to approximately 80 minutes, approximately 35 minutes to approximately 90 minutes, approximately 35 minutes to approximately 100 minutes, approximately 35 minutes to approximately 110 minutes, approximately 35 minutes to approximately 120 minutes, approximately 35 minutes to approximately 130 minutes, approximately 40 minutes to approximately 50 minutes, approximately 40 minutes to approximately 60 minutes, approximately 40 minutes to approximately 70 minutes, approximately 40 minutes to approximately 80 minutes, approximately 40 minutes to approximately 90 minutes, approximately 40 minutes to approximately 100 minutes, approximately 40 minutes to approximately 110 minutes, approximately 40 minutes to approximately 120 minutes, approximately 40 minutes to approximately 130 minutes, approximately 45 minutes to approximately 50 minutes, approximately 45 minutes to approximately 60 minutes, approximately 45 minutes to approximately 70 minutes, approximately 45 minutes to approximately 80 minutes, approximately 45 minutes to approximately 90 minutes, approximately 45 minutes to approximately 100 minutes, approximately 45 minutes to approximately 110 minutes, approximately 45 minutes to approximately 120 minutes, and approximately 45 minutes to approximately 130 minutes. In some embodiments, the annealing process lasts for a period of approximately 1 minute to approximately 60 minutes. In some embodiments, the annealing process lasts for a period of approximately 45 minutes to approximately 60 minutes. The longer water annealing post-treatment corresponds to increased crystallinity of the fimbriae fragments.

In some embodiments, the annealed fibrous protein fragment membrane is prepared by immersing a wet fibrous protein fragment membrane in 100% methanol at room temperature for 60 minutes. Methanol annealing transforms the composition of the fibrous protein fragment membrane from a predominantly amorphous random coil to a crystalline antiparallel β-sheet structure.

In some embodiments, SPF as described herein can be used to prepare SPF microparticles by precipitation with methanol. Alternative flash drying, fluidized bed drying, spray drying, or vacuum drying can be applied to remove water from the silk solution. The SPF powder can then be stored and handled without refrigeration or other special treatment procedures. In some embodiments, the SPF powder comprises low molecular weight silk core protein fragments. In some embodiments, the SPF powder comprises medium molecular weight silk core protein fragments. In some embodiments, the SPF powder comprises a mixture of low molecular weight and medium molecular weight silk core protein fragments.

As used herein, the terms "substantially sericin-free" or "substantially sericin-free" refer to silk fibers in which most of the sericin has been removed. In one embodiment, substantially sericin-free sericin refers to sericin having about 0.01 wt% to about 10.0 wt% sericin. In one embodiment, substantially sericin-free sericin refers to sericin having about 0.01 wt% to about 9.0 wt% sericin. In one embodiment, substantially sericin-free sericin refers to sericin having about 0.01 wt% to about 8.0 wt% sericin. In one embodiment, substantially sericin-free sericin refers to sericin having about 0.01 wt% to about 7.0 wt% sericin. In one embodiment, substantially sericin-free sericin refers to sericin having about 0.01 wt% to about 6.0 wt% sericin. In one embodiment, substantially sericin-free sericin refers to sericin having about 0.01 wt% to about 5.0 wt% sericin. In one embodiment, a silk core protein that is substantially free of sericin refers to a silk core protein having about 0% to about 4.0% by weight of sericin. In one embodiment, a silk core protein that is substantially free of sericin refers to a silk core protein having about 0.05% to about 4.0% by weight of sericin. In one embodiment, a silk core protein that is substantially free of sericin refers to a silk core protein having about 0.1% to about 4.0% by weight of sericin. In one embodiment, a silk core protein that is substantially free of sericin refers to a silk core protein having about 0.5% to about 4.0% by weight of sericin. In one embodiment, a silk core protein that is substantially free of sericin refers to a silk core protein having about 1.0% to about 4.0% by weight of sericin. In one embodiment, a silk core protein that is substantially free of sericin refers to a silk core protein having about 1.5% to about 4.0% by weight of sericin. In one embodiment, a silk core protein that is substantially free of sericin refers to a silk core protein having about 2.0% to about 4.0% by weight of sericin. In one embodiment, a silk core protein that is substantially free of sericin refers to a silk core protein having a sericin content of about 2.5% to about 4.0% by weight. In one embodiment, a silk core protein that is substantially free of sericin refers to a silk core protein having a sericin content of about 0.01% to about 0.1% by weight. In one embodiment, a silk core protein that is substantially free of sericin refers to a silk core protein having a sericin content of less than about 0.1% by weight. In one embodiment, a silk core protein that is substantially free of sericin refers to a silk core protein having a sericin content of less than about 0.05% by weight. In one embodiment, when the silk source is added to a boiling (100°C) aqueous sodium carbonate solution for a treatment time of about 30 minutes to about 60 minutes, a degumming loss of about 26.0% to about 31.0% by weight is obtained.

The following are non-limiting examples of suitable ranges of parameters used in the preparation of the silk solutions of this disclosure. The silk solutions of this disclosure may include one or more, but not all, of these parameters, and may be prepared using various combinations of such ranges of parameters.

In one embodiment, the SPF percentage in the solution is less than 30.0% by weight. In one embodiment, the SPF percentage in the solution is less than 25.0% by weight. In one embodiment, the SPF percentage in the solution is less than 20.0% by weight. In one embodiment, the SPF percentage in the solution is less than 19.0% by weight. In one embodiment, the SPF percentage in the solution is less than 18.0% by weight. In one embodiment, the SPF percentage in the solution is less than 17.0% by weight. In one embodiment, the SPF percentage in the solution is less than 16.0% by weight. In one embodiment, the SPF percentage in the solution is less than 15.0% by weight. In one embodiment, the SPF percentage in the solution is less than 14.0% by weight. In one embodiment, the SPF percentage in the solution is less than 13.0% by weight. In one embodiment, the SPF percentage in the solution is less than 12.0% by weight. In one embodiment, the SPF percentage in the solution is less than 11.0% by weight. In one embodiment, the SPF percentage in the solution is less than 10.0% by weight. In one embodiment, the SPF percentage in the solution is less than 9.0% by weight. In one embodiment, the SPF percentage in the solution is less than 8.0% by weight. In one embodiment, the SPF percentage in the solution is less than 7.0% by weight. In one embodiment, the SPF percentage in the solution is less than 6.0% by weight. In one embodiment, the SPF percentage in the solution is less than 5.0% by weight. In one embodiment, the SPF percentage in the solution is less than 4.0% by weight. In one embodiment, the SPF percentage in the solution is less than 3.0% by weight. In one embodiment, the SPF percentage in the solution is less than 2.0% by weight. In one embodiment, the SPF percentage in the solution is less than 1.0% by weight. In one embodiment, the SPF percentage in the solution is less than 0.9% by weight. In one embodiment, the SPF percentage in the solution is less than 0.8% by weight. In one embodiment, the SPF percentage in the solution is less than 0.7% by weight. In one embodiment, the SPF percentage in the solution is less than 0.6% by weight. In one embodiment, the SPF percentage in the solution is less than 0.5% by weight. In one embodiment, the SPF percentage in the solution is less than 0.4% by weight. In one embodiment, the SPF percentage in the solution is less than 0.3% by weight. In one embodiment, the SPF percentage in the solution is less than 0.2% by weight. In one embodiment, the SPF percentage in the solution is less than 0.1% by weight.

In one embodiment, the SPF percentage in the solution is greater than 0.1 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.2 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.3 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.4 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.5 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.6 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.7 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.8 wt%. In one embodiment, the SPF percentage in the solution is greater than 0.9 wt%. In one embodiment, the SPF percentage in the solution is greater than 1.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 2.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 3.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 4.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 5.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 6.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 7.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 8.0 wt%. In one embodiment, the SPF percentage in the solution is greater than 9.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 10.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 11.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 12.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 13.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 14.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 15.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 16.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 17.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 18.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 19.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 20.0% by weight. In one embodiment, the SPF percentage in the solution is greater than 25.0% by weight.

In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 30.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 25.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 20.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 15.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 10.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 9.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 8.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 7.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 6.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 6.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 5.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 5.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 4.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 4.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 3.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 3.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 2.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 2.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 2.4 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.5 wt% to about 5.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.5 wt% to about 4.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.5 wt% to about 4.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.5 wt% to about 3.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.5 wt% to about 3.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.5 wt% to about 2.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 1.0 wt% to about 4.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 1.0 wt% to about 3.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 1.0 wt% to about 3.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 1.0 wt% to about 2.5 wt%. In one embodiment, the SPF percentage in the solution ranges from about 1.0 wt% to about 2.4 wt%. In one embodiment, the SPF percentage in the solution ranges from about 1.0 wt% to about 2.0 wt%.

In one embodiment, the SPF percentage in the solution ranges from about 20.0 wt% to about 30.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 10.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 1.0 wt% to about 10.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 2 wt% to about 10.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 0.1 wt% to about 6.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 6.0 wt% to about 10.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 6.0 wt% to about 8.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 6.0 wt% to about 9.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 10.0 wt% to about 20.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 11.0 wt% to about 19.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 12.0 wt% to about 18.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 13.0 wt% to about 17.0 wt%. In one embodiment, the SPF percentage in the solution ranges from about 14.0 wt% to about 16.0 wt%. In one embodiment, the SPF percentage in the solution is about 1.0 wt%. In one embodiment, the SPF percentage in the solution is about 1.5 wt%. In one embodiment, the SPF percentage in the solution is about 2.0 wt%. In one embodiment, the SPF percentage in the solution is about 2.4 wt%. In one embodiment, the SPF percentage in the solution is 3.0 wt%. In one embodiment, the SPF percentage in the solution is 3.5 wt%. In one embodiment, the SPF percentage in the solution is about 4.0 wt%. In one embodiment, the SPF percentage in the solution is about 4.5 wt%. In one embodiment, the SPF percentage in the solution is about 5.0 wt%. In one embodiment, the SPF percentage in the solution is about 5.5 wt%. In one embodiment, the SPF percentage in the solution is about 6.0 wt%. In one embodiment, the SPF percentage in the solution is about 6.5% by weight. In one embodiment, the SPF percentage in the solution is about 7.0% by weight. In one embodiment, the SPF percentage in the solution is about 7.5% by weight. In one embodiment, the SPF percentage in the solution is about 8.0% by weight. In one embodiment, the SPF percentage in the solution is about 8.5% by weight. In one embodiment, the SPF percentage in the solution is about 9.0% by weight. In one embodiment, the SPF percentage in the solution is about 9.5% by weight. In one embodiment, the SPF percentage in the solution is about 10.0% by weight.

In one embodiment, the percentage of sericin in the solution is less than detectable to 25.0% by weight. In one embodiment, the percentage of sericin in the solution is less than detectable to 5.0% by weight. In one embodiment, the percentage of sericin in the solution is 1.0% by weight. In one embodiment, the percentage of sericin in the solution is 2.0% by weight. In one embodiment, the percentage of sericin in the solution is 3.0% by weight. In one embodiment, the percentage of sericin in the solution is 4.0% by weight. In one embodiment, the percentage of sericin in the solution is 5.0% by weight. In one embodiment, the percentage of sericin in the solution is 10.0% by weight. In one embodiment, the percentage of sericin in the solution is 25.0% by weight.

In some embodiments, the filament-based protein fragments of this disclosure are storage stable (they do not slowly or spontaneously gel when stored in aqueous solution and do not aggregate over time, thus the molecular weight does not increase) for 10 days to 3 years, depending on storage conditions, SPF percentage, and number and shipping conditions. Additionally, the pH can be altered to extend shelf life and/or support shipping conditions by preventing premature folding and aggregation of the filaments. In one embodiment, the stability of the LiBr-filament fragment solution is 0 to 1 year. In one embodiment, the stability of the LiBr-filament fragment solution is 0 to 2 years. In one embodiment, the stability of the LiBr-filament fragment solution is 0 to 3 years. In one embodiment, the stability of the LiBr-filament fragment solution is 0 to 4 years. In one embodiment, the stability of the LiBr-filament fragment solution is 0 to 5 years. In one embodiment, the stability of the LiBr-filament fragment solution is 1 to 2 years. In one embodiment, the stability of the LiBr-filament fragment solution is 1 to 3 years. In one embodiment, the stability of the LiBr-filament fragment solution is 1 to 4 years. In one embodiment, the stability of the LiBr-filament fragment solution is 1 to 5 years. In one embodiment, the stability of the LiBr-filament fragment solution is 2 to 3 years. In one embodiment, the stability of the LiBr-filament fragment solution is 2 to 4 years. In one embodiment, the stability of the LiBr-filament fragment solution is 2 to 5 years. In one embodiment, the stability of the LiBr-filament fragment solution is 3 to 4 years. In one embodiment, the stability of the LiBr-filament fragment solution is 3 to 5 years. In one embodiment, the stability of the LiBr-filament fragment solution is 4 to 5 years.

In one embodiment, the stability of the disclosed composition is from 10 days to 6 months. In one embodiment, the stability of the disclosed composition is from 6 months to 12 months. In one embodiment, the stability of the disclosed composition is from 12 months to 18 months. In one embodiment, the stability of the disclosed composition is from 18 months to 24 months. In one embodiment, the stability of the disclosed composition is from 24 months to 30 months. In one embodiment, the stability of the disclosed composition is from 30 months to 36 months. In one embodiment, the stability of the disclosed composition is from 36 months to 48 months. In one embodiment, the stability of the disclosed composition is from 48 months to 60 months.

In one embodiment, selected properties of the SPF-coated article, which may be enhanced compared to the uncoated article, may include one or more of the following: dimensional stability against washing, dimensional stability against dry cleaning, appearance after washing, appearance after dry cleaning, color fastness to washing, color fastness to dry cleaning, color fastness to non-chlorine bleach, seam torque/helix (for woven fabrics), color fastness to bleaching, color fastness to rubbing, color fastness to water, color fastness to light, color fastness to perspiration, color fastness to chlorinated pool water, color fastness to seawater, tensile strength, seam slippage, tear strength, seam breaking strength, abrasion resistance, pilling resistance, tensile recovery, bursting strength, and resistance to mold rotation during storage. Color fastness (label), ozone fastness, fuzz retention, flexural and slant fastness, saliva fastness, snag resistance, wrinkle resistance (e.g., garment appearance, fabric crease retention, fabric surface smoothness), water resistance, water resistance, stain resistance (e.g., water resistance, oil resistance, water/alcohol resistance), vertical wicking, absorbency, drying rate, stain removal, breathability, wicking, antimicrobial properties, UV protection, torque resistance, odor resistance, biocompatibility, wetting time, absorption rate, spreading speed, cumulative unidirectional transport, flame retardancy, coloring properties, fabric softening properties, pH regulating properties, anti-felt properties, and overall moisture management.

In any of the foregoing embodiments, at least one property of the article is improved, wherein the improved property is wash resistance and dimensional stability, and wherein, relative to the uncoated article, the amount of improvement in said property is selected from the group consisting of: at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 100%, at least 125%, at least 150%, at least 200%, at least 300%, at least 400%, and at least 500%.

In any of the foregoing embodiments, at least one property of the article is improved, wherein the improved property is washability and dimensional retention, and wherein, relative to the uncoated article, the amount of improvement in said property is selected from the group consisting of: at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 100%, at least 125%, at least 150%, at least 200%, at least 300%, at least 400%, and at least 500%.

In any of the foregoing embodiments, at least one property of the article is improved, wherein the improved property is shrinkage resistance, and wherein, relative to the uncoated article, the amount of improvement in said property is selected from the group consisting of: at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 100%, at least 125%, at least 150%, at least 200%, at least 300%, at least 400%, and at least 500%.

Compositions and methods including silk protein fragment coatings

In one embodiment, this disclosure may include textiles, such as fibers, yarns, fabrics, or other materials and combinations thereof, which may be coated with an SPF mixture solution (i.e., silk core protein solution (SFS)) as described herein to produce coated articles. In one embodiment, the coated articles described herein may be treated with additional chemical agents that may enhance the properties of the coated articles. In one embodiment, the SFS may include one or more chemical agents that may enhance the properties of the coated articles.

In one embodiment, the textile can be a flexible material (woven or nonwoven), comprising a network of natural and/or man-made fibers, threads, yarns, or combinations thereof. SFS can be applied at any stage of textile processing, from a single fiber to yarn, fabric, thread, or combinations thereof.

In one embodiment, the fiber may be a natural fiber, which may comprise a natural fiber cellulose matrix, wherein the natural fiber cellulose matrix may include one or more of the following: (1) pulp, such as flax pulp, hemp pulp, hibiscus pulp, jute pulp, flax pulp, and/or ramie pulp; (2) leaves, such as flax leaves, hemp leaves, sisal leaves, Manila hemp leaves, banana leaves, hena camu leaves, ramie leaves, Indian hemp leaves, and/or coconut fiber leaves; and (3) seed fibers, such as cotton seed fibers and/or kapok seed fibers. In one embodiment, the fiber may be a natural fiber, which may comprise a natural fiber protein matrix, wherein the natural fiber protein matrix may include one or more of the following: (1) hair, such as alpaca hair, camel hair, cashmere, llama hair, mohair, and/or llama wool; (2) down, such as sheep wool; (3) filaments, such as silk. In one embodiment, the fiber may be a natural fiber, which may comprise a natural fiber mineral matrix, including asbestos. In one embodiment, the fiber may be a man-made fiber, which may comprise a man-made fiber organic natural polymer matrix, the man-made fiber organic natural polymer matrix comprising one or more of the following: (1) a cellulose matrix, such as bamboo, rayon, lyocell, acetate and/or triacetate; (2) a protein matrix, such as azlon; (3) alginate; and (4) rubber. In one embodiment, the fiber may be a man-made fiber, which may comprise a man-made fiber organic synthetic matrix, the man-made fiber organic synthetic matrix comprising one or more of the following: acrylic acid, anidex, aromatic polyamide, fluorocarbon, modified polyacrylonitrile, novoloid, nylon, nytril, olefin, PBI, polycarbonate, polyester, rubber, salon, SPANDEX, vinal, vinvon. In one embodiment, the fiber may be a man-made fiber, which may comprise a man-made fiber inorganic matrix, the inorganic matrix comprising one or more of the following: glass materials, metallic materials, and carbon materials.

In one embodiment, the yarn may include natural fibers, which may comprise a natural fiber cellulose matrix, wherein the natural fiber cellulose matrix may be derived from: (1) pulps, such as flax pulp, hemp pulp, hibiscus pulp, jute pulp, flax pulp, and/or ramie pulp; (2) leaves, such as flax leaves, hemp leaves, sisal leaves, Manila hemp leaves, banana leaves, henaquin leaves, ramie leaves, Indian hemp leaves, and/or coconut fiber leaves; or (3) seed fibers, such as cotton seed fibers and/or kapok seed fibers. In one embodiment, the yarn may include natural fibers, which may comprise a natural fiber protein matrix, wherein the natural fiber protein matrix may be derived from: (1) wool, such as alpaca wool, camel wool, cashmere, llama wool, mohair, and/or llama wool; (2) down, such as sheep wool; or (3) filaments, such as silk. In one embodiment, the yarn may include natural fibers, which may comprise a natural fiber mineral matrix, including asbestos. In one embodiment, the yarn may include synthetic fibers, which may comprise a synthetic fiber organic natural polymer matrix, the synthetic fiber organic natural polymer matrix including: (1) a cellulose matrix, such as bamboo, rayon, lyocell, acetate and/or triacetate; (2) a protein matrix, such as azlon; (3) alginate; or (4) rubber. In one embodiment, the yarn may include synthetic fibers, which may comprise a synthetic fiber organic synthetic matrix, the synthetic fiber organic synthetic matrix including: acrylic acid, anidex, aromatic polyamide, fluorocarbon, modified polyacrylonitrile, novoloid, nylon, nytril, olefin, PBI, polycarbonate, polyester, rubber, salon, SPANDEX, vinal, vinvon. In one embodiment, the yarn may include synthetic fibers, which may comprise a synthetic fiber inorganic matrix, the synthetic fiber inorganic matrix including glass materials, metallic materials, carbon materials and/or specialty materials.

In one embodiment, the fabric may include natural fibers and/or yarns, the natural fibers and/or yarns comprising a natural fiber cellulose matrix, wherein the natural fiber cellulose matrix may be derived from: (1) sizing agents, such as flax sizing agents, hemp sizing agents, hibiscus sizing agents, jute sizing agents, flax sizing agents, and/or ramie sizing agents; (2) leaves, such as flax leaves, hemp leaves, sisal leaves, Manila hemp leaves, banana leaves, henna leaves, ramie leaves, Indian hemp leaves, and/or coconut fiber leaves; or (3) seed fibers, such as cotton seed fibers and/or kapok seed fibers. In one embodiment, the fabric may include natural fibers and/or yarns, the natural fibers and/or yarns comprising a natural fiber protein matrix, wherein the natural fiber protein matrix may be derived from: (1) wool, such as alpaca wool, camel wool, cashmere, llama wool, mohair, and/or pygmy alpaca wool; (2) down, such as sheep wool; or (3) filaments, such as silk. In one embodiment, the fabric may include natural fibers and/or yarns, which may contain a natural fiber mineral matrix, including asbestos. In one embodiment, the fabric may include synthetic fibers and/or yarns, which may contain a synthetic fiber organic natural polymer matrix, which may include: (1) a cellulose matrix, such as bamboo, rayon, lyocell, acetate and/or triacetate; (2) a protein matrix, such as azlon; (3) alginate; or (4) rubber. In one embodiment, the fabric may include synthetic fibers and/or yarns, which may contain a synthetic fiber organic synthetic matrix, which may include: acrylic acid, anidex, aromatic polyamides, fluorocarbons, modified polyacrylonitrile, novoloid, nylon, nytril, olefins, PBI, polycarbonate, polyester, rubber, salon, SPANDEX, vinal, and vinvon. In one embodiment, the fabric may include synthetic fibers and/or yarns, the synthetic fibers and/or yarns may contain a synthetic fiber inorganic matrix, the synthetic fiber inorganic matrix may include glass materials, metal materials, carbon materials and/or specialty materials.

In some embodiments, the fabric may include alpaca fiber, alpaca wool, alpaca cashmere, llamaskin fiber, llamaskin cashmere, llamaskin cashmere, cotton, sheep wool, sheep cashmere, byss silk, chiengora, qiviut, yak hair, rabbit hair, lamb's wool, mohair, Tibetan cashmere, lopi, camel hair, Pashmina cashmere, Angora cashmere, silk, spider silk, Manila hemp fiber, coconut fiber, flax fiber, jute fiber, kapok fiber, hemp fiber, raffia fiber, bamboo fiber, hemp, modal fiber, pineapple hemp, ramie, sisal, soybean protein fiber, polyester, polyamide, polyaramid, polytetrafluoroethylene, polyethylene, polypropylene, polyurethane, silicone, mixtures of polyurethane and polyethylene glycol, ultra-high molecular weight polyethylene, high performance polyethylene, nylon, LYCRA (polyester-polyurethane copolymer, also known as SPANDEX and elastomer), or mixtures thereof. In some embodiments, the fabric includes pile. In some embodiments, the fabric comprises an inert synthetic material such as polyester, polyamide, polyaramid, polytetrafluoroethylene, polyethylene, polypropylene, polyurethane, silicone, a mixture of polyurethane and polyethylene glycol, ultra-high molecular weight polyethylene, high performance polyethylene, nylon, LYCRA (polyester-polyurethane copolymer, also known as SPANDEX and elastomer), rayon, or a mixture thereof.

In some embodiments, the fabric comprises one or more of the following selected from the group consisting of: cotton, silk, alpaca wool, alpaca cashmere, llamaskin wool, llamaskin cashmere, cotton, cashmere, sheep wool, sheep cashmere, and combinations thereof. In some embodiments, the fabric comprises one or more of the following: natural fleece, synthetic fleece, alpaca wool, alpaca cashmere, llamaskin wool, llamaskin cashmere, cashmere, sheep wool, sheep cashmere, mohair, camel hair, or Angora cashmere.

In some embodiments, the article described herein may contain 100% by weight (w/w) of a synthetic fiber component. In some embodiments, the article of manufacture described herein may contain, by weight (w/w) greater than 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20%, 21%, 22%, 23%, 24%, 25%, 26%, 27%, 28%, 29%, 30%, 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, 41%, 42%, 43%, 44%, 45%, 46%, 47%, 48%, 49%, 50%, 51%, 52%, ... The article comprises 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% of a synthetic fiber component, wherein the remainder of the article is a non-synthetic fiber component by weight (w/w), as described herein. In some embodiments, the article of manufacture described herein may contain less than 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20%, 21%, 22%, 23%, 24%, 25%, 26%, 27%, 28%, 29%, 30%, 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, 41%, 42%, 43%, 44%, 45%, 46%, 47%, 48%, 49%, 50%, 51%, 52% by weight (w/w) of the article of manufacture. The article comprises 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% of a synthetic fiber component, wherein the remainder of the article is a non-synthetic fiber component by weight (w/w), as described herein. In some embodiments, the article of manufacture described herein may comprise about 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20%, 21%, 22%, 23%, 24%, 25%, 26%, 27%, 28%, 29%, 30%, 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, 41%, 42%, 43%, 44%, 45%, 46%, 47%, 48%, 49%, 50%, 51%, 52% by weight (w/w) of the article of manufacture. The article comprises 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% of a synthetic fiber component, wherein the remainder of the article is a non-synthetic fiber component by weight (w/w), as described herein.

In some embodiments, the coating further comprises a crosslinking agent. In some embodiments, any SPF described herein, including silk core protein or silk core protein-based fragments, is chemically modified with a precursor linker comprising a crosslinking agent to form a silk conjugate. In some embodiments, the fabric is covalently linked to the crosslinking agent. In some embodiments, the crosslinking agent is covalently linked to a surfactant and/or emulsifier. In some embodiments, the crosslinking agent is covalently linked to the fabric and the surfactant and/or emulsifier. In some embodiments, the crosslinking agent is covalently linked to both the fabric and the SPF.

The precursor linker can be selected from any of the following natural cross-linking agents: caffeic acid, tannic acid, genipin, proanthocyanidins, etc. The precursor cross-linking can be selected from any of the following enzyme cross-linking agents: transglutaminase cross-linking, hydrolase cross-linking, peptidase cross-linking (e.g., SrtA sorting enzyme from Staphylococcus aureus), oxidoreductase cross-linking, tyrosinase cross-linking, laccase cross-linking, peroxidase cross-linking (e.g., horseradish peroxidase), lysyl oxidase cross-linking, peptide ligases (e.g., butterfly pea mucin 1, peptide ligase, subtilis ligase, etc.), etc.

In some embodiments, filamentin or filamentin-based protein fragments are chemically modified with precursor linkers to form filament conjugates with crosslinking agents or activators, said crosslinking agents or activators being independently selected from N-hydroxysuccinimide ester crosslinkers, imine ester crosslinkers, aminobenzoic acid sulfosuccinimide esters, methacrylates, silanes, silicates, alkynes, azides, aldehydes, carbodiimide crosslinkers, dicyclohexylcarbodiimide activators, dicyclohexylcarbodiimide crosslinkers, maleimide crosslinkers, haloacetyl crosslinkers, pyridyl disulfide crosslinkers, hydrazide crosslinkers, alkoxyamine crosslinkers, reductive amination crosslinkers, aryl azide crosslinkers, diaziridine crosslinkers, azide-phosphine crosslinkers, transferase crosslinkers, hydrolase crosslinkers, glutamine transaminase crosslinkers, peptidase crosslinkers, oxidoreductase crosslinkers, tyrosinase crosslinkers, laccase crosslinkers, peroxidase crosslinkers, lysine oxidase crosslinkers, and any combination thereof. Some chemically modified silken proteins have been described in J Mater Chem. June 23, 2009, 19(36), 6443–6450, including cyanuric chloride-activated coupling, carbodiimide coupling, arginine masking, chlorosulfonic acid reaction, diazo coupling, tyrosinase-catalyzed grafting, and poly(methacrylate) grafting.

In some embodiments, the article further comprises a crosslinking agent. In some embodiments, the crosslinking agent is a polyphenolic compound containing 12 phenolic hydroxyl groups, having a molecular weight of about 500-4000 Da, and about 5-7 aromatic rings per 1000 Da. In some embodiments, the crosslinking agent is a polyphenolic compound selected from the group consisting of: curcumin, demethoxycurcumin, bisdemethoxycurcumin, resveratrol, caffeic acid, tannins, gallic tannins, proanthocyanidins, hydrolyzable tannins, root bark tannins, gallic acid, chlorogenic acid, sarstigmol, capsaicin, 6-shogaol, 6-gingerol, flavonoids, flavanols, new flavonoids, arbutin, cynarin, apigenin, isocitronellol, etc. Luteolin, hesperidin, citrulline, galangin, kaempferol, myricetin, quercetin, rutin, limonene, curcurocitrin, sennaol, hesperidin, naringin, naringin, sennain, quercetin, chitosan A, stigmosiderin, daidzein, estrol, gentiosperidin, genistein, daidzein, epoetin, lactoglobulin, pycnogenol, silymarin, lignin, and combinations thereof.

In one embodiment, the coating is applied horizontally to the article comprising the fabric. In another embodiment, the coating is applied horizontally to the fabric. In one embodiment, the thickness of the coating is selected from about 5 nm, about 10 nm, about 15 nm, about 20 nm, about 25 nm, about 50 nm, about 100 nm, about 200 nm, about 500 nm, about 1 μm, about 5 μm, about 10 μm, and about 20 μm. In another embodiment, the thickness range of the coating is selected from about 5 nm to about 100 nm, about 100 nm to about 200 nm, about 200 nm to about 500 nm, about 1 μm to about 2 μm, about 2 μm to about 5 μm, about 5 μm to about 10 μm, and about 10 μm to about 20 μm.

In one embodiment, the fabric is treated with a polymer such as polyglycolic acid (PGA), polyethylene glycol, copolymers of glycolide, glycolide/L-lactide copolymer (PGA/PLLA), glycolide/trimethylene carbonate copolymer (PGA/TMC), polylactide (PLA), stereopolymers of PLA, poly-L-lactide (PLLA), poly-DL-lactide (PDLLA), L-lactide/DL-lactide copolymer, copolymers of PLA, lactide/tetramethylglycolic acid copolymer, lactide/trimethylene carbonate copolymer, lactide/δ-valerolactone copolymer, lactide/ε-caprolactone copolymer, polyphenol peptides, PLA/polyethylene oxide copolymer, and asymmetric 3,6-substituted poly-1,4-dioxane-2. 5-Diketone, poly-β-hydroxybutyrate (PHBA), PHBA/β-hydroxyvalerate copolymer (PHBA/HVA), poly-β-hydroxypropionate (PHPA), polydioxanone (PDS), poly-δ-valerolactone, poly-ε-caprolactone, methyl methacrylate-N-vinylpyrrolidone copolymer, polyesteramide, polyester of oxalic acid, polydihydropyran, polyalkyl 2-cyanoacrylate, polyurethane (PU), polyvinyl alcohol (PVA), polypeptide, poly-β-malic acid (PMLA), poly-β-alkanic acid, polyvinyl alcohol (PVA), polyethylene oxide (PEO), chitosan polymer, polyethylene, polypropylene, polyacetal, polyamide, polyester, polysulfone, polyetheretherketone, polyethylene terephthalate, polycarbonate, polyaryletherketone and polyetherketoneketone.

In one embodiment, the textile can be manufactured using one or more of the following processes: weaving, knitting, and nonwoven processes. In one embodiment, the weaving process can include plain weave, twill weave, and/or satin weave. In one embodiment, the knitting process can include weft knitting (e.g., circular knitting, flatbed knitting, and/or full-shape knitting) and/or warp knitting (e.g., terikeld knitting, Raschel knitting, and/or crochet knitting). In one embodiment, the nonwoven process can include stabilized fibers (e.g., dry-laid and/or wet-laid) and/or continuous filaments (e.g., spun-laid and/or meltblown).

In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is a fabric for human clothing (including functional and/or sportswear). In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric exhibits improved moisture management properties and/or microbial growth tolerance. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is a fabric for home upholstery. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is used for automotive upholstery. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is used for aircraft upholstery. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is used for the upholstery of public, commercial, military, or other transportation vehicles (including buses and trains). In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is used for the upholstery of products requiring high abrasion resistance compared to conventional upholstery.

In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is manufactured as a trim fabric for automotive interiors. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the article is manufactured as a steering wheel fabric product. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is manufactured as a headrest fabric product. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is manufactured as an armrest fabric product. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is manufactured as an automotive floor mat fabric product. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is manufactured as an automotive or vehicle carpet fabric product. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is manufactured as an automotive trim fabric product. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is manufactured as a child car seat fabric product. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is a fabric product manufactured as a seat belt or seatbelt. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is a fabric product manufactured as a dashboard. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is a fabric product manufactured as a seat. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is a fabric product manufactured as a seat panel. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is a fabric product manufactured as an interior panel. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is a fabric product manufactured as an airbag cover. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is a fabric product manufactured as an airbag. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is a fabric product manufactured as a sun visor. In one embodiment, this disclosure provides an article comprising a fabric coated with silk protein fragments, wherein the fabric is a fabric product manufactured as a wire harness. In one embodiment, this disclosure provides an article coated with silk protein fragments, wherein the article is a padding layer. In one embodiment, this disclosure provides an article coated with silk protein fragments, wherein the product is an insulation component for automobiles, aircraft, or other vehicles. In some embodiments, the coating comprises an article coated with silk core protein fragments having a weight-average molecular weight range of about 1 kDa to about 350 kDa, wherein the average weight-average molecular weight range of the silk core protein fragments is selected from about 5 to about 10 kDa, about 6 kDa to about 17 kDa, about 17 kDa to about 39 kDa, about 39 kDa to about 80 kDa, about 60 to about 100 kDa, and about 80 kDa to about 144 kDa, wherein the polydispersity of the silk core protein fragments is about 1.5 to about 3.0 or about 1.0 to about 5.0, and optionally, wherein the protein or protein fragments, prior to coating the fabric, have not spontaneously or gradually gelled and have not undergone significant changes in color or turbidity when in solution for at least 10 days. The coating comprises silk core protein fragments with a weight-average molecular weight ranging from about 5 kDa to about 144 kDa, wherein the average weight-average molecular weight range of the silk core protein fragments is selected from about 5 to about 10 kDa, about 6 kDa to about 17 kDa, about 17 kDa to about 39 kDa, about 39 kDa to about 80 kDa, about 60 to about 100 kDa, and about 80 kDa to about 144 kDa, wherein the polydispersity of the silk core protein fragments is about 1.5 to about 3.0, and optionally, wherein the protein or protein fragments do not spontaneously or gradually gel and do not show significant changes in color or turbidity when in solution for at least 10 days prior to coating the fabric.

In one embodiment, this disclosure provides an article of manufacture comprising a fabric coated with silk protein fragments. In one embodiment, the article of manufacture is a fabric for making tents, sleeping bags, ponchos, and soft-walled coolers. In one embodiment, the fabric is a fabric for making sports equipment. In one embodiment, the fabric is a fabric for making outdoor gear. In one embodiment, the fabric is a fabric for making hiking gear (such as shoulder straps and backpacks). In one embodiment, the fabric is a fabric for making rock climbing equipment. In one embodiment, the fabric is canvas. In one embodiment, the fabric is a fabric for making hats. In one embodiment, the fabric is a fabric for making umbrellas. In one embodiment, the fabric is a fabric for making tents. In one embodiment, the fabric is a fabric for making baby bassinet, baby blanket, or baby pajamas. In one embodiment, the fabric is a fabric for making gloves (such as driving gloves or sports gloves). In one embodiment, the fabric is a fabric for making athletic pants (such as loose-fitting pants, running pants, yoga pants, or athletic pants). In one embodiment, the fabric is a fabric for making sweatshirts (such as loose-fitting sweatshirts, running sweatshirts, yoga sweatshirts, or athletic sweatshirts). In one embodiment, the fabric is a fabric used for manufacturing beach equipment (such as beach umbrellas, beach chairs, beach blankets, and beach towels). In one embodiment, the fabric is a fabric used for manufacturing jackets or coats. In one embodiment, the fabric is a fabric used for manufacturing medical clothing (such as surgical drapes, surgical gowns, surgical sleeves, laboratory sleeves, laboratory coats, wound dressings, sterile wraps, surgical masks, immobilization bandages, support devices, compression bandages, shoe covers, surgical blankets, etc.). The coating comprises silk-based proteins or fragments thereof with a weight-average molecular weight ranging from about 5 kDa to about 144 kDa.

In one embodiment, this disclosure provides an article of textile comprising a textile coated with a protein based on silk core protein or fragments thereof. In one embodiment, the textile is a textile for manufacturing tents, sleeping bags, ponchos, and soft-walled coolers. In one embodiment, the textile is a textile for manufacturing sports equipment. In one embodiment, the textile is a textile for manufacturing outdoor gear. In one embodiment, the textile is a textile for manufacturing hiking gear (such as shoulder straps and backpacks). In one embodiment, the textile is a textile for manufacturing rock climbing equipment. In one embodiment, the textile is canvas. In one embodiment, the textile is a textile for manufacturing hats. In one embodiment, the textile is a textile for manufacturing umbrellas. In one embodiment, the textile is a textile for manufacturing tents. In one embodiment, the textile is a textile for manufacturing baby bassinet, baby blanket, or baby pajamas. In one embodiment, the textile is a textile for manufacturing gloves (such as driving gloves or sports gloves). In one embodiment, the textile is a textile for manufacturing athletic pants (such as loose-fitting pants, running pants, yoga pants, or athletic pants). In one embodiment, the textile is a textile for manufacturing sweatshirts (such as loose-fitting sweatshirts, running sweatshirts, yoga sweatshirts, or athletic sweatshirts). In one embodiment, the textiles are textiles used to manufacture beach equipment (such as beach umbrellas, beach chairs, beach blankets, and beach towels). In one embodiment, the textiles are textiles used to manufacture jackets or coats. In one embodiment, the textiles are textiles used to manufacture medical clothing (such as surgical drapes, surgical gowns, surgical sleeves, laboratory sleeves, laboratory coats, wound dressings, sterile wraps, surgical masks, immobilization bandages, support devices, compression bandages, shoe covers, surgical blankets, etc.). The coating comprises a silk-based protein or fragment thereof with a weight-average molecular weight ranging from about 1 kDa to about 350 kDa, wherein the average weight-average molecular weight range of the silk-based protein or fragment thereof is selected from about 5 to about 10 kDa, about 6 kDa to about 17 kDa, about 17 kDa to about 39 kDa, about 39 kDa to about 80 kDa, about 60 to about 100 kDa, and about 80 kDa to about 144 kDa, wherein the polydispersity of the silk-based protein or fragment thereof is about 1.0 to about 5.0, and optionally, wherein the protein or protein fragment thereof does not spontaneously or gradually gel and does not show significant change in color or turbidity when in solution for at least 10 days prior to coating the fabric.

In one embodiment, this disclosure provides a shoe coated with a protein based on silk-core protein or fragments thereof. In another embodiment, this disclosure provides a shoe coated with a protein based on silk-core protein or fragments thereof, wherein the shoe exhibits improved properties compared to an uncoated shoe. In yet another embodiment, this disclosure provides a shoe coated with a protein based on silk-core protein or fragments thereof, wherein the shoe exhibits improved properties compared to an uncoated shoe, and wherein the improved property is stain resistance. In yet another embodiment, this disclosure provides a shoe coated with a protein based on silk-core protein or fragments thereof, wherein the shoe exhibits improved properties compared to an uncoated shoe, and wherein the shoe is made of natural or synthetic leather. The coating comprises a silk-based protein or fragment thereof with a weight-average molecular weight ranging from about 1 kDa to about 350 kDa or from about 5 kDa to about 144 kDa, wherein the average weight-average molecular weight range of the silk-based protein or fragment thereof is selected from about 5 to about 10 kDa, about 6 kDa to about 17 kDa, about 17 kDa to about 39 kDa, about 39 kDa to about 80 kDa, about 60 to about 100 kDa, and about 80 kDa to about 144 kDa, wherein the polydispersity of the silk-based protein or fragment thereof is about 1.0 to about 5.0 or about 1.5 to about 3.0, and optionally, wherein the protein or protein fragment thereof does not spontaneously or gradually gel and does not show significant change in color or turbidity when in solution for at least 10 days prior to coating the fabric.

In one aspect, this disclosure provides a method for preparing silk-coated fabrics and/or articles using silk protein fragments of this disclosure. In some embodiments, the silk-coated fabric is a silk core protein-coated fabric. In some embodiments, the silk-coated article is a silk core protein-coated article. In some embodiments, this disclosure also includes an article prepared by the method of this disclosure. In some embodiments, this disclosure also includes an article comprising a coated fabric prepared by the method of this disclosure. In some embodiments, this disclosure also includes a coated fabric prepared by the method of the present invention.

In some embodiments, this disclosure includes a method for preparing a silk core protein coated fabric, the method comprising applying a solution containing a reducing agent to the fabric, applying a silk core protein solution to the fabric, and drying the fabric.

In some embodiments, this disclosure includes a method for improving the size retention of a fabric during washing, the method comprising applying a solution containing a reducing agent to the fabric, applying a silk core protein solution to the fabric, and drying the fabric.

In one aspect, this disclosure includes a method for improving the size retention of a fabric during washing, the method comprising coating the surface of the fabric with a solution containing a reducing agent, preparing a silk core protein solution containing silk core protein fragments, coating the surface of the fabric with the silk core protein solution, and drying the surface of the fabric coated with the silk core protein solution, wherein, after washing, the coated fabric substantially retains its initial size before washing.

This disclosure contemplates any surfactant and/or emulsifier. In one non-limiting example, the surfactant and/or emulsifier is used in combination with a silk fibroin solution to treat a fabric. In one non-limiting example, the surfactant and/or emulsifier is used to pretreat the surface of a fabric to improve surface affinity between the silk fibroin fragments and the fabric. In some embodiments, the surfactant and/or emulsifier is a natural surfactant and/or emulsifier. In some embodiments, the surfactant and/or emulsifier is selected from cocoyl glucoside, decyl glucoside, lauryl glucoside, sucrose cocoate, octyl/octyl glucoside, and octyl/octyl glucoside. In some embodiments, the surfactant and/or emulsifier is selected from polyoxyethylene sorbitan monooleate, polyoxyethylene sorbitan trioleate, and polyoxyethylene castor oil. In some embodiments, the surfactant and/or emulsifier is selected from polyoxyethylene (10-30) sorbitan monooleate, polyoxyethylene (10-30) sorbitan trioleate, and polyoxyethylene (10-50) castor oil. In some embodiments, the surfactant and/or emulsifier is selected from polyoxyethylene (20) sorbitan monooleate, polyoxyethylene (20) sorbitan trioleate, and polyoxyethylene (29) castor oil. In some embodiments, the surfactant and/or emulsifier is polyoxyethylene (20) sorbitan monooleate. In some embodiments, the surfactant and/or emulsifier is polyoxyethylene (20) sorbitan monolaurate. In some embodiments, the surfactant and/or emulsifier is polyoxyethylene (20) sorbitan monopalmitate. In some embodiments, the surfactant and/or emulsifier is polyoxyethylene (20) sorbitan monostearate. In some embodiments, the surfactant and/or emulsifier is polyoxyethylene (20) sorbitan trioleate. In some embodiments, the surfactant and/or emulsifier is polyoxyethylene (20) sorbitan tristearate. In some embodiments, the surfactant and/or emulsifier is polyoxyethylene (29) castor oil. In some embodiments, the surfactant and/or emulsifier comprises sorbitan monofatty acid. In some embodiments, the surfactant and/or emulsifier comprises sorbitan trifatty acid. In some embodiments, the surfactant and/or emulsifier comprises castor oil. In some embodiments, the surfactant and/or emulsifier has a given degree of ethoxylation, which can be adjusted to produce a specific HLB value.

In some embodiments, the concentration of the surfactant and/or emulsifier in the solution ranges from 0.01 g/L to about 100 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier in the solution ranges from 0.1 g/L to about 50 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier in the solution ranges from 0.5 g/L to about 25 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier in the solution ranges from 1 g/L to about 20 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier in the solution ranges from about 20 g/L to about 50 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 1 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 2 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 3 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 4 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 5 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 6 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 7 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 8 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 9 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 10 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 11 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 12 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 13 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 14 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 15 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 16 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 17 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 18 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 19 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 20 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 21 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 22 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 23 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 24 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 25 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 26 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 27 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 28 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 29 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 30 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 31 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 32 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 33 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 34 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 35 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 36 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 37 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 38 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 39 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 40 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 41 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 42 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 43 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 44 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 45 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 46 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 47 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 48 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 49 g/L. In some embodiments, the concentration of the surfactant and/or emulsifier is about 50 g/L.

In some embodiments, the concentration of the fibroin fragment in the solution ranges from 0.01 g/L to about 100 g/L. In some embodiments, the concentration of the fibroin fragment in the solution ranges from 0.1 g/L to about 50 g/L. In some embodiments, the concentration of the fibroin fragment in the solution ranges from 0.5 g/L to about 25 g/L. In some embodiments, the concentration of the fibroin fragment in the solution ranges from 1 g/L to about 20 g/L. In some embodiments, the concentration of the fibroin fragment in the solution ranges from about 20 g/L to about 50 g/L. In some embodiments, the concentration of the fibroin fragment is about 1 g/L. In some embodiments, the concentration of the fibroin fragment is about 2 g/L. In some embodiments, the concentration of the fibroin fragment is about 3 g/L. In some embodiments, the concentration of the fibroin fragment is about 4 g/L. In some embodiments, the concentration of the fibroin fragment is about 5 g/L. In some embodiments, the concentration of the silk core protein fragment is about 6 g/L. In some embodiments, the concentration of the silk core protein fragment is about 7 g/L. In some embodiments, the concentration of the silk core protein fragment is about 8 g/L. In some embodiments, the concentration of the silk core protein fragment is about 9 g/L. In some embodiments, the concentration of the silk core protein fragment is about 10 g/L. In some embodiments, the concentration of the silk core protein fragment is about 11 g/L. In some embodiments, the concentration of the silk core protein fragment is about 12 g/L. In some embodiments, the concentration of the silk core protein fragment is about 13 g/L. In some embodiments, the concentration of the silk core protein fragment is about 14 g/L. In some embodiments, the concentration of the silk core protein fragment is about 15 g/L. In some embodiments, the concentration of the silk core protein fragment is about 16 g/L. In some embodiments, the concentration of the silk core protein fragment is about 17 g/L. In some embodiments, the concentration of the silk core protein fragment is about 18 g/L. In some embodiments, the concentration of the silk core protein fragment is about 19 g/L. In some embodiments, the concentration of the silk core protein fragment is about 20 g/L. In some embodiments, the concentration of the silk core protein fragment is about 21 g/L. In some embodiments, the concentration of the silk core protein fragment is about 22 g/L. In some embodiments, the concentration of the silk core protein fragment is about 23 g/L. In some embodiments, the concentration of the silk core protein fragment is about 24 g/L. In some embodiments, the concentration of the silk core protein fragment is about 25 g/L. In some embodiments, the concentration of the silk core protein fragment is about 26 g/L. In some embodiments, the concentration of the silk core protein fragment is about 27 g/L. In some embodiments, the concentration of the silk core protein fragment is about 28 g/L. In some embodiments, the concentration of the silk core protein fragment is about 29 g/L. In some embodiments, the concentration of the silk core protein fragment is about 30 g/L. In some embodiments, the concentration of the silk core protein fragment is about 31 g/L. In some embodiments, the concentration of the silk core protein fragment is about 32 g/L. In some embodiments, the concentration of the silk core protein fragment is about 33 g/L. In some embodiments, the concentration of the silk core protein fragment is about 34 g/L. In some embodiments, the concentration of the silk core protein fragment is about 35 g/L. In some embodiments, the concentration of the silk core protein fragment is about 36 g/L. In some embodiments, the concentration of the silk core protein fragment is about 37 g/L. In some embodiments, the concentration of the silk core protein fragment is about 38 g/L. In some embodiments, the concentration of the silk core protein fragment is about 39 g/L. In some embodiments, the concentration of the silk core protein fragment is about 40 g/L. In some embodiments, the concentration of the silk core protein fragment is about 41 g/L. In some embodiments, the concentration of the silk core protein fragment is about 42 g/L. In some embodiments, the concentration of the fibroin fragment is about 43 g/L. In some embodiments, the concentration of the fibroin fragment is about 44 g/L. In some embodiments, the concentration of the fibroin fragment is about 45 g/L. In some embodiments, the concentration of the fibroin fragment is about 46 g/L. In some embodiments, the concentration of the fibroin fragment is about 47 g/L. In some embodiments, the concentration of the fibroin fragment is about 48 g/L. In some embodiments, the concentration of the fibroin fragment is about 49 g/L. In some embodiments, the concentration of the fibroin fragment is about 50 g/L.

In some embodiments, the w/w ratio of the filoin fragments to the surfactant and/or emulsifier in the solution is about 99:1, about 98:2, about 97:3, about 96:4, about 95:5, about 94:6, about 93:7, about 92:8, about 91:9, about 90:10, about 89:11, about 88:12, about 87:13, about 86:14, about 85:15, about 84:16, about 83:17, about 82:18, about 81:19, about 80:20, about 79:21, about 78... :22, 77:23, 76:24, 75:25, 74:26, 73:27, 72:28, 71:29, 70:30, 69:31, 68:32, 67:33, 66:34, 65:35, 64:36, 63:37, 62:38, 61:39, 60:40, 59:41, 58:42, 57:43, 56:44, 55:45, 54:46, 53:47 Approximately 52:48, Approximately 51:49, Approximately 50:50, Approximately 49:51, Approximately 48:52, Approximately 47:53, Approximately 46:54, Approximately 45:55, Approximately 44:56, Approximately 43:57, Approximately 42:58, Approximately 41:59, Approximately 40:60, Approximately 39:61, Approximately 38:62, Approximately 37:63, Approximately 36:64, Approximately 35:65, Approximately 34:66, Approximately 33:67, Approximately 32:68, Approximately 31:69, Approximately 30:70, Approximately 29:71, Approximately 28:72, Approximately 2 7:73, approximately 26:74, approximately 25:75, approximately 24:76, approximately 23:77, approximately 22:78, approximately 21:79, approximately 20:80, approximately 19:81, approximately 18:82, approximately 17:83, approximately 16:84, approximately 15:85, approximately 14:86, approximately 13:87, approximately 12:88, approximately 11:89, approximately 10:90, approximately 9:91, approximately 8:92, approximately 7:93, approximately 6:94, approximately 5:95, approximately 4:96, approximately 3:97, approximately 2:98, or approximately 1:99. In some embodiments, the w/w ratio of the silk core protein fragments to the surfactant and/or emulsifier in the solution is approximately 1:1.

In some embodiments, the w/w ratio of the silk core protein fragments to the surfactant and/or emulsifier in the article is about 99:1, about 98:2, about 97:3, about 96:4, about 95:5, about 94:6, about 93:7, about 92:8, about 91:9, about 90:10, about 89:11, about 88:12, about 87:13, about 86:14, about 85:15, about 84:16, about 83:17, about 82:18, about 81:19, about 80:20, about 79:21, about 78 :22, 77:23, 76:24, 75:25, 74:26, 73:27, 72:28, 71:29, 70:30, 69:31, 68:32, 67:33, 66:34, 65:35, 64:36, 63:37, 62:38, 61:39, 60:40, 59:41, 58:42, 57:43, 56:44, 55:45, 54:46, 53:47 Approximately 52:48, Approximately 51:49, Approximately 50:50, Approximately 49:51, Approximately 48:52, Approximately 47:53, Approximately 46:54, Approximately 45:55, Approximately 44:56, Approximately 43:57, Approximately 42:58, Approximately 41:59, Approximately 40:60, Approximately 39:61, Approximately 38:62, Approximately 37:63, Approximately 36:64, Approximately 35:65, Approximately 34:66, Approximately 33:67, Approximately 32:68, Approximately 31:69, Approximately 30:70, Approximately 29:71, Approximately 28:72, Approximately 2 7:73, about 26:74, about 25:75, about 24:76, about 23:77, about 22:78, about 21:79, about 20:80, about 19:81, about 18:82, about 17:83, about 16:84, about 15:85, about 14:86, about 13:87, about 12:88, about 11:89, about 10:90, about 9:91, about 8:92, about 7:93, about 6:94, about 5:95, about 4:96, about 3:97, about 2:98, or about 1:99. In some embodiments, the w/w ratio of the silk core protein fragments to the surfactant and/or emulsifier in the article is about 1:1.

In some embodiments, the silk-core protein solution comprises low-molecular-weight, medium-molecular-weight, and/or high-molecular-weight silk-core protein fragments. In some embodiments, the silk-core protein solution comprises low-molecular-weight silk-core protein fragments. In some embodiments, the silk-core protein solution comprises medium-molecular-weight silk-core protein fragments.

In some implementations, drying the surface of the fabric involves heating the surface of the fabric without substantially altering the properties of the silk core protein coating.

In some embodiments, the method includes an additional step of drying the surface of the fabric. In some embodiments, the additional drying step is performed after coating the surface of the fabric with a solution containing a reducing agent. In some embodiments, the additional drying step is performed before coating the surface with a silk core protein solution.

In some embodiments, the fabric substantially retains its initial dimensions before washing after washing. In some embodiments, after washing, the fabric retains substantially most of its initial dimensions compared to similar fabrics not treated with surfactants and/or emulsifiers and silk core protein solutions.

In any of the foregoing embodiments, at least one property of the article is improved, wherein the improved property is wash resistance and dimensional stability, and wherein, relative to the uncoated article, the amount of improvement in said property is selected from the group consisting of: at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 100%, at least 125%, at least 150%, at least 200%, at least 300%, at least 400%, and at least 500%.

In any of the foregoing embodiments, at least one property of the article is improved, wherein the improved property is moisture management. In some embodiments, moisture management is improved compared to similar articles comprising similar fabrics but without a coating. Moisture management can be assessed by any method known in the art, such as, but not limited to, by absorbency testing, vertical wicking testing, or drying rate testing. Moisture management can be improved by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 100%, at least 125%, at least 150%, at least 200%, at least 300%, at least 400%, or at least 500%.

In any of the foregoing embodiments, at least one property of the article is improved, wherein the improved property is washability and dimensional retention, and wherein, relative to the uncoated article, the amount of improvement in said property is selected from the group consisting of: at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 100%, at least 125%, at least 150%, at least 200%, at least 300%, at least 400%, and at least 500%.

In any of the foregoing embodiments, at least one property of the article is improved, wherein the improved property is shrinkage resistance, and wherein, relative to the uncoated article, the amount of improvement in said property is selected from the group consisting of: at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 100%, at least 125%, at least 150%, at least 200%, at least 300%, at least 400%, and at least 500%.

In one embodiment, the aforementioned improved properties, or any other improved properties described herein, are determined after a certain number of machine washing cycles (e.g., by a household washing machine), said cycles being selected from the group consisting of: 0 cycles, 1 cycle, 2 cycles, 3 cycles, 4 cycles, 5 cycles, 6 cycles, 7 cycles, 8 cycles, 9 cycles, 10 cycles, 11 cycles, 12 cycles, 13 cycles, 14 cycles, 15 cycles, 20 cycles, 25 cycles, 30 cycles, 35 cycles, 40 cycles, 45 cycles, and 50 cycles.

In one embodiment, the concentration of the silk core protein solution is less than 30.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 25.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 20.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 19.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 18.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 17.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 16.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 15.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 14.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 13.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 12.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 11.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 10.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 9.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 8.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 7.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 6.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 5.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 4.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 3.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 2.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 1.0% w/v. In one embodiment, the concentration of the silk core protein solution is less than 0.9% w/v. In one embodiment, the concentration of the silk core protein solution is less than 0.8% w/v. In one embodiment, the concentration of the silk core protein solution is less than 0.7% w/v. In one embodiment, the concentration of the silk core protein solution is less than 0.6% w/v. In one embodiment, the concentration of the silk core protein solution is less than 0.5% w/v. In one embodiment, the concentration of the silk core protein solution is less than 0.4% w/v. In one embodiment, the concentration of the silk core protein solution is less than 0.3% w/v. In one embodiment, the concentration of the silk core protein solution is less than 0.2% w/v. In one embodiment, the concentration of the silk core protein solution is less than 0.1% w/v.

In one embodiment, the concentration of the silk core protein solution is greater than 0.1% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 0.2% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 0.3% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 0.4% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 0.5% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 0.6% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 0.7% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 0.8% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 0.9% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 1.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 2.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 3.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 4.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 5.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 6.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 7.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 8.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 9.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 10.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 11.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 12.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 13.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 14.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 15.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 16.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 17.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 18.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 19.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 20.0% w/v. In one embodiment, the concentration of the silk core protein solution is greater than 25.0% w/v.

In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 30.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 25.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 20.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 15.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 10.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 9.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 8.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 7.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 6.5% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 6.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 5.5% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 5.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 4.5% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 4.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 3.5% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 3.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 2.5% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 2.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 2.4% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.5% w/v to about 5.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.5% w/v to about 4.5% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.5% w/v to about 4.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.5% w/v to about 3.5% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.5% w/v to about 3.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.5% w/v to about 2.5% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 1.0% w/v to about 4.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 1.0% w/v to about 3.5% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 1.0% w/v to about 3.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 1.0% w/v to about 2.5% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 1.0% w/v to about 2.4% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 1.0% w/v to about 2.0% w/v.

In one embodiment, the concentration of the silk core protein solution ranges from about 20.0% w/v to about 30.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 10.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 1.0% w/v to about 10.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 2% w/v to about 10.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 0.1% w/v to about 6.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 6.0% w/v to about 10.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 6.0% w/v to about 8.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 6.0% w/v to about 9.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 10.0% w/v to about 20.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 11.0% w/v to about 19.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 12.0% w/v to about 18.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 13.0% w/v to about 17.0% w/v. In one embodiment, the concentration of the silk core protein solution ranges from about 14.0% w/v to about 16.0% w/v. In one embodiment, the concentration of the silk core protein solution is about 1.0% w/v. In one embodiment, the concentration of the silk core protein solution is about 0.5% w/v. In one embodiment, the concentration of the silk core protein solution is about 1.5% w/v. In one embodiment, the concentration of the silk core protein solution is about 2.0% by weight. In one embodiment, the concentration of the silk core protein solution is about 2.4% w/v. In one embodiment, the concentration of the silk core protein solution is 3.0% w/v. In one embodiment, the concentration of the silk core protein solution is 3.5% w/v. In one embodiment, the concentration of the silk core protein solution is about 4.0% w/v. In one embodiment, the concentration of the silk core protein solution is about 4.5% w/v. In one embodiment, the concentration of the silk core protein solution is about 5.0% w/v. In one embodiment, the concentration of the silk core protein solution is about 5.5% w/v. In one embodiment, the concentration of the silk core protein solution is about 6.0% w/v. In one embodiment, the concentration of the silk core protein solution is about 6.5% w/v. In one embodiment, the concentration of the silk core protein solution is about 7.0% w/v. In one embodiment, the concentration of the silk core protein solution is about 7.5% w/v. In one embodiment, the concentration of the silk core protein solution is about 8.0% w/v. In one embodiment, the concentration of the silk core protein solution is about 8.5% w/v. In one embodiment, the concentration of the silk core protein solution is about 9.0% w/v. In one embodiment, the concentration of the silk core protein solution is about 9.5% w/v. In another embodiment, the concentration of the silk core protein solution is about 10.0% w/v.

In some embodiments, the SFS contains an acidic agent. In some embodiments, the acidic agent is Bronsted acid. In one embodiment, the acidic agent includes one or more of citric acid and acetic acid. In one embodiment, the acidic agent facilitates the deposition and coating of the SPF mixture (i.e., the SFS coating) on the textile to be coated, compared to the absence of an acidic agent. In one embodiment, the acidic agent improves the crystallization of the SPF mixture at the textile to be coated.

In one embodiment, the concentration of the acidifying agent added is greater than about 0.001%, or greater than about 0.002%, or greater than about 0.003%, or greater than about 0.004%, or greater than about 0.005%, or greater than about 0.006%, or greater than about 0.007%, or greater than about 0.008%, or greater than about 0.009%, or greater than about 0.01%, or greater than about 0.02%, or greater than about 0.03%, or greater than about 0.04% by weight (%w/w or %w/v) or by volume (v/v). %, or greater than about 0.05%, or greater than about 0.06%, or greater than about 0.07%, or greater than about 0.08%, or greater than about 0.09%, or greater than about 0.1%, or greater than about 0.2%, or greater than about 0.3%, or greater than about 0.4%, or greater than about 0.5%, or greater than about 0.6%, or greater than about 0.7%, or greater than about 0.8%, or greater than about 0.9%, or greater than about 1.0%, or greater than about 2.0%, or greater than about 3.0%, or greater than about 4.0%, or greater than about 5.0%.

In one embodiment, the concentration of the acidifying agent added is less than about 0.001%, or less than about 0.002%, or less than about 0.003%, or less than about 0.004%, or less than about 0.005%, or less than about 0.006%, or less than about 0.007%, or less than about 0.008%, or less than about 0.009%, or less than about 0.01%, or less than about 0.02%, or less than about 0.03%, or less than about 0.04% by weight (%w/w or %w/v) or by volume (v/v). %, or less than about 0.05%, or less than about 0.06%, or less than about 0.07%, or less than about 0.08%, or less than about 0.09%, or less than about 0.1%, or less than about 0.2%, or less than about 0.3%, or less than about 0.4%, or less than about 0.5%, or less than about 0.6%, or less than about 0.7%, or less than about 0.8%, or less than about 0.9%, or less than about 1.0%, or less than about 2.0%, or less than about 3.0%, or less than about 4.0%, or less than about 5.0%.

In some implementations, the SFS may have a pH less than about 9, or less than about 8.5, or less than about 8, or less than about 7.5, or less than about 7, or less than about 6.5, or less than about 6, or less than about 5.5, or less than about 5, or less than about 4.5, or less than about 4, or greater than about 3.5, or greater than about 4, or greater than about 4.5, or greater than about 5, or greater than about 5.5, or greater than about 6, or greater than about 6.5, or greater than about 7, or greater than about 7.5, or greater than about 8, or greater than about 8.5.

In some embodiments, the SFS may include an acidic agent and may have a pH less than about 9, or less than about 8.5, or less than about 8, or less than about 7.5, or less than about 7, or less than about 6.5, or less than about 6, or less than about 5.5, or less than about 5, or less than about 4.5, or less than about 4, or greater than about 3.5, or greater than about 4, or greater than about 4.5, or greater than about 5, or greater than about 5.5, or greater than about 6, or greater than about 6.5, or greater than about 7, or greater than about 7.5, or greater than about 8, or greater than about 8.5.

In some embodiments, the SFS, with or without surfactants and/or emulsifiers, has a pH range of about 3 to 5. In some embodiments, the SFS, with or without surfactants and/or emulsifiers, has a pH of about 4. In some embodiments, the SFS, with or without surfactants and/or emulsifiers, has a pH of about 4.5. In some embodiments, the SFS, with or without surfactants and/or emulsifiers, has a pH of about 4 to about 4.5.

In some embodiments, SFS may be applied to fibers and/or yarns having a diameter less than about 100 nm, or less than about 200 nm, or less than about 300 nm, or less than about 400 nm, or less than about 500 nm, or less than about 600 nm, or less than about 700 nm, or less than about 800 nm, or less than about 900 nm, or less than about 1000 nm, or less than about 2 μm, or less than about 5 μm, or less than about 10 μm, or less than about 20 μm, or less than about 30 μm, or less than about 40 μm, or less than about 50 μm, or less than about 60 μm, or less than about 70 μm, or less than about 80 μm, or less than about 90 μm, or less than about 100 μm, or less than about 200 μm, or less than about 300 μm, or less than about 400 μm, or less than about 500 μm, or less than about 60 μm. 0 μm, or less than about 700 μm, or less than about 800 μm, or less than about 900 μm, or less than about 1000 μm, or less than about 2 mm, or less than about 3 mm, or less than about 4 mm, or less than about 5 mm, or less than about 6 mm, or less than about 7 mm, or less than about 8 mm, or less than about 9 mm, or less than about 10 mm, or less than about 20 mm, or less than about 30 mm, or less than about 40 mm, or less than about 50 mm, or less than about 60 mm, or less than about 70 mm, or less than about 80 mm, or less than about 90 mm, or less than about 100 mm, or less than about 200 mm, or less than about 300 mm, or less than about 400 mm, or less than about 500 mm, or less than about 600 mm, or less than about 700 mm, or less than about 800 mm, or less than about 900 mm, or less than about 1000 mm.

In some embodiments, SFS may be applied to fibers and/or yarns having a diameter greater than about 100 nm, or greater than about 200 nm, or greater than about 300 nm, or greater than about 400 nm, or greater than about 500 nm, or greater than about 600 nm, or greater than about 700 nm, or greater than about 800 nm, or greater than about 900 nm, or greater than about 1000 nm, or greater than about 2 μm, or greater than about 5 μm, or greater than about 10 μm, or greater than about 20 μm, or greater than about 30 μm, or greater than about 40 μm, or greater than about 50 μm, or greater than about 60 μm, or greater than about 70 μm, or greater than about 80 μm, or greater than about 90 μm, or greater than about 100 μm, or greater than about 200 μm, or greater than about 300 μm, or greater than about 400 μm, or greater than about 500 μm, or greater than about 60 μm. 0 μm, or greater than about 700 μm, or greater than about 800 μm, or greater than about 900 μm, or greater than about 1000 μm, or greater than about 2 mm, or greater than about 3 mm, or greater than about 4 mm, or greater than about 5 mm, or greater than about 6 mm, or greater than about 7 mm, or greater than about 8 mm, or greater than about 9 mm, or greater than about 10 mm, or greater than about 20 mm, or greater than about 30 mm, or greater than about 40 mm, or greater than about 50 mm, or greater than about 60 mm, or greater than about 70 mm, or greater than about 80 mm, or greater than about 90 mm, or greater than about 100 mm, or greater than about 200 mm, or greater than about 300 mm, or greater than about 400 mm, or greater than about 500 mm, or greater than about 600 mm, or greater than about 700 mm, or greater than about 800 mm, or greater than about 900 mm, or greater than about 1000 mm.

In some embodiments, SFS may be applied to fibers and/or yarns having a length less than about 100 nm, or less than about 200 nm, or less than about 300 nm, or less than about 400 nm, or less than about 500 nm, or less than about 600 nm, or less than about 700 nm, or less than about 800 nm, or less than about 900 nm, or less than about 1000 nm, or less than about 2 μm, or less than about 5 μm, or less than about 10 μm, or less than about 20 μm, or less than about 30 μm, or less than about 40 μm, or less than about 50 μm, or less than about 60 μm, or less than about 70 μm, or less than about 80 μm, or less than about 90 μm, or less than about 100 μm, or less than about 200 μm, or less than about 300 μm, or less than about 400 μm, or less than about 500 μm, or less than about 60 μm. 0 μm, or less than about 700 μm, or less than about 800 μm, or less than about 900 μm, or less than about 1000 μm, or less than about 2 mm, or less than about 3 mm, or less than about 4 mm, or less than about 5 mm, or less than about 6 mm, or less than about 7 mm, or less than about 8 mm, or less than about 9 mm, or less than about 10 mm, or less than about 20 mm, or less than about 30 mm, or less than about 40 mm, or less than about 50 mm, or less than about 60 mm, or less than about 70 mm, or less than about 80 mm, or less than about 90 mm, or less than about 100 mm, or less than about 200 mm, or less than about 300 mm, or less than about 400 mm, or less than about 500 mm, or less than about 600 mm, or less than about 700 mm, or less than about 800 mm, or less than about 900 mm, or less than about 1000 mm.

In some embodiments, SFS may be applied to fibers and/or yarns having a length greater than about 100 nm, or greater than about 200 nm, or greater than about 300 nm, or greater than about 400 nm, or greater than about 500 nm, or greater than about 600 nm, or greater than about 700 nm, or greater than about 800 nm, or greater than about 900 nm, or greater than about 1000 nm, or greater than about 2 μm, or greater than about 5 μm, or greater than about 10 μm, or greater than about 20 μm, or greater than about 30 μm, or greater than about 40 μm, or greater than about 50 μm, or greater than about 60 μm, or greater than about 70 μm, or greater than about 80 μm, or greater than about 90 μm, or greater than about 100 μm, or greater than about 200 μm, or greater than about 300 μm, or greater than about 400 μm, or greater than about 500 μm, or greater than about 60 μm. 0 μm, or greater than about 700 μm, or greater than about 800 μm, or greater than about 900 μm, or greater than about 1000 μm, or greater than about 2 mm, or greater than about 3 mm, or greater than about 4 mm, or greater than about 5 mm, or greater than about 6 mm, or greater than about 7 mm, or greater than about 8 mm, or greater than about 9 mm, or greater than about 10 mm, or greater than about 20 mm, or greater than about 30 mm, or greater than about 40 mm, or greater than about 50 mm, or greater than about 60 mm, or greater than about 70 mm, or greater than about 80 mm, or greater than about 90 mm, or greater than about 100 mm, or greater than about 200 mm, or greater than about 300 mm, or greater than about 400 mm, or greater than about 500 mm, or greater than about 600 mm, or greater than about 700 mm, or greater than about 800 mm, or greater than about 900 mm, or greater than about 1000 mm.

In some embodiments, SFS may be applied to fibers and/or yarns having a weight (g/ ^m² ) of less than about 1 g/m², or less than about 2 g/ ^m² , or less than about 3 g/ ^m² , or less than about 4 g/ ^m² , or less than about 5 g/ ^m² , or less than about 6 g/ ^m² , or less than about 7 g/ ^m² , or less than about 8 g/ ^m² , or less than about 9 g/ ^m² , or less than about 10 g/ ^m² , or less than about 20 g/ ^m² , or less than about ³⁰ g/ ^m² , or less than about 40 g/ ^m² , or less than about 50 g/ ^m² , or less than about 60 g/ ^m² , or less than about 70 g/ ^m² , or less than about 80 g/ ^m² , or less than about 90 g/m² ^. Or less than about 100 g/ ^m² , or less than about 200 g/ ^m² , or less than about 300 g/ ^m² , or less than about 400 g/ ^m² , or less than about 500 g/ ^m² .

In some embodiments, SFS may be applied to fibers and/or yarns having a weight (g/ ^m² ) greater than about 1 g/ ^m² , or greater than about 2 g/m², or greater than about 3 g/ ^m² , or greater than about 4 g/ ^m² , or greater than about 5 g/ ^m² , or greater than about 6 g/ ^m² , or greater than about 7 g/ ^m² , or greater than about 8 g/ ^m² , or greater than about 9 g/ ^m² , or greater than about 10 g/ ^m² , or greater than about 20 g/ ^m² , or greater than about 30 ^g / ^m² , or greater than about 40 g/ ^m² , or greater than about 50 g/ ^m² , or greater than about 60 g/ ^m² , or greater than about 70 g/ ^m² , or greater than about 80 g/ ^m² , or greater than about 90 g/m² ^. Or greater than approximately 100 g/ ^m² , or greater than approximately 200 g/ ^m² , or greater than approximately 300 g/ ^m² , or greater than approximately 400 g/ ^m² , or greater than approximately 500 g/ ^m² .

In some embodiments, SFS can be applied to a fabric having a thickness of less than about 100 nm, or less than about 200 nm, or less than about 300 nm, or less than about 400 nm, or less than about 500 nm, or less than about 600 nm, or less than about 700 nm, or less than about 800 nm, or less than about 900 nm, or less than about 1000 nm, or less than about 2 μm, or less than about 5 μm, or less than about 10 μm, or less than about 20 μm, or less than about 30 μm, or less than about 40 μm, or less than about 50 μm, or less than about 60 μm, or Less than about 70 μm, or less than about 80 μm, or less than about 90 μm, or less than about 100 μm, or less than about 200 μm, or less than about 300 μm, or less than about 400 μm, or less than about 500 μm, or less than about 600 μm, or less than about 700 μm, or less than about 800 μm, or less than about 900 μm, or less than about 1000 μm, or less than about 2 mm, or less than about 3 mm, or less than about 4 mm, or less than about 5 mm, or less than about 6 mm, or less than about 7 mm, or less than about 8 mm, or less than about 9 mm, or less than about 10 mm.

In some embodiments, SFS can be applied to a fabric having a thickness greater than about 100 nm, or greater than about 200 nm, or greater than about 300 nm, or greater than about 400 nm, or greater than about 500 nm, or greater than about 600 nm, or greater than about 700 nm, or greater than about 800 nm, or greater than about 900 nm, or greater than about 1000 nm, or greater than about 2 μm, or greater than about 5 μm, or greater than about 10 μm, or greater than about 20 μm, or greater than about 30 μm, or greater than about 40 μm, or greater than about 50 μm, or greater than about 60 μm, or Greater than approximately 70 μm, or greater than approximately 80 μm, or greater than approximately 90 μm, or greater than approximately 100 μm, or greater than approximately 200 μm, or greater than approximately 300 μm, or greater than approximately 400 μm, or greater than approximately 500 μm, or greater than approximately 600 μm, or greater than approximately 700 μm, or greater than approximately 800 μm, or greater than approximately 900 μm, or greater than approximately 1000 μm, or greater than approximately 2 mm, or greater than approximately 3 mm, or greater than approximately 4 mm, or greater than approximately 5 mm, or greater than approximately 6 mm, or greater than approximately 7 mm, or greater than approximately 8 mm, or greater than approximately 9 mm, or greater than approximately 10 mm.

In some embodiments, SFS may be applied to a fabric having a width less than about 100 nm, or less than about 200 nm, or less than about 300 nm, or less than about 400 nm, or less than about 500 nm, or less than about 600 nm, or less than about 700 nm, or less than about 800 nm, or less than about 900 nm, or less than about 1000 nm, or less than about 2 μm, or less than about 5 μm, or less than about 1 0 μm, or less than about 20 μm, or less than about 30 μm, or less than about 40 μm, or less than about 50 μm, or less than about 60 μm, or less than about 70 μm, or less than about 80 μm, or less than about 90 μm, or less than about 100 μm, or less than about 200 μm, or less than about 300 μm, or less than about 400 μm, or less than about 500 μm, or less than about 600 μm, or less than about 700 μm, or less than about 800μm, or less than about 900μm, or less than about 1000μm, or less than about 2mm, or less than about 3mm, or less than about 4mm, or less than about 5mm, or less than about 6mm, or less than about 7mm, or less than about 8mm, or less than about 9mm, or less than about 10mm, or less than about 20mm, or less than about 30mm, or less than about 40mm, or less than about 50mm, or less than about 60mm, or less than about 70mm, or less than about 80mm, or less than about 90mm, or less than about 100mm, or less than about 200mm, or less than about 300mm, or less than about 400mm, or less than about 500mm, or less than about 600mm, or less than about 700mm, or less than about 800mm, or less than about 900mm, or less than about 1000mm, or less than about 2m, or less than about 3m, or less than about 4m, or less than about 5m.

In some embodiments, SFS may be applied to a fabric having a width greater than about 100 nm, or greater than about 200 nm, or greater than about 300 nm, or greater than about 400 nm, or greater than about 500 nm, or greater than about 600 nm, or greater than about 700 nm, or greater than about 800 nm, or greater than about 900 nm, or greater than about 1000 nm, or greater than about 2 μm, or greater than about 5 μm, or greater than about 1 0 μm, or greater than about 20 μm, or greater than about 30 μm, or greater than about 40 μm, or greater than about 50 μm, or greater than about 60 μm, or greater than about 70 μm, or greater than about 80 μm, or greater than about 90 μm, or greater than about 100 μm, or greater than about 200 μm, or greater than about 300 μm, or greater than about 400 μm, or greater than about 500 μm, or greater than about 600 μm, or greater than about 700 μm, or greater than about 800μm, or greater than about 900μm, or greater than about 1000μm, or greater than about 2mm, or greater than about 3mm, or greater than about 4mm, or greater than about 5mm, or greater than about 6mm, or greater than about 7mm, or greater than about 8mm, or greater than about 9mm, or greater than about 10mm, or greater than about 20mm, or greater than about 30mm, or greater than about 40mm, or greater than about 50mm, or greater than about 60mm, or greater than about 70mm, or greater than about 80mm, or greater than about 90mm, or greater than about 100mm, or greater than about 200mm, or greater than about 300mm, or greater than about 400mm, or greater than about 500mm, or greater than about 600mm, or greater than about 700mm, or greater than about 800mm, or greater than about 900mm, or greater than about 1000mm, or greater than about 2m, or greater than about 3m, or greater than about 4m, or greater than about 5m.

In some embodiments, SFS may be applied to a fabric having a length less than about 100 nm, or less than about 200 nm, or less than about 300 nm, or less than about 400 nm, or less than about 500 nm, or less than about 600 nm, or less than about 700 nm, or less than about 800 nm, or less than about 900 nm, or less than about 1000 nm, or less than about 2 μm, or less than about 5 μm, or less than about 10 μm, or less than about 20 μm, or less than about 30 μm, or less than about 40 μm, or less than about 50 μm, or less than about 60 μm, or less than about 70 μm, or less than about 80 μm, or less than about 90 μm, or less than about 100 μm, or less than about 200 μm, or less than about 300 μm, or less than about 400 μm, or less than about 500 μm, or less than about 600 μm, or less than about 7 μm. 00μm, or less than about 800μm, or less than about 900μm, or less than about 1000μm, or less than about 2mm, or less than about 3mm, or less than about 4mm, or less than about 5mm, or less than about, or less than about 6mm, or less than about 7mm, or less than about 8mm, or less than about 9mm, or less than about 10mm, or less than about 20mm, or less than about 30mm, or less than about 40mm, or less than about 50mm, or less than about 60mm, or less than about 70mm, or less than about 80mm, or less than about 90mm, or less than about 100mm, or less than about 200mm, or less than about 300mm, or less than about 400mm, or less than about 500mm, or less than about 600mm, or less than about 700mm, or less than about 800mm, or less than about 900mm, or less than about 1000mm.

In some embodiments, SFS can be applied to a fabric having a length greater than about 100 nm, or greater than about 200 nm, or greater than about 300 nm, or greater than about 400 nm, or greater than about 500 nm, or greater than about 600 nm, or greater than about 700 nm, or greater than about 800 nm, or greater than about 900 nm, or greater than about 1000 nm, or greater than about 2 μm, or greater than about 5 μm, or greater than about 10 μm, or greater than about 20 μm, or greater than about 30 μm, or greater than about 40 μm, or greater than about 50 μm, or greater than about 60 μm, or greater than about 70 μm, or greater than about 80 μm, or greater than about 90 μm, or greater than about 100 μm, or greater than about 200 μm, or greater than about 300 μm, or greater than about 400 μm, or greater than about 500 μm, or greater than about 600 μm. Or greater than approximately 700 μm, or greater than approximately 800 μm, or greater than approximately 900 μm, or greater than approximately 1000 μm, or greater than approximately 2 mm, or greater than approximately 3 mm, or greater than approximately 4 mm, or greater than approximately 5 mm, or greater than approximately 6 mm, or greater than approximately 7 mm, or greater than approximately 8 mm, or greater than approximately 9 mm, or greater than approximately 10 mm, or greater than approximately 20 mm, or greater than approximately 30 mm, or greater than approximately 40 mm, or greater than approximately 50 mm, or greater than approximately 60 mm, or greater than approximately 70 mm, or greater than approximately 80 mm, or greater than approximately 90 mm, or greater than approximately 100 mm, or greater than approximately 200 mm, or greater than approximately 300 mm, or greater than approximately 400 mm, or greater than approximately 500 mm, or greater than approximately 600 mm, or greater than approximately 700 mm, or greater than approximately 800 mm, or greater than approximately 900 mm, or greater than approximately 1000 mm.

In some embodiments, SFS may be applied to a fabric having a stretch percentage of less than about 1%, or less than about 2%, or less than about 3%, or less than about 4%, or less than about 5%, or less than about 6%, or less than about 7%, or less than about 8%, or less than about 9%, or less than about 10%, or less than about 20%, or less than about 30%, or less than about 40%, or less than about 50%, or less than about 60%, or less than about 70%, or less than about 80%, or less than about 90%, or less than about 100%, or less than about 110%, or less than about 120%, or less than about 130%, or less than about 140%, or less than about 150%, or less than about 160%, or less than about 170%, or less than about 180%, or less than about 190%, or less than about 200%. The stretch percentage of a fabric with an unstretched width can be determined, and the fabric can be stretched to the stretched width. Then, the unstretched width is subtracted from the stretched width to obtain the net stretched width. The net stretched width is then divided, and the quotient is multiplied by 100 to obtain the stretch percentage (%).

In some embodiments, SFS may be applied to a fabric having a stretch percentage greater than about 1%, or greater than about 2%, or greater than about 3%, or greater than about 4%, or greater than about 5%, or greater than about 6%, or greater than about 7%, or greater than about 8%, or greater than about 9%, or greater than about 10%, or greater than about 20%, or greater than about 30%, or greater than about 40%, or greater than about 50%, or greater than about 60%, or greater than about 70%, or greater than about 80%, or greater than about 90%, or greater than about 100%, or greater than about 110%, or greater than about 120%, or greater than about 130%, or greater than about 140%, or greater than about 150%, or greater than about 160%, or greater than about 170%, or greater than about 180%, or greater than about 190%, or greater than about 200%.

In some embodiments, SFS may be applied to a fabric having a tensile energy (N/ ^cm² ) of less than about 1 cN/ ^cm² , or less than about 2 cN/ ^cm² , or less than about 3 cN/ ^cm² , or less than about 4 cN/ ^cm² , or less than about 5 cN/ ^cm² , or less than about 5 cN/ ^cm² , or less than about 6 cN/cm², or less than about 7 cN/ ^cm² , or less than about 8 cN/ ^{cm² , or less than about 9 cN/cm², or less than about 10 cN/cm², or less than about 20 cN/cm² , or less} than about 30 cN/ ^cm² , or less than about 40 cN/ ^cm² , or less than about 50 cN/ ^cm² , or less than about 60 cN/ ^cm² , or less than about 70 cN/ ^cm² , or less than about 80 cN/cm² ^. Or less than about 90 cN/ ^cm² , or less than about 100 cN/ ^cm² , or less than about 2 N/ ^cm² , or less than about 3 N/ ^cm² , or less than about 4 N/ ^cm² , or less than about 5 N/ ^cm² , or less than about 6 N/ ^cm² , or less than about 7 N/ ^cm² , or less than about 8 N/ ^cm² , or less than about 9 N/ ^cm² , or less than about 10 N/ ^cm² , or less than about 20 N/ ^cm² , or less than about 30 N/ ^cm² , or less than about 40 N/ ^cm² , or less than about 50 N/ ^cm² , or less than about 60 N/ ^cm² , or less than about 70 N/ ^cm² , or less than about 80 N/ ^cm² , or less than about 90 N/ ^cm² , or less than about 100 N/ ^cm² Or less than about 150 N/ ^cm² , or less than about 200 N/ ^cm² .

In some embodiments, SFS may be applied to a fabric having a tensile energy (N/ ^cm² ) greater than about 1 cN/ ^cm² , or greater than about 2 cN/ ^cm² , or greater than about 3 cN/ ^cm² , or greater than about 4 cN/ ^cm² , or greater than about 5 cN/ ^cm² , or greater than about 5 cN/ ^cm² , or greater than about 6 cN/ ^cm² , or greater than about 7 cN/ ^cm² , or greater than about 8 cN/ ^cm² , or greater than about 9 cN/ ^cm² , or greater than about 10 cN/ ^cm² , or greater than about 20 cN/ ^cm² , or greater than about 30 cN/ ^cm² , or greater than about 40 cN/ ^cm² , or greater than about 50 cN/ ^cm² , or greater than about 60 cN/ ^cm² , or greater than about 70 cN/ ^cm² , or greater than about 80 cN/cm² ^. Or greater than approximately 90 cN/ ^cm² , or greater than approximately 100 cN/ ^cm² , or greater than approximately 2 N/ ^cm² , or greater than approximately 3 N/ ^cm² , or greater than approximately 4 N/ ^cm² , or greater than approximately 5 N/ ^cm² , or greater than approximately 6 N/ ^cm² , or greater than approximately 7 N/ ^cm² , or greater than approximately 8 N/ ^cm² , or greater than approximately 9 N/ ^cm² , or greater than approximately 10 N/ ^cm² , or greater than approximately 20 N/ ^cm² , or greater than approximately 30 N/ ^cm² , or greater than approximately 40 N/ ^cm² , or greater than approximately 50 N/ ^cm² , or greater than approximately 60 N/ ^cm² , or greater than approximately 70 N/ ^cm² , or greater than approximately 80 N/ ^cm² , or greater than approximately 90 N/ ^cm² , or greater than approximately 100 N/ ^cm² Or greater than approximately 150 N/ ^cm² , or greater than approximately 200 N/ ^cm² .

In some embodiments, SFS may be applied to a fabric having a shear stiffness (N/cm⁻¹) of less than about 1 cN/cm⁻¹, or less than about 2 cN/cm⁻¹, or less than about 3 cN/cm⁻¹, or less than about 4 cN/cm⁻¹, or less than about 5 cN/cm⁻¹, or less than about 5 cN/cm⁻¹, or less than about 6 cN/cm⁻¹, or less than about 7 cN/cm⁻¹, or less than about 8 cN/cm⁻¹, or less than about 9 cN/cm⁻¹, or less than about 10 cN/cm⁻¹, or less than about 20 cN/cm⁻¹, or less than about 30 cN/cm⁻¹, or less than about 40 cN/cm⁻¹, or less than about 50 cN/cm⁻¹, or less than about 60 cN/cm⁻¹, or less than about 70 cN/cm⁻¹, or less than about 80 cN/cm⁻¹, or less than... At approximately 90 cN/cm-degree, or less than approximately 100 cN/cm-degree, or less than approximately 2 N/cm-degree, or less than approximately 3 N/cm-degree, or less than approximately 4 N/cm-degree, or less than approximately 5 N/cm-degree, or less than approximately 6 N/cm-degree, or less than approximately 7 N/cm-degree, or less than approximately 8 N/cm-degree, or less than approximately 9 N/cm-degree, or less than approximately 10 N/cm-degree, or less than approximately 20 N/cm-degree, or less than approximately 30 N/cm-degree, or less than approximately 40 N/cm-degree, or less than approximately 50 N/cm-degree, or less than approximately 60 N/cm-degree, or less than approximately 70 N/cm-degree, or less than approximately 80 N/cm-degree, or less than approximately 90 N/cm-degree, or less than approximately 100 N/cm-degree, or less than approximately 150 N/cm-degree, or less than approximately 200 N/cm-degree.

In some embodiments, SFS may be applied to a fabric having a shear stiffness (N/cm⁻¹) greater than about 1 cN/cm⁻¹, or greater than about 2 cN/cm⁻¹, or greater than about 3 cN/cm⁻¹, or greater than about 4 cN/cm⁻¹, or greater than about 5 cN/cm⁻¹, or greater than about 5 cN/cm⁻¹, or greater than about 6 cN/cm⁻¹, or greater than about 7 cN/cm⁻¹, or greater than about 8 cN/cm⁻¹, or greater than about 9 cN/cm⁻¹, or greater than about 10 cN/cm⁻¹, or greater than about 20 cN/cm⁻¹, or greater than about 30 cN/cm⁻¹, or greater than about 40 cN/cm⁻¹, or greater than about 50 cN/cm⁻¹, or greater than about 60 cN/cm⁻¹, or greater than about 70 cN/cm⁻¹, or greater than about 80 cN/cm⁻¹, or greater than... At approximately 90 cN/cm-degree, or greater than approximately 100 cN/cm-degree, or greater than approximately 2 N/cm-degree, or greater than approximately 3 N/cm-degree, or greater than approximately 4 N/cm-degree, or greater than approximately 5 N/cm-degree, or greater than approximately 6 N/cm-degree, or greater than approximately 7 N/cm-degree, or greater than approximately 8 N/cm-degree, or greater than approximately 9 N/cm-degree, or greater than approximately 10 N/cm-degree, or greater than approximately 20 N/cm-degree, or greater than approximately 30 N/cm-degree, or greater than approximately 40 N/cm-degree, or greater than approximately 50 N/cm-degree, or greater than approximately 60 N/cm-degree, or greater than approximately 70 N/cm-degree, or greater than approximately 80 N/cm-degree, or greater than approximately 90 N/cm-degree, or greater than approximately 100 N/cm-degree, or greater than approximately 150 N/cm-degree, or greater than approximately 200 N/cm-degree.

In some embodiments, SFS may be applied to a fabric having a flexural stiffness (N· ^cm² /cm) of less than about 1 cN· ^cm² /cm, or less than about 2 cN· ^cm² /cm, or less than about 3 cN· ^cm² /cm, or less than about 4 cN· ^cm² /cm, or less than about 5 cN· ^cm² /cm, or less than about 5 cN· ^cm² /cm, or less than about 6 cN· ^cm² /cm, or less than about 7 cN· ^cm² /cm, or less than about 8 cN· ^cm² /cm, or less than about 9 cN· ^cm² /cm, or less than about 10 cN· ^cm² /cm, or less than about 20 cN· ^cm² /cm, or less than about 30 cN· ^cm² /cm, or less than about 40 cN· ^cm² /cm, or less than about 50 cN· ^cm² /cm, or less than about 60 cN·cm²/cm ^. /cm, or less than about 70 cN· ^cm² /cm, or less than about 80 cN· ^cm² /cm, or less than about 90 cN· ^cm² /cm, or less than about 100 cN· ^cm² /cm, or less than about 2 N· ^cm² /cm, or less than about 3 N· ^cm² /cm, or less than about 4 N· ^cm² /cm, or less than about 5 N· ^cm² /cm, or less than about 6 N· ^cm² /cm, or less than about 7 N· ^cm² /cm, or less than about 8 N· ^cm² /cm, or less than about 9 N· ^cm² /cm, or less than about 10 N· ^cm² /cm, or less than about 20 N· ^cm² /cm, or less than about 30 N· ^cm² /cm, or less than about 40 N· ^cm² /cm, or less than about 50 N· ^cm² /cm, or less than about 60 N· ^cm² /cm, or less than about 70 N·cm²/cm ^. /cm, or less than about 80 N· ^cm² /cm, or less than about 90 N· ^cm² /cm, or less than about 100 N· ^cm² /cm, or less than about 150 N· ^cm² /cm, or less than about 200 N· ^cm² /cm.

In some embodiments, SFS may be applied to a fabric having a flexural stiffness (N· ^cm² /cm) greater than about 1 cN· ^cm² /cm, or greater than about 2 cN· ^cm² /cm, or greater than about 3 cN· ^cm² /cm, or greater than about 4 cN· ^cm² /cm, or greater than about 5 cN· ^cm² /cm, or greater than about 5 cN· ^cm² /cm, or greater than about 6 cN·cm²/cm, or greater than about ⁷ cN· ^cm² /cm, or greater than about 8 cN· ^cm² /cm, or greater than about 9 cN· ^cm² /cm, or greater than about 10 cN· ^cm² /cm, or greater than about 20 cN· ^cm² /cm, or greater than about 30 cN· ^cm² /cm, or greater than about 40 cN· ^cm² /cm, or greater than about 50 cN· ^cm² /cm, or greater than about 60 cN·cm²/cm ^. /cm, or greater than about 70 cN· ^cm² /cm, or greater than about 80 cN· ^cm² /cm, or greater than about 90 cN· ^cm² /cm, or greater than about 100 cN· ^cm² /cm, or greater than about 2 N· ^cm² /cm, or greater than about 3 N· ^cm² /cm, or greater than about 4 N· ^cm² /cm, or greater than about 5 N· ^cm² /cm, or greater than about 6 N· ^cm² /cm, or greater than about 7 N· ^cm² /cm, or greater than about 8 N· ^cm² /cm, or greater than about 9 N· ^cm² /cm, or greater than about 10 N· ^cm² /cm, or greater than about 20 N· ^cm² /cm, or greater than about 30 N· ^cm² /cm, or greater than about 40 N· ^cm² /cm, or greater than about 50 N· ^cm² /cm, or greater than about 60 N· ^cm² /cm, or greater than about 70 N·cm²/cm ^. /cm, or greater than about 80 N· ^cm² /cm, or greater than about 90 N· ^cm² /cm, or greater than about 100 N· ^cm² /cm, or greater than about 150 N· ^cm² /cm, or greater than about 200 N· ^cm² /cm.

In some embodiments, SFS may be applied to a fabric having a compressive energy (N·cm/ ^cm² ) of less than about 1 cN·cm/ ^cm² , or less than about 2 cN·cm/ ^cm² , or less than about 3 cN·cm/ ^cm² , or less than about 4 cN·cm/ ^cm² , or less than about 5 cN·cm/ ^cm² , or less than about 6 cN·cm/ ^cm² , or less than about 7 cN·cm/ ^cm² , or less than about 8 cN·cm/ ^cm² , or less than about 9 cN·cm/ ^cm² , or less than about ¹⁰ cN·cm/ ^cm² , or less than about 20 cN·cm/ ^cm² , or less than about 30 cN·cm/ ^cm² , or less than about 40 cN·cm/ ^cm² , or less than about 50 cN·cm/cm² ^. Or less than about 60 cN·cm/ ^cm² , or less than about 70 cN·cm/ ^cm² , or less than about 80 cN·cm/ ^cm² , or less than about 90 cN·cm/ ^cm² , or less than about 100 cN·cm/ ^cm² , or less than about 2 N·cm/ ^cm² , or less than about 3 N·cm/ ^cm² , or less than about 4 N·cm/ ^cm² , or less than about 5 N·cm/ ^cm² , or less than about 6 N·cm/ ^cm² , or less than about 7 N·cm/ ^cm² , or less than about 8 N·cm/ ^cm² , or less than about 9 N·cm/ ^cm² , or less than about 10 N·cm/ ^cm² , or less than about 20 N·cm/ ^cm² , or less than about 30 N·cm/ ^cm² , or less than about 40 N·cm/ ^cm² Or less than about 50 N·cm/ ^cm² , or less than about 60 N·cm/ ^cm² , or less than about 70 N·cm/ ^cm² , or less than about 80 N·cm/ ^cm² , or less than about 90 N·cm/ ^cm² , or less than about 100 N·cm/ ^cm² , or less than about 150 N·cm/ ^cm² , or less than about 200 N·cm/ ^cm² .

In some embodiments, SFS may be applied to a fabric having a compressive energy (N·cm/ ^cm² ) greater than about 1 cN·cm/ ^cm² , or greater than about 2 cN·cm/ ^cm² , or greater than about 3 cN·cm/ ^cm² , or greater than about 4 cN·cm/ ^cm² , or greater than about 5 cN·cm/ ^cm² , or greater than about 6 cN·cm/ ^cm² , or greater than about 7 cN·cm/ ^cm² , or greater than about 8 cN·cm/ ^cm² , or greater than about 9 cN·cm/ ^cm² , or greater than about ¹⁰ cN·cm/ ^cm² , or greater than about 20 cN·cm/ ^cm² , or greater than about 30 cN·cm/ ^cm² , or greater than about 40 cN·cm/ ^cm² , or greater than about 50 cN·cm/cm² ^. Or greater than about 60 cN·cm/ ^cm² , or greater than about 70 cN·cm/ ^cm² , or greater than about 80 cN·cm/ ^cm² , or greater than about 90 cN·cm/ ^cm² , or greater than about 100 cN·cm/ ^cm² , or greater than about 2 N·cm/ ^cm² , or greater than about 3 N·cm/ ^cm² , or greater than about 4 N·cm/ ^cm² , or greater than about 5 N·cm/ ^cm² , or greater than about 6 N·cm/ ^cm² , or greater than about 7 N·cm/ ^cm² , or greater than about 8 N·cm/ ^cm² , or greater than about 9 N·cm/ ^cm² , or greater than about 10 N·cm/ ^cm² , or greater than about 20 N·cm/ ^cm² , or greater than about 30 N·cm/ ^cm² , or greater than about 40 N·cm/ ^cm² Or greater than about 50 N·cm/ ^cm² , or greater than about 60 N·cm/ ^cm² , or greater than about 70 N·cm/ ^cm² , or greater than about 80 N·cm/ ^cm² , or greater than about 90 N·cm/ ^cm² , or greater than about 100 N·cm/ ^cm² , or greater than about 150 N·cm/ ^cm² , or greater than about 200 N·cm/ ^cm² .

In some embodiments, SFS may be applied to a fabric having a coefficient of friction less than about 0.04, or less than about 0.05, or less than about 0.06, or less than about 0.07, or less than about 0.08, or less than about 0.09, or less than about 0.10, or less than about 0.10, or less than about 0.15, or less than about 0.20, or less than about 0.25, or less than about 0.30, or less than about 0.35, or less than about 0.40, or less than about 0.45, or less than about 0.50, or less than about 0.55, or less than about 0.60, or less than about 0.65, or less than about 0.70, or less than about 0.75, or less than about 0.80, or less than about 0.85, or less than about 0.90, or less than about 0.95, or less than about 1.00, or less than about 1.05.

In some embodiments, SFS may be applied to a fabric having a coefficient of friction greater than about 0.04, or greater than about 0.05, or greater than about 0.06, or greater than about 0.07, or greater than about 0.08, or greater than about 0.09, or greater than about 0.10, or greater than about 0.10, or greater than about 0.15, or greater than about 0.20, or greater than about 0.25, or greater than about 0.30, or greater than about 0.35, or greater than about 0.40, or greater than about 0.45, or greater than about 0.50, or greater than about 0.55, or greater than about 0.60, or greater than about 0.65, or greater than about 0.70, or greater than about 0.75, or greater than about 0.80, or greater than about 0.85, or greater than about 0.90, or greater than about 0.95, or greater than about 1.00, or greater than about 1.05.

In some embodiments, chemical finishing agents may be applied to textiles before or after coating them with SFS. In one embodiment, chemical finishing may be intended to apply chemical reagents and/or SFS to textiles, including fibers, yarns, and fabrics, or to garments made from such fibers, yarns, and fabrics, to alter the properties of the original textile or garment and to achieve properties that were not originally present in the textile or garment. Regarding the chemical finishing agent, textiles treated with such a chemical finishing agent may act as a surface treatment agent and/or the treatment agent may alter the elemental analysis of the matrix polymer of the treated textile.

In one embodiment, a type of chemical finishing may include applying a solution of certain silk core proteins to the textile. For example, SFS may be applied to the fabric after dyeing, but there are also cases where SFS may need to be applied during processing, during dyeing, or after the selected textiles or fabrics, threads, or yarns are assembled into garments. In some embodiments, after application, the SFS may be dried using heat. The SFS may then be fixed to the surface of the textile in a treatment step known as curing.

In some embodiments, SFS may be provided in a concentrated form suspended in water. In some embodiments, the SFS may have a concentration, by weight (%w/w or %w/v) or by volume (v/v) of less than about 50%, or less than about 45%, or less than about 40%, or less than about 35%, or less than about 30%, or less than about 25%, or less than about 20%, or less than about 15%, or less than about 10%, or less than about 5%, or less than about 4%, or less than about 3%, or less than about 2%, or less than about 1%, or less than about 0.1%, or less than about 0.01%, or less than about 0.001%, or less than about 0.0001%, or less than about 0.00001%. In some embodiments, the SFS may have a concentration greater than about 50% by weight (%w/w or %w/v) or greater than about 45% by volume (v/v), or greater than about 40% by weight, or greater than about 35% by volume, or greater than about 30% by volume, or greater than about 25% by volume, or greater than about 20% by volume, or greater than about 15% by volume, or greater than about 10% by volume, or greater than about 5% by volume, or greater than about 4% by volume, or greater than about 3% by volume, or greater than about 2% by volume, or greater than about 1% by volume, or greater than about 0.1% by volume, or greater than about 0.01% by volume, or greater than about 0.001% by volume, or greater than about 0.00001%.

In some embodiments, the solution concentration and the moisture absorption rate of the material determine the amount of silk core protein solution (SFS), which may contain silk-based proteins or fragments thereof, which can be fixed or adhered to the coated textile. The moisture absorption rate can be expressed as follows:

The total amount of SFS added to textile materials can be expressed by the following formula:

Regarding methods for more broadly applying SFS to textiles, SFS can be applied to textiles via pad or roller application processes, saturation and removal processes, and/or localized application processes. Furthermore, methods of filament application (i.e., SFS application or coating) can include bath coating, light-touch roller coating, spray coating, and/or double-sided roller coating. In some embodiments, the coating process (e.g., bath coating, light-touch roller coating, spray coating, double-sided roller coating, roller coating, saturation and removal application, and/or localized application), drying process, and curing process can be varied as described herein to alter one or more selected textile (e.g., fabric) properties of the resulting coated textile, wherein such properties include, but are not limited to, wetting time, absorption rate, spreading speed, cumulative unidirectional transport, and/or overall moisture management capability. In some embodiments, the aforementioned selected properties can be enhanced by modifying one or more of the coating process, drying process, and curing process as described herein.

In one implementation, pad application can be used on dry or wet textiles. For example, it can be applied to the fabric after the dyeing process. The fabric can be fed into a water bath solution and saturated. The fabric to be coated can then be passed through a set of rollers, thereby extracting excess bath solution to achieve the desired moisture absorption percentage based on several variables. Variables affecting the moisture absorption percentage include roller pressure and material, fabric composition and structure, and SFS viscosity.

In one embodiment, padding applied to wet textiles can be used to reduce the cost of drying fabrics after dyeing. The fabric exiting the padding rollers can retain a higher percentage by weight than the fabric entering the padding rollers to maintain SFS deposition on the fabric; any dilution of the SFS solution due to water present on the incoming fabric may need to be taken into account.

In one implementation, saturation and removal application is a low moisture absorption method, which can, for example, address some of the problems associated with removing large amounts of water during the drying process. Since the fabric can be dried from the outer surface inwards in the oven, water can migrate from the inside out, resulting in a higher coating concentration on the outer surface. At lower water content, migration can be reduced due to the higher viscosity of the solution. However, reduced moisture absorption can lead to uneven solution deposition.

In one embodiment, vacuum suction can be used as a method for achieving low moisture absorption. The saturated fabric can be subjected to a vacuum, which draws the solution out of the fabric and returns it to the application ring. Air jetting can also be a method for providing low moisture absorption. The saturated fabric can be subjected to high-pressure steam, which removes the solution from the fabric and returns it to the application ring.

In one implementation, the porous bowl method can be used for low moisture absorption. Solid pad rollers can be replaced with rubber-coated fiber rollers. Saturated fabrics can withstand the pressure of the rollers because the roller's porosity allows more solution to be extruded from the fabric.

In one embodiment, the transfer padding method can be used for low moisture absorption. The saturated fabric can be dried through two consecutive drying processes with a nonwoven fabric and can be compressed under low pressure. Excess solution can be extracted from the treated fabric using the nonwoven fabric.

In one implementation, localized application can be used as a low moisture absorption rate application method, which deposits the required amount of SFS onto the fabric without removing any excess material. The method described above can be used for single-sided coating application, but variations exist that allow for double-sided coating.

In one embodiment, light-touch roller coating can be used as a localized application method to transfer SFS from a roller (i.e., a kissing roller) to one side of the fabric. Solution viscosity, roller surface finishing agent, roller speed, fabric speed, fabric contact angle on the roller, and fabric properties are parameters that control the amount of solution deposited on the fabric.

In one implementation, a variation of the kissing roller technology could be the Triatex MA system, which uses two moisture content sensors to determine the amount of solution absorbed at the kissing roller and adjusts controllable variables of the kissing roller to maintain consistency in solution deposition onto the fabric.

In one implementation, ring transfer application can be used as a localized application method that transfers the SFS from the saturated ring fabric to the fabric to be coated between low-pressure pad rollers. A two-roller configuration allows for minimized contact with the fabric, while a three-roller configuration allows for greater contact with the fabric.

In one implementation, engraved roller application can be used as a localized application method to transfer metered SFS onto a fabric. This can be achieved by engraving a pattern with precise depth and design containing controlled amounts of SFS onto the surface of the roller. A blade can be used to remove any solution deposited on the roller surface to maintain consistent transfer of the solution to the fabric to be coated.

In one embodiment, rotary screen printing can be used as a localized application method, which deposits SFS onto the fabric by allowing a solution to permeate through the screen of the roller. The solution can be contained at a set level in the screen printing roller core, while any excess solution can be removed from the inner roller wall using a blade to provide a clean surface for the next rotation of the screen printing roller.

In one embodiment, magnetic roller coating can be used as a localized application method that deposits SFS from a kissing roller onto the fabric to be coated. The kissing roller is partially immersed in the bath solution, and the magnetic field generated in the fabric drive roller determines the magnitude of the pressure applied by the kissing roller, thereby controlling the solution absorption rate.

In one implementation, spraying can be used as a localized application method, which transfers SFS onto the fabric via an atomized solution. The spray pattern can be controlled by nozzle pattern, size, and airflow. Spraying application can be used for single-sided or double-sided application.

In one implementation, foam application can be performed using a localized application method that transfers the SFS (Sparkling Foam Solution) onto the fabric. The amount of water applied to the fabric can be reduced by replacing a portion of the water in the solution with air to generate the foam. Foam application can be used for single-sided or double-sided application, where the same foam can be deposited via a squeeze roller, or different foam solutions can be provided via a transfer roller or a slit applicator.

In one embodiment, the application of SFS can be performed after garment assembly. In another embodiment, the process can take place in a washing and dyeing machine or a spray booth. For example, the washing and dyeing machine may be shaped like a household front-loading washing machine, allowing the process to be performed when the dyeing is exhausted or having a separate processing cycle. In one embodiment, the spray booth machine may include a manual or fully automated process. For example, the garment may be worn by a mannequin, while an operator or humanoid robot sprays the solution onto the fabric.

In one implementation, the SFS may be an aqueous solution, which, after being applied to the textile, may require thermal vaporization to infuse the SFS into the textile. Thermal vaporization can be applied by using devices such as infrared or radio frequency dryers to transfer heat via radiation.

In one implementation, thermal vaporization can be applied by convection of hot air circulating in an oven to reach the desired temperature, while the fabric is clamped and conveyed by a conveyor belt. This allows for complete control over the fabric width dimensions.

In one implementation, thermal vaporization can be applied through conduction, bringing the textile into contact with heated rollers or calendering rollers. Since the fabric is not clamped, control over the fabric width is minimal.

In one implementation, curing of SFS on textiles can be accomplished using the same equipment used for thermal vaporization in continuous or individual cycles.

In one embodiment, the curing time and temperature can depend on the polymer content of the textile and the preferred combination method of the SFS with the specific polymer. The curing process may not begin until thermal vaporization is complete.

In some implementations, sensors can be used to monitor SFS deposition on textiles as well as drying and curing steps.

In some implementations, non-contact sensors, such as the Pleva AF120 sensor based on water-based microwave absorption, can be used to monitor SFS deposition. Material moisture content can be measured based on water-based microwave absorption. A semiconductor oscillator transmits microwave energy via a network. The unabsorbed portion of the energy can be received by a microwave receiver on the opposite side. The absorption amount is a measurement of the absolute moisture content. Microwave sensors are capable of detecting and measuring moisture content from a minimum of 0 to 2000 g _H₂O / ^m² .

In some implementations, for wide-width fabric processing, multiple sensors can be paired in parallel to transmit data analysis to a centralized control system loop that can add more solution to the lower areas of the fabric.

In some implementations, another microwave-based sensor, such as Mahlo's Aqualot, can be used. Instead of measuring the attenuation of microwaves by the number of water molecules in the gap, the sensor assesses the shift in the resonant frequencies of the two standing waves relative to each other.

In some implementations, another non-contact sensor for SFS can be MoistTech's IR-3000, which is based on near-infrared sensing technology. This sensor measures the near-infrared energy reflected at a given wavelength, which is inversely proportional to the number of absorbing molecules in the fabric.

In some implementations, residual moisture at the end of the curing process can be measured to further confirm the drying and curing process. In addition to the sensors mentioned above, Mahlo's contact sensors (such as the Textometer RMS) can also be used to measure humidity via conductivity.

In some implementations, monitoring the end of the drying process phase can be achieved by measuring the fabric temperature using a non-contact temperature sensor. When the wet product enters the dryer, it is first heated to its cooling limit temperature. In some implementations, the product temperature may begin to rise again when the water content drops to a residual moisture level. The closer the product temperature is to the circulating air temperature in the dryer, the slower the temperature continues to rise. In some implementations, the temperature required for processing, fixing, or condensation is reached at a certain temperature threshold (referred to as the set temperature).

In some implementations, to determine the dwell time at the desired product temperature, a high-temperature resistant infrared pyrometer can be used to non-contactly measure the surface temperature of the product at multiple locations within the dryer. The Mahlo Permaset VMT is an infrared pyrometer that can be assembled into multiple units to monitor the temperature of the entire dryer. Setex is another manufacturer that provides fabric temperature sensors for dryers and ovens, such as models WTM V11, V21, and V41.

In some embodiments, SFS can be applied to the textile during immersion dyeing. In some embodiments, the process may involve adding the fabric to a bath initially called a batch and allowing the fabric to equilibrate with the solution. Immersion dyeing can be the ability of silk core protein molecules to move from the solution to the fibers or threads of the textile (directness). The directness of silk core proteins can be affected by temperature or additives (such as salt).

In some implementations, the immersion process can take anywhere from a few minutes to several hours. Once the fabric has absorbed or fixed as much of the silk core protein as possible, the bath can be emptied and the fabric can be rinsed to remove any excess solution.

In some implementations, an important parameter in the dyeing process can be the so-called specific liquor ratio. It describes the ratio of the mass of the fabric to the volume of the SFS bath and determines the amount of silk core protein deposited on the textile.

In some implementations, SFS can be applied to textiles during the jet dyeing process. The jet dyeing machine can be formed by a closed tubular system in which the fabric is placed. To transport the fabric through the tubes, the dye liquor is jetted via venturi tubes. The jetting can create turbulence. This can facilitate SFS penetration and prevent the fabric from contacting the tube walls. For example, since the fabric is typically exposed to a relatively high concentration of liquid within the transport tubes, a small SFS bath is required at the bottom of the container. This arrangement can be sufficient for smooth movement of the container from back to front.

In some implementations, SFS can be applied during paddle dyeing. Paddle dyeing machines are generally applicable to a variety of textiles, but this method is best suited for garments. Heat can be generated by directly injecting steam into the coating bath. In one implementation, the paddle dyeing machine is operated by paddles that circulate the bath and garments in a perforated central island. SFS, water, and heated steam are added here. An overhead paddle machine can be described as a bucket with paddles having full-width blades. The blades are typically submerged several centimeters into the bucket. This action agitates the bath and pushes the garments to be dyed downwards, thus immersing them in the dye solution.

In some embodiments, the processing methods described herein can be used to apply SFS to textiles using one or more of the following parameters, including but not limited to fabric speed, solution viscosity, solution added to the fabric, fabric width, drying temperature, drying time, curing time, fabric tension, padding pressure, padding roll Shore hardness, spreader temperature, and common drying and curing temperatures. In one embodiment, the processing method parameters may also include condensation temperature, which can vary depending on the chemical scheme used to apply SFS to the textiles.

In one embodiment, the fabric speed used in the method of this disclosure may be less than about 0.1 m/min, or less than about 0.2 m/min, or less than about 0.3 m/min, or less than about 0.4 m/min, or less than about 0.5 m/min, or less than about 0.6 m/min, or less than about 0.7 m/min, or less than about 0.8 m/min, or less than about 0.9 m/min, or less than about 1 m/min, or less than about 2 m/min, or less than about 3 m/min, or less than about 4 m/min, or less than about 5 m/min, or less than about 6 m/min, or less than about 7 m/min, or less than about 8 m/min, or less than about 9 m/min, or less than about 10 m/min, or less than about 20 m/min, or less than about 30 m/min, or less than about 40 m/min, or less than about 50 m/min, or less than about 60 m/min.

In one embodiment, the fabric speed used in the method of this disclosure may be greater than about 0.1 m/min, or greater than about 0.2 m/min, or greater than about 0.3 m/min, or greater than about 0.4 m/min, or greater than about 0.5 m/min, or greater than about 0.6 m/min, or greater than about 0.7 m/min, or greater than about 0.8 m/min, or greater than about 0.9 m/min, or greater than about 1 m/min, or greater than about 2 m/min, or greater than about 3 m/min, or greater than about 4 m/min, or greater than about 5 m/min, or greater than about 6 m/min, or greater than about 7 m/min, or greater than about 8 m/min, or greater than about 9 m/min, or greater than about 10 m/min, or greater than about 20 m/min, or greater than about 30 m/min, or greater than about 40 m/min, or greater than about 50 m/min, or greater than about 60 m/min.

In one embodiment, the solution viscosity used in the method of this disclosure may be less than about 1000 mPas, or less than about 1500 mPas, or less than about 2000 mPas, or less than about 2500 mPas, or less than about 3000 mPas, or less than about 4000 mPas, or less than about 4500 mPas, or less than about 5000 mPas, or less than about 5500 mPas, or less than about 6000 mPas, or less than about 6500 mPas. 00 mPas, or less than about 7000 mPas, or less than about 7500 mPas, or less than about 8000 mPas, or less than about 8500 mPas, or less than about 9000 mPas, or less than about 9500 mPas, or less than about 10000 mPas, or less than about 10500 mPas, or less than about 11000 mPas, or less than about 11500 mPas, or less than about 12000 mPas.

In one embodiment, the solution viscosity used in the method of this disclosure may be greater than about 1000 mPas, or greater than about 1500 mPas, or greater than about 2000 mPas, or greater than about 2500 mPas, or greater than about 3000 mPas, or greater than about 4000 mPas, or greater than about 4500 mPas, or greater than about 5000 mPas, or greater than about 5500 mPas, or greater than about 6000 mPas, or greater than about 6500 mPas. 00 mPas, or greater than about 7000 mPas, or greater than about 7500 mPas, or greater than about 8000 mPas, or greater than about 8500 mPas, or greater than about 9000 mPas, or greater than about 9500 mPas, or greater than about 10000 mPas, or greater than about 10500 mPas, or greater than about 11000 mPas, or greater than about 11500 mPas, or greater than about 12000 mPas.

In one embodiment, for the method of this disclosure, the solution may be added to textiles (e.g., fabrics) in an amount less than about 0.01 g/ ^m² , or less than about 0.02 g/ ^m² , or less than about 0.03 g/ ^m² , or less than about 0.04 g/ ^m² , or less than about 0.05 g/ ^m² , or less than about 0.06 g/ ^m² , or less than about 0.07 g/ ^m² , or less than about 0.08 g/ ^m² , or less than about 0.09 g/ ^m² , or less than about 0.10 g/ ^m² , or less than about 0.2 g/ ^m² , or less than about 0.3 g/ ^m² , or less than about 0.4 g/ ^m² , or less than about 0.5 g/ ^m² , or less than about 0.6 g/ ^m² , or less than about 0.7 g/ ^m² , or less than about 0.8 g/m². ^2. or less than about 0.9 g/ ^m² , or less than about 1 g/ ^m² , or less than about 2 g/ ^m² , or less than about 3 g/ ^m² , or less than about 4 g/ ^m² , or less than about 5 g/ ^m² , or less than about 6 g/ ^m² , or less than about 7 g/ ^m² , or less than about 8 g/ ^m² , or less than about 9 g/ ^m² , or less than about 10 g/ ^m² , or less than about 20 g/ ^m² , or less than about 30 g/ ^m² , or less than about 40 g/ ^m² , or less than about 50 g/ ^m² , or less than about 60 g/ ^m² , or less than about 70 g/ ^m² , or less than about 80 g/ ^m² , or less than about 90 g/ ^m² , or less than about 100 g/ ^m² .

In one embodiment, for the method of this disclosure, the solution may be added to textiles (e.g., fabrics) in an amount greater than about 0.01 g/ ^m² , or greater than about 0.02 g/ ^m² , or greater than about 0.03 g/ ^m² , or greater than about 0.04 g/ ^m² , or greater than about 0.05 g/ ^m² , or greater than about 0.06 g/ ^m² , or greater than about 0.07 g/ ^m² , or greater than about 0.08 g/ ^m² , or greater than about 0.09 g/ ^m² , or greater than about 0.10 g/ ^m² , or greater than about 0.2 g/ ^m² , or greater than about 0.3 g/ ^m² , or greater than about 0.4 g/ ^m² , or greater than about 0.5 g/ ^m² , or greater than about 0.6 g/ ^m² , or greater than about 0.7 g/ ^m² , or greater than about 0.8 g/m². ^2. or greater than about 0.9 g/ ^m² , or greater than about 1 g/ ^m² , or greater than about 2 g/ ^m² , or greater than about 3 g/ ^m² , or greater than about 4 g/ ^m² , or greater than about 5 g/ ^m² , or greater than about 6 g/ ^m² , or greater than about 7 g/ ^m² , or greater than about 8 g/ ^m² , or greater than about 9 g/ ^m² , or greater than about 10 g/ ^m² , or greater than about 20 g/ ^m² , or greater than about 30 g/ ^m² , or greater than about 40 g/ ^m² , or greater than about 50 g/ ^m² , or greater than about 60 g/ ^m² , or greater than about 70 g/ ^m² , or greater than about 80 g/ ^m² , or greater than about 90 g/ ^m² , or greater than about 100 g/ ^m² .

In one embodiment, the fabric width used in the method of this disclosure may be less than about 1 mm, or less than about 2 mm, or less than about 3 mm, or less than about 4 mm, or less than about 5 mm, or less than about 6 mm, or less than about 7 mm, or less than about 8 mm, or less than about 9 mm, or less than about 10 mm, or less than about 20 mm, or less than about 30 mm, or less than about 40 mm, or less than about 50 mm, or less than about 60 mm, or less than about 70 mm, or less than about 80 mm. m, or less than about 90 mm, or less than about 100 mm, or less than about 200 mm, or less than about 300 mm, or less than about 400 mm, or less than about 500 mm, or less than about 600 mm, or less than about 700 mm, or less than about 800 mm, or less than about 900 mm, or less than about 1000 mm, or less than about 2000 mm, or less than about 2000 mm, or less than about 3000 mm, or less than about 4000 mm, or less than about 5000 mm.

In one embodiment, the fabric width used in the method of this disclosure may be greater than about 1 mm, or greater than about 2 mm, or greater than about 3 mm, or greater than about 4 mm, or greater than about 5 mm, or greater than about 6 mm, or greater than about 7 mm, or greater than about 8 mm, or greater than about 9 mm, or greater than about 10 mm, or greater than about 20 mm, or greater than about 30 mm, or greater than about 40 mm, or greater than about 50 mm, or greater than about 60 mm, or greater than about 70 mm, or greater than about 80 mm. m, or greater than about 90 mm, or greater than about 100 mm, or greater than about 200 mm, or greater than about 300 mm, or greater than about 400 mm, or greater than about 500 mm, or greater than about 600 mm, or greater than about 700 mm, or greater than about 800 mm, or greater than about 900 mm, or greater than about 1000 mm, or greater than about 2000 mm, or greater than about 2000 mm, or greater than about 3000 mm, or greater than about 4000 mm, or greater than about 5000 mm.

In one embodiment, the drying and/or curing temperature used in the methods of this disclosure may be less than about 70°C, or less than about 75°C, or less than about 80°C, or less than about 85°C, or less than about 90°C, or less than about 95°C, or less than about 100°C, or less than about 110°C, or less than about 120°C, or less than about 130°C, or less than about 140°C, or less than about 150°C, or less than about 160°C, or less than about 170°C, or less than about 180°C, or less than about 190°C, or less than about 200°C, or less than about 210°C, or less than about 220°C, or less than about 230°C.

In one embodiment, the drying and/or curing temperature used in the methods of this disclosure may be greater than about 70°C, or greater than about 75°C, or greater than about 80°C, or greater than about 85°C, or greater than about 90°C, or greater than about 95°C, or greater than about 100°C, or greater than about 110°C, or greater than about 120°C, or greater than about 130°C, or greater than about 140°C, or greater than about 150°C, or greater than about 160°C, or greater than about 170°C, or greater than about 180°C, or greater than about 190°C, or greater than about 200°C, or greater than about 210°C, or greater than about 220°C, or greater than about 230°C.

In one embodiment, the drying time for the method of this disclosure may be less than about 10 seconds, or less than about 20 seconds, or less than about 30 seconds, or less than about 40 seconds, or less than about 50 seconds, or less than about 60 seconds, or less than about 2 minutes, or less than about 3 minutes, or less than about 4 minutes, or less than about 5 minutes, or less than about 6 minutes, or less than about 7 minutes, or less than about 8 minutes, or less than about 9 minutes, or less than about 10 minutes, or less than about 20 minutes, or less than about 30 minutes, or less than about 40 minutes, or less than about 50 minutes, or less than about 60 minutes.

In one embodiment, the drying time for the method of this disclosure may be greater than about 10 seconds, or greater than about 20 seconds, or greater than about 30 seconds, or greater than about 40 seconds, or greater than about 50 seconds, or greater than about 60 seconds, or greater than about 2 minutes, or greater than about 3 minutes, or greater than about 4 minutes, or greater than about 5 minutes, or greater than about 6 minutes, or greater than about 7 minutes, or greater than about 8 minutes, or greater than about 9 minutes, or greater than about 10 minutes, or greater than about 20 minutes, or greater than about 30 minutes, or greater than about 40 minutes, or greater than about 50 minutes, or greater than about 60 minutes.

In one embodiment, the curing time for the method of this disclosure may be less than about 1 second, or less than about 2 seconds, or less than about 3 seconds, or less than about 4 seconds, or less than about 5 seconds, or less than about 6 seconds, or less than about 7 seconds, or less than about 8 seconds, or less than about 9 seconds, or less than about 10 seconds, or less than about 20 seconds, or less than about 30 seconds, or less than about 40 seconds, or less than about 50 seconds, or less than about 60 seconds, or less than about 2 minutes, or less than about 3 minutes, or less than about 4 minutes, or less than about 5 minutes, or less than about 6 minutes, or less than about 7 minutes, or less than about 8 minutes, or less than about 9 minutes, or less than about 10 minutes, or less than about 20 minutes, or less than about 30 minutes, or less than about 40 minutes, or less than about 50 minutes, or less than about 60 minutes.

In one embodiment, the curing time for the method of this disclosure may be greater than about 1 second, or greater than about 2 seconds, or greater than about 3 seconds, or greater than about 4 seconds, or greater than about 5 seconds, or greater than about 6 seconds, or greater than about 7 seconds, or greater than about 8 seconds, or greater than about 9 seconds, or greater than about 10 seconds, or greater than about 20 seconds, or greater than about 30 seconds, or greater than about 40 seconds, or greater than about 50 seconds, or greater than about 60 seconds, or greater than about 2 minutes, or greater than about 3 minutes, or greater than about 4 minutes, or greater than about 5 minutes, or greater than about 6 minutes, or greater than about 7 minutes, or greater than about 8 minutes, or greater than about 9 minutes, or greater than about 10 minutes, or greater than about 20 minutes, or greater than about 30 minutes, or greater than about 40 minutes, or greater than about 50 minutes, or greater than about 60 minutes.

In one embodiment, the fabric tension used in the method of this disclosure may be less than about 1N, or less than about 2N, or less than about 3N, or less than about 4N, or less than about 5N, or less than about 6N, or less than about 7N, or less than about 8N, or less than about 9N, or less than about 10N, or less than about 20N, or less than about 30N, or less than about 40N, or less than about 50N, or less than about 60N, or less than about 70N, or less than about 80N, or less than about 90N, or less than about 100N, or less than about 150N, or less than about 200N, or less than about 250N, or less than about 300N.

In one embodiment, the fabric tension used in the method of this disclosure may be greater than about 1N, or greater than about 2N, or greater than about 3N, or greater than about 4N, or greater than about 5N, or greater than about 6N, or greater than about 7N, or greater than about 8N, or greater than about 9N, or greater than about 10N, or greater than about 20N, or greater than about 30N, or greater than about 40N, or greater than about 50N, or greater than about 60N, or greater than about 70N, or greater than about 80N, or greater than about 90N, or greater than about 100N, or greater than about 150N, or greater than about 200N, or greater than about 250N, or greater than about 300N.

In one embodiment, the pressure of the dyeing machine used in the method of this disclosure may be less than about 1 N/mm, or less than about 2 N/mm, or less than about 3 N/mm, or less than about 4 N/mm, or less than about 4 N/mm, or less than about 5 N/mm, or less than about 6 N/mm, or less than about 7 N/mm, or less than about 8 N/mm, or less than about 9 N/mm, or less than about 10 N/mm, or less than about 20 N/mm, or less than about 30 N/mm, or less than about 40 N/mm, or less than about 50 N/mm, or less than about 60 N/mm, or less than about 70 N/mm, or less than about 80 N/mm, or less than about 90 N/mm.

In one embodiment, the pressure of the dyeing machine used in the method of this disclosure may be greater than about 1 N/mm, or greater than about 2 N/mm, or greater than about 3 N/mm, or greater than about 4 N/mm, or greater than about 4 N/mm, or greater than about 5 N/mm, or greater than about 6 N/mm, or greater than about 7 N/mm, or greater than about 8 N/mm, or greater than about 9 N/mm, or greater than about 10 N/mm, or greater than about 20 N/mm, or greater than about 30 N/mm, or greater than about 40 N/mm, or greater than about 50 N/mm, or greater than about 60 N/mm, or greater than about 70 N/mm, or greater than about 80 N/mm, or greater than about 90 N/mm.

In one embodiment, the Shore hardness of the dyeing mill rolls used in the methods of this disclosure may be less than about 70 Shore A, or less than about 75 Shore A, or less than about 80 Shore A, or less than about 85 Shore A, or less than about 90 Shore A, or less than about 95 Shore A, or less than about 100 Shore A.

In one embodiment, the Shore hardness of the dyeing mill rolls used in the methods of this disclosure may be greater than about 70 Shore A, or greater than about 75 Shore A, or greater than about 80 Shore A, or greater than about 85 Shore A, or greater than about 90 Shore A, or greater than about 95 Shore A, or greater than about 100 Shore A.

In one embodiment, the temperature of the spreader used in the method of this disclosure may be less than about 70°C, or less than about 75°C, or less than about 80°C, or less than about 85°C, or less than about 90°C, or less than about 95°C, or less than about 100°C, or less than about 110°C, or less than about 120°C, or less than about 130°C, or less than about 140°C, or less than about 150°C, or less than about 160°C, or less than about 170°C, or less than about 180°C, or less than about 190°C, or less than about 200°C, or less than about 210°C, or less than about 220°C, or less than about 230°C.

In one embodiment, the temperature of the spreader used in the method of this disclosure may be greater than about 70°C, or greater than about 75°C, or greater than about 80°C, or greater than about 85°C, or greater than about 90°C, or greater than about 95°C, or greater than about 100°C, or greater than about 110°C, or greater than about 120°C, or greater than about 130°C, or greater than about 140°C, or greater than about 150°C, or greater than about 160°C, or greater than about 170°C, or greater than about 180°C, or greater than about 190°C, or greater than about 200°C, or greater than about 210°C, or greater than about 220°C, or greater than about 230°C.

In one embodiment, the common drying temperature used in the methods of this disclosure may be less than about 110°C, or less than about 115°C, or less than about 120°C, or less than about 125°C, or less than about 130°C, or less than about 135°C, or less than about 140°C, or less than about 145°C, or less than about 150°C.

In one embodiment, the common drying temperature used in the methods of this disclosure may be greater than about 110°C, or greater than about 115°C, or greater than about 120°C, or greater than about 125°C, or greater than about 130°C, or greater than about 135°C, or greater than about 140°C, or greater than about 145°C, or greater than about 150°C.

In some embodiments, the fibroin-coated material (e.g., fabric) can withstand selected temperatures, where the selection of the selected temperature is for drying, curing, and/or heat setting of dyes that can be applied to the material (e.g., LYCRA). As used herein, "heat resistance" can refer to the properties of the fibroin coating deposited on the material, wherein the fibroin coating and/or fibroin itself does not exhibit a significant improvement in the properties of the fibroin coating compared to a control material with a comparable fibroin coating that has not been subjected to selected temperatures for drying, curing, washing cycles, and/or heat setting purposes (i.e., "significantly improved" fibroin coating properties). In some embodiments, the selected temperature is the glass transition temperature ( _Tg ) of the material after the fibroin coating has been applied. In some implementations, the selected temperature is greater than about 65°C, or greater than about 70°C, or greater than about 80°C, or greater than about 90°C, or greater than about 100°C, or greater than about 110°C, or greater than about 120°C, or greater than about 130°C, or greater than about 140°C, or greater than about 150°C, or greater than about 160°C, or greater than about 170°C, or greater than about 180°C, or greater than about 190°C, or greater than about 200°C, or greater than about 210°C, or greater than about 220°C. In some implementations, the selected temperature is less than about 65°C, or less than about 70°C, or less than about 80°C, or less than about 90°C, or less than about 100°C, or less than about 110°C, or less than about 120°C, or less than about 130°C, or less than about 140°C, or less than about 150°C, or less than about 160°C, or less than about 170°C, or less than about 180°C, or less than about 190°C, or less than about 200°C, or less than about 210°C, or less than about 220°C.

In one embodiment, "significantly improved" silk core protein coating performance can be a reduction in selected properties of the silk core protein coating, such as wetting time, absorption rate, spreading speed, cumulative unidirectional transport, or overall moisture management capability, compared to a control silk core protein coating that has not undergone selected temperature cycles for drying, curing, washing, and/or heat setting purposes. This reduction is less than about 1%, less than about 2%, or less than about 3% in terms of wetting time, absorption rate, spreading speed, cumulative unidirectional transport, or overall moisture management capability compared to a control silk core protein coating that has not undergone selected temperature cycles for drying, curing, washing, and/or heat setting purposes. The reduction may be less than about 4%, or less than about 5%, or less than about 6%, or less than about 7%, or less than about 8%, or less than about 9%, or less than about 10%, or less than about 15%, or less than about 20%, or less than about 25%, or less than about 30%, or less than about 35%, or less than about 40%, or less than about 45%, or less than about 50%, or less than about 60%, or less than about 70%, or less than about 80%, or less than about 90%, or less than about 100%. In some embodiments, "wash cycle" may refer to at least one wash cycle, or at least two wash cycles, or at least three wash cycles, or at least four wash cycles, or at least five wash cycles.

In one embodiment, "significantly improved" silk core protein coating performance can be an increase in selected properties of the silk core protein coating, such as wetting time, absorption rate, spreading speed, cumulative unidirectional transport, or overall moisture management capability, compared to a control silk core protein coating that has not undergone selected temperature cycles for drying, curing, washing, and/or heat setting purposes. This increase, compared to a control silk core protein coating that has not undergone selected temperature cycles for drying, curing, washing, and/or heat setting purposes, is an increase of less than about 1%, or less than about 2%, or less than about 3% in terms of wetting time, absorption rate, spreading speed, cumulative unidirectional transport, or overall moisture management capability. An increase, or less than about 4%, or less than about 5%, or less than about 6%, or less than about 7%, or less than about 8%, or less than about 9%, or less than about 10%, or less than about 15%, or less than about 20%, or less than about 25%, or less than about 30%, or less than about 35%, or less than about 40%, or less than about 45%, or less than about 50%, or less than about 60%, or less than about 70%, or less than about 80%, or less than about 90%, or less than about 100%. In some embodiments, "wash cycle" may refer to at least one wash cycle, or at least two wash cycles, or at least three wash cycles, or at least four wash cycles, or at least five wash cycles.

In some embodiments, the SFS-coated article may be subjected to heat setting to solidify one or more dyes that can be applied to the SFS-coated article, thereby permanently solidifying one or more dyes on the SFS-coated article. In some embodiments, the SFS-coated article may be heat-set resistant, wherein the SFS coating on the SFS-coated article can withstand heat setting temperatures greater than about 100°C, or greater than about 110°C, or greater than about 120°C, or greater than about 130°C, or greater than about 140°C, or greater than about 150°C, or greater than about 160°C, or greater than about 170°C, or greater than about 180°C, or greater than about 190°C, or greater than about 200°C, or greater than about 210°C, or greater than about 220°C. In some implementations, the selected temperature is less than about 100°C, or less than about 110°C, or less than about 120°C, or less than about 130°C, or less than about 140°C, or less than about 150°C, or less than about 160°C, or less than about 170°C, or less than about 180°C, or less than about 190°C, or less than about 200°C, or less than about 210°C, or less than about 220°C.

In one embodiment, after the silk-core coated material is subjected to heating and/or curing as described herein, the silk-core coated material may partially dissolve or partially incorporate into a portion of the material. Not limited to any theory of this disclosure, when the silk-core coated material is heated to a temperature greater than about the glass transition temperature (Tg) of the coated material, the silk-core coating may partially dissolve or partially incorporate into a portion of the material.

In some embodiments, the material coated with the silk core protein as described herein may be sterile or may be sterilized to provide a sterile silk core protein coated material. Alternatively, or otherwise, the methods described herein may include sterile SFS prepared from sterile silk core protein.

In some embodiments, fabric constructions compatible with the methods of this disclosure include woven fabrics, knitted fabrics, and nonwoven fabrics.

In some embodiments, the coating patterns provided by the methods of this disclosure include single-sided coating, double-sided coating, and/or overall coating.

In some implementations, equipment manufacturers capable of producing devices configured for continuous coating of SFS on textiles include, but are not limited to, Aigle, Amba Projex, Bombi, Bruckner, Cavitec, Crosta, Dienes Apparatebau, Eastsign, Europlasma, Fermor, Fontanet, Gaston Systems, Hansa Mixer, Harish, Has Group, Icomatex, Idealtech, Interspare, Isotex, Klieverik, KTP, M P, Mageba, Mahr Feinpruef, Matex, Mathis, Menzel LP, and Meyer. , Monforts, Morrison Textile, Mtex, Muller Frick, Muratex Textile, Reliant Machinery, Rollmac, Salvade, SandvikTps, Santex, Chmitt-Machinen, Schott&Meissner, Sel lers, Sicam, Siltex, Starlinger, Swatik Group India, Techfull, TMT Manenti, Unitech Textile Machinery, Weko, Willy, Wumag Texroll, Yamuna, Zappa and Zimmer Austria.

In some implementations, equipment manufacturers capable of producing SFS configured for dry coating on textiles include, but are not limited to, Alea, Alkan Makina, Anglada, Atac Makina, Bianco, Bruckner, Campen, CHTC, CTMTC, Dilmenler, Elteksmak, Erbatech, Fontanet, Harish, Icomatex, Ilsung, Inspiron, Interspare, Master, Mathis, Monfongs, Monforts, Salvade, Schmitt-Maschinen, Sellers, Sicam, Siltex, Swastik Group India, Tacome, Tubetex, Turbang, Unitech Textile Machinery, and Yamuna.

The following clauses describe certain implementation schemes.

Clause 1. An article comprising a fabric and a coating, wherein the coating comprises a surfactant and/or emulsifier system, and silk core protein fragments having a fraction selected from about 1 kDa to about 5 kDa, about 5 kDa to about 10 kDa, about 6 kDa to about 17 kDa, about 10 kDa to about 15 kDa, about 14 kDa to about 30 kDa, about 15 kDa to about 20 kDa, about 17 kDa to about 39 kDa, about 20 kDa to about 25 kDa, and about 25 kDa. a. average weight-average molecular weight of about 30 kDa, about 30 kDa to about 35 kDa, about 35 kDa to about 40 kDa, about 39 kDa to about 54 kDa, about 39 kDa to about 80 kDa, about 40 kDa to about 45 kDa, about 45 kDa to about 50 kDa, about 50 kDa to about 55 kDa, about 55 kDa to about 60 kDa, about 60 kDa to about 100 kDa, or about 80 kDa to about 144 kDa, and polydispersity in the range of 1 to about 5.

Clause 2. The article according to Clause 1, wherein the polydispersity of said silk core protein fragment is from 1 to about 1.5, from about 1.5 to about 2.0, from about 2.0 to about 2.5, from about 2.5 to about 3.0, from about 3.0 to about 3.5, from about 3.5 to about 4.0, from about 4.0 to about 4.5 or from about 4.5 to about 5.0.

Clause 3. The article of manufacture according to Clause 1, wherein the polydispersity of the silk core protein fragment is from about 1.5 to about 3.0.

Clause 4. The article of manufacture according to Clause 1, wherein the silk core protein fragment comprises one or more of low molecular weight silk core protein fragments and medium molecular weight silk core protein fragments.

Clause 5. The article according to any one of Clauses 1 to 4 further comprises about 0.01% (w/w) to about 10% (w/w) of sericin relative to the said sericin fragment.

Clause 6. An article of any one of Clauses 1 to 5, wherein the fabric comprises one or more of the following: polyester, polyamide, polyaramid, polytetrafluoroethylene, polyethylene, polypropylene, polyurethane, silicone, a mixture of polyurethane and polyethylene glycol, ultra-high molecular weight polyethylene, high performance polyethylene, nylon, LYCRA (polyester-polyurethane copolymer, also known as SPANDEX and elastomer), or a mixture thereof.

Clause 7. The article according to any one of Clauses 1 to 6, wherein the coating further comprises one or more of a wetting agent, a defoamer, a softener, a wicking agent and an antimicrobial agent.

Clause 8. The article according to any one of Clauses 1 to 7, wherein the w/w ratio of the silk core protein fragments in the coating to the surfactant and/or emulsifier system is about 99:1, about 98:2, about 97:3, about 96:4, about 95:5, about 94:6, about 93:7, about 92:8, about 91:9, about 90:10, about 89:11, about 88:12, about 87:13, about 86:14, about 85:15, about 84:16, about 83:17, about 82:18, about 81:19, about 8 0:20, approximately 79:21, approximately 78:22, approximately 77:23, approximately 76:24, approximately 75:25, approximately 74:26, approximately 73:27, approximately 72:28, approximately 71:29, approximately 70:30, approximately 69:31, approximately 68:32, approximately 67:33, approximately 66:34, approximately 65:35, approximately 64:36, approximately 63:37, approximately 62:38, approximately 61:39, approximately 60:40, approximately 59:41, approximately 58:42, approximately 57:43, approximately 56:44, approximately 55:45, approximately 54 :46, about 53:47, about 52:48, about 51:49, about 50:50, about 49:51, about 48:52, about 47:53, about 46:54, about 45:55, about 44:56, about 43:57, about 42:58, about 41:59, about 40:60, about 39:61, about 38:62, about 37:63, about 36:64, about 35:65, about 34:66, about 33:67, about 32:68, about 31:69, about 30:70, about 29:71, about 28: 72, 27:73, 26:74, 25:75, 24:76, 23:77, 22:78, 21:79, 20:80, 19:81, 18:82, 17:83, 16:84, 15:85, 14:86, 13:87, 12:88, 11:89, 10:90, 9:91, 8:92, 7:93, 6:94, 5:95, 4:96, 3:97, 2:98 or 1:99.

Clause 9. The article according to any one of Clauses 1 to 7, wherein the w/w ratio of the silk core protein fragments in the coating to the surfactant and/or emulsifier is about 1:1, about 1:2, about 1:4, about 1:8, about 1:16 or about 1:32.

Clause 10. The article according to any one of Clauses 1 to 7, wherein the w/w ratio of the silk core protein fragments in the coating to the surfactant and/or emulsifier system is about 1:1, about 1:2, about 1:3, about 1:4, about 1:5, about 1:6, about 1:7, about 1:8, about 1:9, about 1:10, about 1:11, about 1:12, about 1:13, about 1:14, about 1:15, about 1:16, about 1:17, about 1:18, about 1:19, about 1:20, about 1:21, about 1:22, about 1:23, about 1:24, about 1:25, about 1:26, about 1:27, about 1:28, about 1:29, about 1:30, about 1:31 or about 1:32.

Clause 11. The article according to any one of Clauses 1 to 10, wherein the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene sorbitan monooleate, polyoxyethylene sorbitan trioleate, polyoxyethylene castor oil, and any combination thereof.

Clause 12. The article according to any one of Clauses 1 to 10, wherein the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene (10-30) sorbitan monooleate, polyoxyethylene (10-30) sorbitan trioleate, polyoxyethylene (10-50) castor oil, and any combination thereof.

Clause 13. An article according to any one of Clauses 1 to 10, wherein the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene (20) sorbitan monooleate, polyoxyethylene (20) sorbitan trioleate, polyoxyethylene (29) castor oil, and any combination thereof.

Clause 14. An article according to any one of Clauses 1 to 10, wherein the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene (20) sorbitol monolaurate, polyoxyethylene (20) sorbitol monopalmitate, polyoxyethylene (20) sorbitol monostearate, polyoxyethylene (20) sorbitol tristearate, and any combination thereof.

Clause 15. An article according to any one of Clauses 1 to 10, wherein the surfactant and/or emulsifier system comprises one or more of the following: sorbitol monofatty acid, sorbitol trifatty acid, castor oil, and any combination thereof.

Clause 16. The article according to any one of Clauses 1 to 15, wherein the surfactant and/or emulsifier system comprises one or more of the following: cocoyl glucoside, decyl glucoside, lauryl glucoside, sucrose cocoate, octyl/octyl glucoside, octyl/octyl glucoside, and any combination thereof.

Clause 17. The article of any one of Clauses 1 to 16, wherein the HLB of the surfactant and/or emulsifier system is from about 11 to about 13.50.

Clause 18. The article of any one of Clauses 1 to 16, wherein the HLB of the surfactant and/or emulsifier system is about 11 to about 11.50, about 11.50 to about 12, about 12 to about 12.50, about 12.50 to about 13 or about 13 to about 13.50. In some embodiments, the HLB of the surfactant and/or emulsifier system is about 11, about 11.1, about 11.2, about 11.3, about 11.4, about 11.5, about 11.6, about 11.7, about 11.8, about 11.9, about 12, about 12.1, about 12.2, about 12.3, about 12.4, about 12.5, about 12.6, about 12.7, about 12.8, about 12.9, about 13, about 13.1, about 13.2, about 13.3, about 13.4, about 13.5, about 13.6, about 13.7, about 13.8, about 13.9, or about 14.

Clause 19. An article according to any one of Clauses 1 to 18, wherein the article has improved moisture management compared with a similar article comprising a similar fabric but without a coating.

Clause 20. Articles of manufacture as described in Clause 19, wherein moisture management is assessed by a water absorption test, a vertical wicking test, or a drying rate test.

Clause 21. An article according to any one of Clauses 1 to 20, wherein the article has improved drape compared to a similar article comprising a similar fabric but without a coating.

Clause 22. An article according to any one of Clauses 1 to 21, wherein the article has improved smoothness compared to a similar article comprising a similar fabric but without a coating.

Clause 23. An article of any one of Clauses 1 to 22, wherein the article has an improved hand feel compared to a similar article comprising a similar fabric but without a coating.

Clause 24. An article according to any one of Clauses 1 to 23, wherein the article has a lower charge density at a given pH value compared with a similar article comprising a similar fabric but without a coating.

Clause 25. A method for preparing a silk core protein coated fabric, the method comprising: applying a solution comprising a surfactant and/or emulsifier system to the fabric; applying a silk core protein fragment solution to the fabric; and drying the fabric.

Clause 26. A method for preparing a silk core protein coated fabric, the method comprising: applying a solution comprising a surfactant and/or emulsifier system and silk core protein fragments to the fabric; and drying the fabric.

Clause 27. The method according to Clause 25 or Clause 26, wherein the concentration of the silk core protein fragment in the solution ranges from 0.01 g/L to about 100 g/L.

Clause 28. The method according to any one of Clauses 25 to 27, wherein the concentration of the surfactant and/or emulsifier system in the solution ranges from 0.01 g/L to about 100 g/L.

Clause 29. The method according to any one of Clauses 25 to 28, wherein the silken protein fragment has an average weight-average molecular weight selected from about 1 kDa to about 5 kDa, about 5 kDa to about 10 kDa, about 6 kDa to about 17 kDa, about 10 kDa to about 15 kDa, about 14 kDa to about 30 kDa, about 15 kDa to about 20 kDa, about 17 kDa to about 39 kDa, about 20 kDa to about 25 kDa, about 25 kDa to about 30 kDa, about 30 kDa to about 35 kDa, about 35 kDa to about 40 kDa, about 39 kDa to about 54 kDa, about 39 kDa to about 80 kDa, about 40 kDa to about 45 kDa, about 45 kDa to about 50 kDa, about 50 kDa to about 55 kDa, about 55 kDa to about 60 kDa, about 60 kDa to about 100 kDa, or about 80 kDa to about 144 kDa, and a polydispersity ranging from 1 to about 5.

Clause 30. The method according to any one of Clauses 25 to 29, wherein the polydispersity of the silk core protein fragment is 1 to about 1.5, about 1.5 to about 2.0, about 2.0 to about 2.5, about 2.5 to about 3.0, about 3.0 to about 3.5, about 3.5 to about 4.0, about 4.0 to about 4.5 or about 4.5 to about 5.0.

Clause 31. The method according to any one of Clauses 25 to 29, wherein the polydispersity of the silk core protein fragment is from about 1.5 to about 3.0.

Clause 32. The method according to any one of Clauses 25 to 29, wherein the silk core protein fragment comprises one or more of low molecular weight silk core protein fragments and medium molecular weight silk core protein fragments.

Clause 33. The method according to any one of Clauses 25 to 32, wherein the solution further comprises about 0.01% (w/w) to about 10% (w/w) of sericin relative to the said sericin fragment.

Clause 34. The method according to any one of Clauses 25 to 33, wherein the fabric comprises one or more of the following: polyester, polyamide, polyaramid, polytetrafluoroethylene, polyethylene, polypropylene, polyurethane, silicone, a mixture of polyurethane and polyethylene glycol, ultra-high molecular weight polyethylene, high performance polyethylene, nylon, LYCRA (polyester-polyurethane copolymer, also known as SPANDEX and elastomer), or a mixture thereof.

Clause 35. The method according to any one of Clauses 25 to 34, wherein the solution further comprises one or more of a wetting agent, an antifoaming agent, a softening agent, a wicking agent, and an antimicrobial agent.

Clause 36. The method according to any one of Clauses 25 to 35, wherein the w/w ratio of the silk core protein fragment to the surfactant and/or emulsifier system is about 99:1, about 98:2, about 97:3, about 96:4, about 95:5, about 94:6, about 93:7, about 92:8, about 91:9, about 90:10, about 89:11, about 88:12, about 87:13, about 86:14, about 85:15, about 84:16, about 83:17, about 82:18, about 81:19, about 80: 20, Approx. 79:21, Approx. 78:22, Approx. 77:23, Approx. 76:24, Approx. 75:25, Approx. 74:26, Approx. 73:27, Approx. 72:28, Approx. 71:29, Approx. 70:30, Approx. 69:31, Approx. 68:32, Approx. 67:33, Approx. 66:34, Approx. 65:35, Approx. 64:36, Approx. 63:37, Approx. 62:38, Approx. 61:39, Approx. 60:40, Approx. 59:41, Approx. 58:42, Approx. 57:43, Approx. 56:44, Approx. 55:45, Approx. 54: 46, Approx. 53:47, Approx. 52:48, Approx. 51:49, Approx. 50:50, Approx. 49:51, Approx. 48:52, Approx. 47:53, Approx. 46:54, Approx. 45:55, Approx. 44:56, Approx. 43:57, Approx. 42:58, Approx. 41:59, Approx. 40:60, Approx. 39:61, Approx. 38:62, Approx. 37:63, Approx. 36:64, Approx. 35:65, Approx. 34:66, Approx. 33:67, Approx. 32:68, Approx. 31:69, Approx. 30:70, Approx. 29:71, Approx. 28: 72, 27:73, 26:74, 25:75, 24:76, 23:77, 22:78, 21:79, 20:80, 19:81, 18:82, 17:83, 16:84, 15:85, 14:86, 13:87, 12:88, 11:89, 10:90, 9:91, 8:92, 7:93, 6:94, 5:95, 4:96, 3:97, 2:98 or 1:99.

Clause 37. The method according to any one of Clauses 25 to 35, wherein the w/w ratio of the silk core protein fragment to the surfactant and/or emulsifier system is about 1:1, about 1:2, about 1:4, about 1:8, about 1:16 or about 1:32.

Clause 38. The method according to any one of Clauses 25 to 35, wherein the w/w ratio of the silk core protein fragment to the surfactant and/or emulsifier system is about 1:1, about 1:2, about 1:3, about 1:4, about 1:5, about 1:6, about 1:7, about 1:8, about 1:9, about 1:10, about 1:11, about 1:12, about 1:13, about 1:14, about 1:15, about 1:16, about 1:17, about 1:18, about 1:19, about 1:20, about 1:21, about 1:22, about 1:23, about 1:24, about 1:25, about 1:26, about 1:27, about 1:28, about 1:29, about 1:30, about 1:31 or about 1:32.

Clause 39. The method according to any one of Clauses 25 to 38, wherein the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene sorbitan monooleate, polyoxyethylene sorbitan trioleate, polyoxyethylene castor oil, and any combination thereof.

Clause 40. The method according to any one of Clauses 25 to 38, wherein the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene (10-30) sorbitan monooleate, polyoxyethylene (10-30) sorbitan trioleate, polyoxyethylene (10-50) castor oil, and any combination thereof.

Clause 41. The method according to any one of Clauses 25 to 38, wherein the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene (20) sorbitan monooleate, polyoxyethylene (20) sorbitan trioleate, polyoxyethylene (29) castor oil, and any combination thereof.

Clause 42. The method according to any one of Clauses 25 to 38, wherein the surfactant and/or emulsifier system comprises one or more of the following: polyoxyethylene (20) sorbitol monolaurate, polyoxyethylene (20) sorbitol monopalmitate, polyoxyethylene (20) sorbitol monostearate, polyoxyethylene (20) sorbitol tristearate, and any combination thereof.

Clause 43. The method according to any one of Clauses 25 to 38, wherein the surfactant and/or emulsifier system comprises one or more of the following: sorbitol monofatty acid, sorbitol trifatty acid, castor oil, and any combination thereof.

Clause 44. The method according to any one of Clauses 25 to 43, wherein the surfactant and/or emulsifier system comprises one or more of the following: cocoyl glucoside, decyl glucoside, lauryl glucoside, sucrose cocoate, octyl/octyl glucoside, octyl/octyl glucoside, and any combination thereof.

Clause 45. The method according to any one of Clauses 25 to 44, wherein the HLB of the surfactant and/or emulsifier system is about 11 to about 13.50.

Clause 46. The method according to any one of Clauses 25 to 44, wherein the HLB of the surfactant and/or emulsifier system is about 11 to about 11.50, about 11.50 to about 12, about 12 to about 12.50, about 12.50 to about 13, or about 13 to about 13.50. In some embodiments, the HLB of the surfactant and/or emulsifier system is about 11, about 11.1, about 11.2, about 11.3, about 11.4, about 11.5, about 11.6, about 11.7, about 11.8, about 11.9, about 12, about 12.1, about 12.2, about 12.3, about 12.4, about 12.5, about 12.6, about 12.7, about 12.8, about 12.9, about 13, about 13.1, about 13.2, about 13.3, about 13.4, about 13.5, about 13.6, about 13.7, about 13.8, about 13.9, or about 14.

Clause 47. The method according to any one of Clauses 25 to 46, wherein the drying includes heating.

Clause 48. The method according to any one of Clauses 25 to 47, wherein the pH of the solution is acidic.

Clause 49. The method according to any one of Clauses 25 to 47, wherein the pH of the solution is about 3.5 to about 4, about 4 to about 4.5, about 4.5 to about 5, about 5 to about 5.5, or about 5.5 to about 6. In some embodiments, the pH of the solution is about 3.5, about 3.6, about 3.7, about 3.8, about 3.9, about 4, about 4.1, about 4.2, about 4.3, about 4.4, about 4.5, about 4.6, about 4.7, about 4.8, about 4.9, about 5, about 5.1, about 5.2, about 5.3, about 5.4, about 5.5, about 5.6, about 5.7, about 5.8, about 5.9, or about 6.

Clause 50. An article of manufacture prepared by any one of Clauses 25 to 49.

Clause 51. The article of the claim pursuant to Clause 50, wherein the article of the claim has improved moisture management compared with similar articles comprising similar fabrics but without a coating.

Clause 52. Articles of manufacture according to Clause 51, wherein moisture management is assessed by a water absorption test, a vertical wicking test, or a drying rate test.

Clause 53. An article according to any one of Clauses 50 to 52, wherein the article has improved drape compared to a similar article comprising a similar fabric but without a coating.

Clause 54. An article according to any one of Clauses 50 to 53, wherein the article has improved smoothness compared to a similar article comprising a similar fabric but without a coating.

Clause 55. An article of any one of Clauses 50 to 54, wherein the article has an improved hand feel compared to a similar article comprising a similar fabric but without a coating.

Clause 56. An article according to any one of Clauses 50 to 55, wherein the article has a lower charge density at a given pH value compared to a similar article comprising a similar fabric but without a coating.

Clause 57. An article according to any one of Clauses 1 to 24 or 50 to 56, wherein the amount of the filoin fragment in the article is from about 0.01 g to 0.5 g/1500 ^m² (denier) to 4000 ^m² (denier).

Clause 58. An article pursuant to any one of Clauses 1 to 24 or 50 to 56, wherein the amount of the fibrin fragment in the article is from about 0.03 g to 0.35 g/1500 ^m² (denier) to 4000 ^m² (denier).

Clause 59. An article pursuant to any one of Clauses 1 to 24 or 50 to 56, wherein the amount of the fibrin fragment in the article is from about 0.05 g to 0.2 g/3000 ^m² (denier) to 4000 ^m² (denier).

Clause 60. An article pursuant to any one of Clauses 1 to 24 or 50 to 56, wherein the amount of the fibrin fragment in the article is from about 0.2 g to 0.35 g/1000 ^m² (denier) to 2500 ^m² (denier).

Clause 61. An article pursuant to any one of Clauses 1 to 24, or 50 to 56, wherein the amount of the filaggrin fragment in the article is about 0.01 g/1000-4500 ^m² (denier), about 0.02 g/1000-4500 ^m² (denier), about 0.03 g/1000-4500 ^m² (denier), about 0.04 g/1000-4500 ^m² (denier), about 0.05 g/1000-4500 ^m² (denier), about 0.06 g/1000-4500 ^m² (denier), about 0.07 g/1000-4500 ^m² (denier), about 0.08 g/1000-4500 ^m² (denier), or about 0.09 g/1000-4500 ^m² (Danil), approx. 0.10g/ ^1000-4500m² (Danil), approx ^. 0.11g/1000-4500m² (Danil), approx. ^0.12g /1000-4500m² (Danil), approx. 0.13g/ ^1000-4500m² (Danil), ^approx . 0.14g/ ^1000-4500m² (Danil), ^approx . 0.15g/1000-4500m² (Danil), approx. 0.16g/1000-4500m² (Danil), approx. 0.17g/ ^1000-4500m² (Danil), approx. 0.18g/ ^1000-4500m² (Danil), approx. 0.19g/ ^1000-4500m² (Danil), approx. 0.2g/ ^1000-4500m² (Danil), approx. 0.21g/ ^1000-4500m² (Danil), approx. ^0.22g /1000-4500m² (Danil), approx. 0.23g/ ^1000-4500m² (Danil), approx. 0.24g/ ^1000-4500m² (Danil), ^approx . 0.25g/1000-4500m² (Danil), approx. 0.26g/ ^1000-4500m² (Danil), approx. 0.27g/ ^1000-4500m² (Danil), approx. 0.28g/ ^1000-4500m² (Danil), approx. 0.29g/ ^1000-4500m² (Dennier), approx. 0.3g/ ^1000-4500m² (Dennier), approx. 0.31g/ ^1000-4500m² (Dennier), approx. ^0.32g /1000-4500m² (Dennier), approx. 0.33g/ ^1000-4500m² (Dennier), approx. 0.34g/ ^1000-4500m² (Dennier), ^approx . 0.35g/1000-4500m² (Dennier), approx. 0.36g/1000-4500m² (Dennier), approx. ^0.37g / ^1000-4500m² (Dennier), approx. 0.38g/ ^1000-4500m² (Dennier), approx. 0.39g/ ^1000-4500m² (Dennier), approx. 0.4g/ ^1000-4500m² (Dennier), approx. 0.41g/ ^1000-4500m² (Dennier), approx. ^0.42g /1000-4500m² (Dennier), approx. 0.43g/ ^1000-4500m² (Dennier), approx. 0.44g/ ^1000-4500m² (Dennier), ^approx . 0.45g/1000-4500m² (Dennier), approx. 0.46g/1000-4500m² (Dennier), approx. ^0.47g / ^1000-4500m² (Dennier), approx. 0.48g/ ^1000-4500m² (Dennier), approx. 0.49g/ ^1000-4500m² (Dennier) or approximately 0.5g/ ^1000-4500m2 (Dennier).

Clause 101. An article comprising a fabric and a coating, wherein the coating comprises a surfactant and a silk core protein fragment having a fraction selected from about 1 kDa to about 5 kDa, about 5 kDa to about 10 kDa, about 6 kDa to about 17 kDa, about 10 kDa to about 15 kDa, about 14 kDa to about 30 kDa, about 15 kDa to about 20 kDa, about 17 kDa to about 39 kDa, about 20 kDa to about 25 kDa, about 25 kDa to about 3... Average weight-average molecular weight of 0 kDa, about 30 kDa to about 35 kDa, about 35 kDa to about 40 kDa, about 39 kDa to about 54 kDa, about 39 kDa to about 80 kDa, about 40 kDa to about 45 kDa, about 45 kDa to about 50 kDa, about 50 kDa to about 55 kDa, about 55 kDa to about 60 kDa, about 60 kDa to about 100 kDa, or about 80 kDa to about 144 kDa, and polydispersity in the range of 1 to about 5.

Clause 102. The article of manufacture according to Clause 101, wherein the polydispersity of the silk core protein fragment is from 1 to about 1.5, from about 1.5 to about 2.0, from about 2.0 to about 2.5, from about 2.5 to about 3.0, from about 3.0 to about 3.5, from about 3.5 to about 4.0, from about 4.0 to about 4.5 or from about 4.5 to about 5.0.

Clause 103. The article of manufacture according to Clause 101, wherein the polydispersity of the silk core protein fragment is from about 1.5 to about 3.0.

Clause 104. The article of manufacture according to Clause 101, wherein the silk core protein fragment comprises one or more of low molecular weight silk core protein fragments and medium molecular weight silk core protein fragments.

Clause 105. The article of any one of Clauses 101 to 104 further comprises about 0.01% (w/w) to about 10% (w/w) of sericin relative to the said sericin fragment.

Clause 66. An article of any one of Clauses 101 to 105, wherein the fabric comprises one or more of the following: polyester, polyamide, polyaramid, polytetrafluoroethylene, polyethylene, polypropylene, polyurethane, silicone, a mixture of polyurethane and polyethylene glycol, ultra-high molecular weight polyethylene, high performance polyethylene, nylon, LYCRA (polyester-polyurethane copolymer, also known as SPANDEX and elastomer), or a mixture thereof.

Clause 107. An article of any one of Clauses 101 to 106, wherein the coating further comprises one or more of a wetting agent, an antifoaming agent, a softening agent, a wicking agent, and an antimicrobial agent.

Clause 108. The article according to any one of Clauses 101 to 107, wherein the w/w ratio of the silk core protein fragments to the surfactant in the coating is about 99:1, about 98:2, about 97:3, about 96:4, about 95:5, about 94:6, about 93:7, about 92:8, about 91:9, about 90:10, about 89:11, about 88:12, about 87:13, about 86:14, about 85:15, about 84:16, about 83:17, about 82:18, about 81:19, or about 80:2. 0, Approximately 79:21, Approximately 78:22, Approximately 77:23, Approximately 76:24, Approximately 75:25, Approximately 74:26, Approximately 73:27, Approximately 72:28, Approximately 71:29, Approximately 70:30, Approximately 69:31, Approximately 68:32, Approximately 67:33, Approximately 66:34, Approximately 65:35, Approximately 64:36, Approximately 63:37, Approximately 62:38, Approximately 61:39, Approximately 60:40, Approximately 59:41, Approximately 58:42, Approximately 57:43, Approximately 56:44, Approximately 55:45, Approximately 54:4 6. Approximately 53:47, Approximately 52:48, Approximately 51:49, Approximately 50:50, Approximately 49:51, Approximately 48:52, Approximately 47:53, Approximately 46:54, Approximately 45:55, Approximately 44:56, Approximately 43:57, Approximately 42:58, Approximately 41:59, Approximately 40:60, Approximately 39:61, Approximately 38:62, Approximately 37:63, Approximately 36:64, Approximately 35:65, Approximately 34:66, Approximately 33:67, Approximately 32:68, Approximately 31:69, Approximately 30:70, Approximately 29:71, Approximately 28:7 2. Approximately 27:73, Approximately 26:74, Approximately 25:75, Approximately 24:76, Approximately 23:77, Approximately 22:78, Approximately 21:79, Approximately 20:80, Approximately 19:81, Approximately 18:82, Approximately 17:83, Approximately 16:84, Approximately 15:85, Approximately 14:86, Approximately 13:87, Approximately 12:88, Approximately 11:89, Approximately 10:90, Approximately 9:91, Approximately 8:92, Approximately 7:93, Approximately 6:94, Approximately 5:95, Approximately 4:96, Approximately 3:97, Approximately 2:98, or Approximately 1:99.

Clause 109. The article of manufacture according to any one of Clauses 101 to 107, wherein the w/w ratio of the silk core protein fragments in the coating to the surfactant is about 1:1.

Clause 110. The article of any one of Clauses 101 to 109, wherein the surfactant is selected from cocoyl glucoside, decyl glucoside, lauryl glucoside, sucrose cocoate, octyl/octyl glucoside and octyl/octyl glucoside.

Clause 111. The article of any one of Clauses 101 to 109, wherein the surfactant is selected from octyl/octyl glucoside and octyl/octyl glucoside.

Clause 112. An article according to any one of Clauses 101 to 111, wherein the article has improved moisture management compared with a similar article comprising a similar fabric but without a coating.

Clause 113. Articles of manufacture according to Clause 112, wherein moisture management is evaluated by a water absorption test, a vertical wicking test, or a drying rate test.

Clause 114. A method for preparing a silk core protein coated fabric, the method comprising: applying a solution containing a surfactant to the fabric; applying a silk core protein fragment solution to the fabric; and drying the fabric.

Clause 115. A method for preparing a silk core protein coated fabric, the method comprising: applying a solution comprising a surfactant and silk core protein fragments to the fabric; and drying the fabric.

Clause 116. The method according to Clause 114 or Clause 115, wherein the concentration of the silk core protein fragment in the solution ranges from 0.01 g/L to about 100 g/L.

Clause 117. The method according to any one of Clauses 114 to 116, wherein the concentration of the surfactant in the solution ranges from 0.01 g/L to about 100 g/L.

Clause 118. The method according to any one of Clauses 114 to 117, wherein the w/w ratio of the silk core protein fragment to the surfactant is about 99:1, about 98:2, about 97:3, about 96:4, about 95:5, about 94:6, about 93:7, about 92:8, about 91:9, about 90:10, about 89:11, about 88:12, about 87:13, about 86:14, about 85:15, about 84:16, about 83:17, about 82:18, about 81:19, about 80:20, about 7 9:21, about 78:22, about 77:23, about 76:24, about 75:25, about 74:26, about 73:27, about 72:28, about 71:29, about 70:30, about 69:31, about 68:32, about 67:33, about 66:34, about 65:35, about 64:36, about 63:37, about 62:38, about 61:39, about 60:40, about 59:41, about 58:42, about 57:43, about 56:44, about 55:45, about 54:46, about 53:47, about 52:48, about 51:49, about 50:50, about 49:51, about 48:52, about 47:53, about 46:54, about 45:55, about 44:56, about 43:57, about 42:58, about 41:59, about 40:60, about 39:61, about 38:62, about 37:63, about 36:64, about 35:65, about 34:66, about 33:67, about 32:68, about 31:69, about 30:70, about 29:71, about 28:72 Approximately 27:73, 26:74, 25:75, 24:76, 23:77, 22:78, 21:79, 20:80, 19:81, 18:82, 17:83, 16:84, 15:85, 14:86, 13:87, 12:88, 11:89, 10:90, 9:91, 8:92, 7:93, 6:94, 5:95, 4:96, 3:97, 2:98, or 1:99.

Clause 119. The method according to any one of Clauses 114 to 118, wherein the solution further comprises one or more of a wetting agent, an antifoaming agent, a softening agent, a wicking agent, and an antimicrobial agent.

Clause 120. The method according to any one of Clauses 114 to 119, wherein the silken protein fragment has an average weight-average molecular weight selected from about 1 kDa to about 5 kDa, about 5 kDa to about 10 kDa, about 6 kDa to about 17 kDa, about 10 kDa to about 15 kDa, about 14 kDa to about 30 kDa, about 15 kDa to about 20 kDa, about 17 kDa to about 39 kDa, about 20 kDa to about 25 kDa, about 25 kDa to about 30 kDa, about 30 kDa to about 35 kDa, about 35 kDa to about 40 kDa, about 39 kDa to about 54 kDa, about 39 kDa to about 80 kDa, about 40 kDa to about 45 kDa, about 45 kDa to about 50 kDa, about 50 kDa to about 55 kDa, about 55 kDa to about 60 kDa, about 60 kDa to about 100 kDa, or about 80 kDa to about 144 kDa, and a polydispersity ranging from 1 to about 5.

Clause 121. The method according to any one of Clauses 114 to 120, wherein the polydispersity of the silk core protein fragment is 1 to about 1.5, about 1.5 to about 2.0, about 2.0 to about 2.5, about 2.5 to about 3.0, about 3.0 to about 3.5, about 3.5 to about 4.0, about 4.0 to about 4.5, or about 4.5 to about 5.0.

Clause 122. The method according to any one of Clauses 114 to 120, wherein the polydispersity of the silk core protein fragment is from about 1.5 to about 3.0.

Clause 123. The method according to any one of Clauses 114 to 120, wherein the silk core protein fragment comprises one or more of low molecular weight silk core protein fragments and medium molecular weight silk core protein fragments.

Clause 124. The method according to any one of Clauses 114 to 123, wherein the solution further comprises about 0.01% (w/w) to about 10% (w/w) of sericin relative to the said sericin fragment.

Clause 125. The method according to any one of Clauses 114 to 124, wherein the fabric comprises one or more of the following: polyester, polyamide, polyaramid, polytetrafluoroethylene, polyethylene, polypropylene, polyurethane, silicone, a mixture of polyurethane and polyethylene glycol, ultra-high molecular weight polyethylene, high performance polyethylene, nylon, LYCRA (polyester-polyurethane copolymer, also known as SPANDEX and elastomer), or a mixture thereof.

Clause 126. The method according to any one of Clauses 114 to 125, wherein the surfactant is selected from cocoyl glucoside, decyl glucoside, lauryl glucoside, sucrose cocoate, octyl/octyl glucoside and octyl/octyl glucoside.

Clause 127. The method according to any one of Clauses 114 to 125, wherein the surfactant is selected from octyl/octyl glucoside and octyl/octyl glucoside.

Clause 128. The method according to any one of Clauses 114 to 127, wherein the drying includes heating.

Clause 129. The method according to Clause 128, wherein the heating substantially does not alter the properties of the coating.

Clause 130. The method according to any one of Clauses 114 to 129, wherein the pH of the solution is acidic.

Clause 131. The method according to any one of Clauses 114 to 129, wherein the pH of the solution is about 4 to about 4.5.

Clause 132. An article prepared by any one of Clauses 114 to 131.

Clause 133. The article of the invention as described in Clause 132, wherein the article of the invention has improved moisture management compared with a similar article of the invention comprising a similar fabric but without a coating.

Clause 134. Articles of manufacture according to Clause 133, wherein moisture management is assessed by a water absorption test, a vertical wicking test, or a drying rate test.

Clause 201. An article comprising a fabric and a coating, wherein the coating comprises a surfactant and/or an emulsifier and a silk core protein fragment having a fraction selected from about 1 kDa to about 5 kDa, about 5 kDa to about 10 kDa, about 6 kDa to about 17 kDa, about 10 kDa to about 15 kDa, about 14 kDa to about 30 kDa, about 15 kDa to about 20 kDa, about 17 kDa to about 39 kDa, about 20 kDa to about 25 kDa, and about 25 kDa. Average weight-average molecular weight of about 30 kDa, about 30 kDa to about 35 kDa, about 35 kDa to about 40 kDa, about 39 kDa to about 54 kDa, about 39 kDa to about 80 kDa, about 40 kDa to about 45 kDa, about 45 kDa to about 50 kDa, about 50 kDa to about 55 kDa, about 55 kDa to about 60 kDa, about 60 kDa to about 100 kDa, or about 80 kDa to about 144 kDa, and polydispersity ranging from 1 to about 5.

Clause 202. The article of manufacture according to Clause 201, wherein the polydispersity of said filoin fragment is from 1 to about 1.5, from about 1.5 to about 2.0, from about 2.0 to about 2.5, from about 2.5 to about 3.0, from about 3.0 to about 3.5, from about 3.5 to about 4.0, from about 4.0 to about 4.5 or from about 4.5 to about 5.0.

Clause 203. The article of manufacture according to Clause 201, wherein the polydispersity of the silk core protein fragment is from about 1.5 to about 3.0.

Clause 204. The article of manufacture according to Clause 201, wherein the silk core protein fragment comprises one or more of low molecular weight silk core protein fragments and medium molecular weight silk core protein fragments.

Clause 205. The article of any one of Clauses 201 to 204 further comprises about 0.01% (w/w) to about 10% (w/w) of sericin relative to the said sericin fragment.

Clause 206. Articles of any one of Clauses 201 to 205, wherein the fabric comprises one or more of the following: polyester, polyamide, polyaramid, polytetrafluoroethylene, polyethylene, polypropylene, polyurethane, silicone, a mixture of polyurethane and polyethylene glycol, ultra-high molecular weight polyethylene, high performance polyethylene, nylon, LYCRA (polyester-polyurethane copolymer, also known as SPANDEX and elastomer), or mixtures thereof.

Clause 207. The article of any one of Clauses 201 to 206, wherein the coating further comprises one or more of a wetting agent, a defoamer, a softener, a wicking agent and an antimicrobial agent.

Clause 208. The article according to any one of Clauses 201 to 207, wherein the w/w ratio of the silk core protein fragments in the coating to the surfactant and/or emulsifier is about 99:1, about 98:2, about 97:3, about 96:4, about 95:5, about 94:6, about 93:7, about 92:8, about 91:9, about 90:10, about 89:11, about 88:12, about 87:13, about 86:14, about 85:15, about 84:16, about 83:17, about 82:18, about 81:19. Approximately 80:20, 79:21, 78:22, 77:23, 76:24, 75:25, 74:26, 73:27, 72:28, 71:29, 70:30, 69:31, 68:32, 67:33, 66:34, 65:35, 64:36, 63:37, 62:38, 61:39, 60:40, 59:41, 58:42, 57:43, 56:44, 55:45, 5... 4:46, about 53:47, about 52:48, about 51:49, about 50:50, about 49:51, about 48:52, about 47:53, about 46:54, about 45:55, about 44:56, about 43:57, about 42:58, about 41:59, about 40:60, about 39:61, about 38:62, about 37:63, about 36:64, about 35:65, about 34:66, about 33:67, about 32:68, about 31:69, about 30:70, about 29:71, about 28 :72, 27:73, 26:74, 25:75, 24:76, 23:77, 22:78, 21:79, 20:80, 19:81, 18:82, 17:83, 16:84, 15:85, 14:86, 13:87, 12:88, 11:89, 10:90, 9:91, 8:92, 7:93, 6:94, 5:95, 4:96, 3:97, 2:98 or 1:99.

Clause 209. The article of any one of Clauses 201 to 207, wherein the w/w ratio of the silk core protein fragments in the coating to the surfactant and/or emulsifier is about 1:1, about 1:2, about 1:4, about 1:8, about 1:16 or about 1:32.

Clause 210. The article according to any one of Clauses 201 to 209, wherein the emulsifier and/or surfactant is selected from polyoxyethylene sorbitan monooleate, polyoxyethylene sorbitan trioleate, polyoxyethylene castor oil, and any combination thereof.

Clause 211. The article according to any one of Clauses 201 to 209, wherein the emulsifier and/or surfactant is selected from polyoxyethylene (10-30) sorbitan monooleate, polyoxyethylene (10-30) sorbitan trioleate, polyoxyethylene (10-50) castor oil, and any combination thereof.

Clause 212. The article according to any one of Clauses 201 to 209, wherein the emulsifier and/or surfactant is selected from polyoxyethylene (20) sorbitan monooleate, polyoxyethylene (20) sorbitan trioleate, polyoxyethylene (29) castor oil, and any combination thereof.

Clause 213. Articles according to any one of Clauses 201 to 212, wherein the emulsifier and/or surfactant has an HLB value between 11 and 13.50.

Clause 214. An article of any one of Clauses 201 to 213, wherein the article has improved moisture management compared with a similar article comprising a similar fabric but without a coating.

Clause 215. Articles of manufacture according to Clause 214, wherein moisture management is assessed by a water absorption test, a vertical wicking test, or a drying rate test.

Clause 216. An article according to any one of Clauses 201 to 213, wherein the article has improved drape compared to a similar article comprising a similar fabric but without a coating.

Clause 217. An article of any one of Clauses 201 to 213, wherein the article has improved smoothness compared with a similar article comprising a similar fabric but without a coating.

Clause 218. An article of any one of Clauses 201 to 213, wherein the article has an improved hand feel compared to a similar article comprising a similar fabric but without a coating.

Clause 219. A method for preparing a silk core protein coated fabric, the method comprising: applying a solution comprising a surfactant and/or emulsifier system to the fabric; applying a silk core protein fragment solution to the fabric; and drying the fabric.

Clause 220. A method for preparing a silk core protein coated fabric, the method comprising: applying a solution comprising a surfactant and/or emulsifier system and silk core protein fragments to the fabric; and drying the fabric.

Clause 221. The method according to Clause 219 or Clause 220, wherein the concentration of the filamentin fragment in the solution ranges from 0.01 g/L to about 100 g/L.

Clause 222. The method according to any one of Clauses 219 to 221, wherein the concentration of the surfactant and/or emulsifier system in the solution ranges from 0.01 g/L to about 100 g/L.

Clause 223. The method according to any one of Clauses 219 to 222, wherein the w/w ratio of the silk core protein fragment to the surfactant and/or emulsifier system is about 99:1, about 98:2, about 97:3, about 96:4, about 95:5, about 94:6, about 93:7, about 92:8, about 91:9, about 90:10, about 89:11, about 88:12, about 87:13, about 86:14, about 85:15, about 84:16, about 83:17, about 82:18, about 81:19, about 8 0:20, approximately 79:21, approximately 78:22, approximately 77:23, approximately 76:24, approximately 75:25, approximately 74:26, approximately 73:27, approximately 72:28, approximately 71:29, approximately 70:30, approximately 69:31, approximately 68:32, approximately 67:33, approximately 66:34, approximately 65:35, approximately 64:36, approximately 63:37, approximately 62:38, approximately 61:39, approximately 60:40, approximately 59:41, approximately 58:42, approximately 57:43, approximately 56:44, approximately 55:45, approximately 54 :46, about 53:47, about 52:48, about 51:49, about 50:50, about 49:51, about 48:52, about 47:53, about 46:54, about 45:55, about 44:56, about 43:57, about 42:58, about 41:59, about 40:60, about 39:61, about 38:62, about 37:63, about 36:64, about 35:65, about 34:66, about 33:67, about 32:68, about 31:69, about 30:70, about 29:71, about 28: 72, 27:73, 26:74, 25:75, 24:76, 23:77, 22:78, 21:79, 20:80, 19:81, 18:82, 17:83, 16:84, 15:85, 14:86, 13:87, 12:88, 11:89, 10:90, 9:91, 8:92, 7:93, 6:94, 5:95, 4:96, 3:97, 2:98 or 1:99.

Clause 224. The method according to any one of Clauses 219 to 222, wherein the w/w ratio of the silk core protein fragment to the surfactant and/or emulsifier system is about 1:1, about 1:2, about 1:4, about 1:8, about 1:16 or about 1:32.

Clause 225. The method according to any one of Clauses 219 to 224, wherein the emulsifier and/or surfactant system comprises one or more of the following: polyoxyethylene sorbitan monooleate, polyoxyethylene sorbitan trioleate, polyoxyethylene castor oil, and any combination thereof.

Clause 226. The method according to any one of Clauses 219 to 224, wherein the emulsifier and/or surfactant system comprises one or more of the following: polyoxyethylene (10-30) sorbitan monooleate, polyoxyethylene (10-30) sorbitan trioleate, polyoxyethylene (10-50) castor oil, and any combination thereof.

Clause 227. The method according to any one of Clauses 219 to 224, wherein the emulsifier and/or surfactant system comprises one or more of the following: polyoxyethylene (20) sorbitan monooleate, polyoxyethylene (20) sorbitan trioleate, polyoxyethylene (29) castor oil, and any combination thereof.

Clause 228. The method according to any one of Clauses 219 to 224, wherein the emulsifier and/or surfactant has an HLB value between 11 and 13.50.

Clause 229. The method according to any one of Clauses 219 to 228, wherein the solution further comprises one or more of a wetting agent, an antifoaming agent, a softening agent, a wicking agent, and an antimicrobial agent.

Clause 230. The method according to any one of Clauses 219 to 229, wherein the silken protein fragment has an average weight-average molecular weight selected from about 1 kDa to about 5 kDa, about 5 kDa to about 10 kDa, about 6 kDa to about 17 kDa, about 10 kDa to about 15 kDa, about 14 kDa to about 30 kDa, about 15 kDa to about 20 kDa, about 17 kDa to about 39 kDa, about 20 kDa to about 25 kDa, about 25 kDa to about 30 kDa, about 30 kDa to about 35 kDa, about 35 kDa to about 40 kDa, about 39 kDa to about 54 kDa, about 39 kDa to about 80 kDa, about 40 kDa to about 45 kDa, about 45 kDa to about 50 kDa, about 50 kDa to about 55 kDa, about 55 kDa to about 60 kDa, about 60 kDa to about 100 kDa, or about 80 kDa to about 144 kDa, and a polydispersity ranging from 1 to about 5.

Clause 231. The method according to any one of Clauses 219 to 230, wherein the polydispersity of the silk core protein fragment is 1 to about 1.5, about 1.5 to about 2.0, about 2.0 to about 2.5, about 2.5 to about 3.0, about 3.0 to about 3.5, about 3.5 to about 4.0, about 4.0 to about 4.5 or about 4.5 to about 5.0.

Clause 232. The method according to any one of Clauses 219 to 230, wherein the polydispersity of the silk core protein fragment is from about 1.5 to about 3.0.

Clause 233. The method according to any one of Clauses 219 to 232, wherein the silk core protein fragment comprises one or more of low molecular weight silk core protein fragments and medium molecular weight silk core protein fragments.

Clause 234. The method according to any one of Clauses 219 to 233, wherein the solution further comprises about 0.01% (w/w) to about 10% (w/w) of sericin relative to the said sericin fragment.

Clause 235. The method according to any one of Clauses 219 to 234, wherein the fabric comprises one or more of the following: polyester, polyamide, polyaramid, polytetrafluoroethylene, polyethylene, polypropylene, polyurethane, silicone, a mixture of polyurethane and polyethylene glycol, ultra-high molecular weight polyethylene, high performance polyethylene, nylon, LYCRA (polyester-polyurethane copolymer, also known as SPANDEX and elastomer), or a mixture thereof.

Clause 236. The method according to any one of Clauses 219 to 235, wherein the drying includes heating.

Clause 237. The method according to any one of Clauses 219 to 236, wherein the pH of the solution is acidic.

Clause 238. The method according to any one of Clauses 219 to 236, wherein the pH of the solution is about 4 to about 4.5.

Clause 239. An article prepared by any one of Clauses 219 to 238.

Clause 240. The article of the invention as described in Clause 239, wherein the article of the invention has improved moisture management compared with a similar article of the invention comprising a similar fabric but without a coating.

Clause 241. Articles of manufacture according to Clause 240, wherein moisture management is assessed by a water absorption test, a vertical wicking test, or a drying rate test.

Clause 242. The article of the claim pursuant to Clause 239, wherein the article has improved drape compared to a similar article comprising a similar fabric but without a coating.

Clause 243. The article of the invention as described in Clause 239, wherein the article of the invention has improved smoothness compared with a similar article of the invention comprising a similar fabric but without a coating.

Clause 244. The article of the invention as described in Clause 239, wherein the article of the invention has an improved hand feel compared to a similar article of the invention which comprises a similar fabric but does not have a coating.

Example

The embodiments covered herein are now described with reference to the following examples. These examples are provided for illustrative purposes only, and the disclosure covered herein should in no way be construed as limiting to these examples, but rather as covering any and all variations as understood as a result of the teachings provided herein.

The compositions disclosed herein can be prepared by various methods known in the art. These methods include those described in the following embodiments and those described in the following specific examples. Modifications to such methods involving techniques commonly used in the field of textile products can also be used.

Example 1: Use of silk core protein and surfactants in synthetic fabrics

As described in this embodiment, fibroin can be used together with surfactants to synthesize fabrics.

Active yarn ^™ molecules containing octyl/octyl glucoside (derived from sugar) provide enhanced moisture management properties for various types of nylon fabrics.

The comfort properties of clothing, especially casual and sportswear, largely depend on its moisture management properties. Moisture management is the ability of textile fabrics to absorb moisture (sweat) from the skin, transfer the moisture to the outer surface, and release it into the environment. With the continued high demand for comfortable clothing, this sector holds enormous growth potential.

Moisture management performance can be enhanced by employing microfiber technology and applying various chemical finishing agents. Microfiber technology increases the specific surface area of the fabric, thus allowing for higher liquid transfer rates. The former option is quite expensive, making chemical finishing options more popular among most manufacturers.

While various moisture management treatments are available for nylon, sustainable chemicals derived from natural sources and the issue of zero-waste management have not been widely reported. Therefore, it is crucial to identify green chemicals for moisture management that are friendly to end-users, water supply systems, the environment, and manufacturers.

Coating of nylon fabrics

The coating solution was prepared by adjusting the pH of water to 4-4.5 using acetic acid. Octyl/octanoyl glucoside was then added to the desired concentration (0.1%), followed by the addition of active silk ^™ at a ratio of 1:1 (v/v) to octyl/octanoyl glucoside. The pH of the final solution was checked and adjusted if it deviated from the 4-4.5 range.

The coating solution was applied to the nylon fabric using a padding roller at a rate of 3 m/min via a padding and curing method. The moisture absorption rate was controlled to 60% ± 3% by adjusting the roller pressure.

The fabric was dried and cured in an oven at 160°C for 1.5 minutes, then left to stand overnight before performance testing.

Performance testing

Moisture management can be evaluated using various testing standards, such as absorbency tests, vertical wicking tests, and drying rate tests. Although the results are expressed differently using different testing methods, the characterization of moisture management performance is relevant.

In this development, a modified AATCC 79 test method for water absorption of textiles was used to determine moisture management performance.

Test Results

Figures 3 and 4 show the test results of active yarns coated with octyl/octyl glucoside on various nylon fabrics, including interlocking fabrics, sweatshirts, warp-knitted fabrics, and padding structures. The results indicate that this novel solution generally improves the absorbency of various nylon fabrics, demonstrating a general improvement in moisture management performance.

Figure 3. Absorbency of Active Yarn ^™ with Octyl/Octayl Glucoside Coating on Various Interlocking Nylon Fabrics. Untreated interlocking nylon fabrics cannot absorb moisture due to poor absorbency. After coating Active Yarn ^™ with Octyl/Octayl Glucoside, the absorbency of all interlocking nylon fabrics increased significantly.

Figure 4. Absorbency of Active Yarn ^™ with Octyl/Octayl Glucoside Coating on Various Nylon Fabrics, excluding the interlocking structure. Untreated nylon fabrics have poor or no absorbency; however, after coating Active Yarn ^™ with Octyl/Octayl Glucoside Coating, the absorbency of all nylon fabrics significantly increases.

Example 2: Use of silk core protein and emulsifiers and/or surfactants on synthetic fabrics

As described in this embodiment, fibroin can be used in conjunction with surfactants and/or emulsifiers to synthesize fabrics. In a non-limiting example, fibroin fragments are used with an emulsion of three ethoxylated fatty acids to impart smoothness and drape to nylon and polyester fabrics without inhibiting the moisture management properties imparted by wicking agents. Wicking agents in textiles are commonly used to improve the comfort properties of casual and sportswear by enhancing the moisture management properties of nylon and polyester fabrics. However, a common problem with many wicking agents is that they consist of hydrophilic surfactants or polymers that attract moisture between the fibers of the textile, causing the fabric to feel heavier and rougher than when not worn. With the widespread use of these surfactants as moisture management agents, new developments are possible in the field of softeners that impart smoothness and drape without inhibiting moisture management properties. Currently, most softeners suffer from two problems: (i) because many of them are oil-based, their hydrophobic properties inhibit water absorption; and (ii) many softeners are derived from petrochemical resources, leading to waste and sustainability issues. While a relatively large number of polymers and oils can enhance fabric hand feel and moisture management, the selection of 100% bio-based fabric softeners is limited. Therefore, there is a need to develop 100% bio-based natural fabric softeners that, when used in conjunction with wicking agents, impart a good hand feel without inhibiting the fabric's moisture management properties.

Without being bound by any particular theory, the system described herein comprises a mixture of ethoxylated monooleate fatty acids, ethoxylated trioleate fatty acids, and hydroxy fatty acids, with an average HLB value between 12 and 12.1 (calculated using Formula 1), acting as an emulsifier and softener, and an active fiber acting as a moisture wicking agent. In this system, variations in the ratio of fatty acids to hydroxy fatty acids result in different HLB values (as shown in Table 2). This, in turn, alters the wash resistance and softening ability of the coating.

Formula 1:

_Ni : The number of moles of surfactant molecule i in the solution; N: The total number of moles of surfactant in the solution; _Mi : The molar mass of the hydrophilic group on surfactant molecule i; _Mi : The total molar mass of surfactant molecule i.

Coating of nylon fabrics

An emulsified mixture of surfactants was prepared by combining polyoxyethylene (20) dehydrated sorbitan monooleate, polyoxyethylene (20) dehydrated sorbitan trioleate, polyoxyethylene (29) castor oil, and water in a ratio of 2:4:8:10 (by mass). The mixture was then sonicated for 3 hours.

The wicking agent solution is then prepared as follows: Active Silk ^™ moisture management agent is added to water at a concentration of 1 g/L. The pH of the solution is then adjusted to 4.5-5 using acetic acid.

After preparing the wicking solution, the surfactant emulsion mixture is then added to the solution at the mass ratios defined in Table 1.

The solution is applied to the fabric via padding and curing at a rate of 3 meters per minute, and the moisture absorption rate is controlled to 50% by roller pressing.

The fabric is then cured in a drying oven at 160°C for 1.5 to 3 minutes, depending on the fabric, and then equilibrated overnight.

Coating of polyester fabrics

An emulsified mixture of surfactants was prepared by combining polyoxyethylene (20) dehydrated sorbitan monooleate, polyoxyethylene (20) dehydrated sorbitan trioleate, polyoxyethylene (29) castor oil, and water in a ratio of 2:4:8:10 (by mass). The mixture was then sonicated for 3 hours.

The wicking agent solution is then prepared as follows: Active Silk ^™ moisture management agent is added to water at a concentration of 1 g/L. The pH of the solution is then adjusted to 4.5-5 using acetic acid.

After preparing the wicking solution, the surfactant emulsion mixture is then added to the solution at the mass ratios defined in Table 1.

The solution is applied to the fabric via padding and curing at a rate of 3 meters per minute, and the moisture absorption rate is controlled to 50% by roller pressing.

The fabric is then cured in a drying oven at 135°C for 1 to 2 minutes, depending on the fabric, and then equilibrated overnight.

Table 1.1 lists the ratios (by mass and final concentration) of the emulsion mixture (emulsion) of silk and surfactant in an aqueous solution.

POMO(g) POTO(g) EC(g) Water (g) HLB a 2 4 0.5 10 12.56 b 2 4 1 10 12.5 c 2 4 2 10 12.39 d 2 4 4 10 12.25 e 2 4 8 10 12.09 f 2 4 16 10 11.94

Table 2. List of surfactants: polyoxyethylene (20) sorbitan monooleate (POMO), polyoxyethylene (20) sorbitan trioleate (POTO), and polyoxyethylene (29) castor oil (EC), mixed in different ratios, and their corresponding HLB values. Row e includes the ratios of surfactants used in the emulsion mixtures of Table 1.

Test methods

Fabric properties

All samples underwent a hand feel test by a panel of N=3 reviewers, and comparisons were made based on factors such as drape (the ease with which the fabric deforms when handled by a user) and smoothness (the apparent roughness of the fabric when rubbed by the user). The test followed a method defined in-house. An absorbency test defined in-house was also used to assess inhibition of moisture management.

Silk washability

The quantitative determination of filaments deposited on the surface was measured using UV/Vis absorbance. Standard curves were generated using different concentrations of filaments in water. Absorbance at 276 nm (tyrosine absorption peak) was then measured to generate a linear curve of absorbance versus solution concentration.

The mass of remaining fibers on the fabric was tested. The fabric was immersed in a 7.6 M LiBr solution overnight under ultrasonic treatment. The fabric was then removed from the solution, and the UV/Vis absorbance of the solution was measured to determine the fiber concentration in the solution. The mass of remaining fibers on the fabric could be calculated using the volume of the solution, the fiber concentration in the solution, and the mass of the fabric.

Test Results

Surfactant system with lightweight fibers

HLB adjustment concentration

According to moisture management data, the optimal concentration for the shortest absorption time was 2 g/L polyoxyethylene (29) castor oil (mixture HLB: 12.39). However, when the concentration was increased to 16 g/L (mixture HLB: 11.94), the absorption time only increased by an average of 17%, and the fabrics all met the maximum standard of 2 seconds absorption time (Figure 5). From a hand feel perspective, generally, the hand feel improved with increasing polyoxyethylene (29) castor oil concentration (Figure 6).

Figure 5 shows the unwashed absorbency curves produced by varying the concentration of polyoxyethylene (29) castor oil in the emulsifier mixture (thus altering the HLB) before addition to the coating solution. Note that the filament concentration in the coating solution was 1 g/L in all samples.

Figure 6 shows the unwashed hand feel grade curves produced by varying the concentration of polyoxyethylene (29) castor oil in the emulsifier mixture (thus altering the HLB) before addition to the coating solution. Note that the silk concentration in the coating solution was 1 g/L in all samples.

Concentration study of surfactant system

As shown in Figure 5, the moisture management data indicates that the decrease in moisture management performance of all tested polyester and nylon fabrics coated with wicking agents and natural softeners was negligible after 0 to 25 washes. The data also shows that all fabrics except JintexGreen exhibited absorbance times of less than 3 seconds after 0 to 25 washes (Figures 7A-7D).

Regarding improvements in hand feel, as shown in Figure 6, the hand feel of the fabric significantly improved with increasing concentration of the natural fabric softener at wash 0. Although the performance decreased slightly after washing, the hand feel remained after 5, 10, and 25 washes (Figure 8).

Figures 7A-7D are graphs showing the moisture management data for unwashed (Figure 7A), 5-washed (Figure 7B), 10-washed (Figure 7C), and 25-washed (Figure 7D) samples produced by varying the concentration of the emulsion mixture (polyoxyethylene (20) dehydrated sorbitol monooleate, polyoxyethylene (20) dehydrated sorbitol trioleate, polyoxyethylene (29) castor oil, and water in a ratio of 2:4:8:10) in the final coating solution; in all samples, the filament concentration in the coating solution was 1 g/L.

Figures 8A-8D are graphs showing the results of unwashed (Figure 8A), 5-washed (Figure 8B), 10-washed (Figure 8C), and 25-washed (Figure 8D) hand feel grades produced by varying the concentration of the emulsion mixture (polyoxyethylene (20) dehydrated sorbitol monooleate, polyoxyethylene (20) dehydrated sorbitol trioleate, polyoxyethylene (29) castor oil, and water in a ratio of 2:4:8:10) in the final coating solution; 1 represents the best hand feel grade score, and 8 represents the worst hand feel grade score; in all samples, the silk concentration in the solution was 1 g/L.

Polyoxyethylene (20) dehydrated sorbitan monooleate with medium weight filaments

According to moisture management data, the absorption time hardly changes with increasing medium-weight yarn weight. Without being bound by any particular theory, generally, the absorption time of medium-weight yarn is longer than that of its low-weight yarn. For a low-molecular-weight yarn of 20 g/L, only one fabric exceeded the 2-second retention standard. However, even with zero washes, one fabric still passed this threshold. When comparing the same fabrics between low-weight and medium-weight yarns, this behavior only worsens with increasing washes (Figures 10A-10D).

From a tactile perspective, similar to the moisture management data, there appears to be no obvious trend in the increase of medium-weight filaments in the coating solution (Figures 9A-9D).

Figures 9A-9D are graphs showing the hand feel grades obtained by varying the concentration of medium molecular weight yarns in the final coating solution for unwashed (Figure 9A), 5-wash (Figure 9B), 10-wash (Figure 9C), and 25-wash (Figure 9D) grades; 1 represents the best grade, and 8 represents the worst grade.

Figures 10A-10D are graphs showing the results of moisture management for unwashed (Figure 10A), 5-wash (Figure 10B), 10-wash (Figure 10C), and 25-wash (Figure 10D) results by varying the concentration of medium molecular weight filaments in the final coating solution.

Quantity of filaments on nylon fabric

The concentration of silk in the solution can be measured by measuring the absorbance of the 276 nm peak of the silk spectrum using UV/Vis absorbance. To quantify the amount of silk remaining on the fabric, a standard curve is generated through continuous dilution of the stock solution. After measuring the absorbance of each solution, a linear curve is fitted to convert the solution absorbance into solution concentration. Silk can be removed from the silk-coated fabric by sonicating the sample in a 9 M LiBr solution for 3 hours. The remaining silk solution can then be measured to quantify the amount of silk removed from the fabric. To determine the fiber surface area, the cross-section of the filaments of each fabric is examined under a microscope to obtain the fabric denier, and the surface area is subsequently calculated.

As can be seen from Figure 11D, filaments are still present on the fabric after washing, but their quantity is reduced. When comparing the percentage of filament mass loss for each sample, the increase in fiber surface area appears to increase the mass loss of filaments in the fabric (Figure 11A). However, it is arguably the reciprocal of the amount of filaments absorbed by the fabric. The increase in fiber surface area appears to be correlated with the decrease in the amount of filaments absorbed by the fabric (Figure 11B). Without being bound by any particular theory, there appears to be a correlation between filament adhesion to the fabric and fiber surface area.

Figures 11A-11D are graphs showing the quantitative UV/Vis experiment of fabrics coated with low molecular weight active yarns and polyoxyethylene (20) monooleate solution. Figure 11A: Graph showing the percentage of yarn loss relative to fiber surface area after five washes. Figure 11B: Graph showing the quantitative mass of yarn on the coated fabric relative to fiber surface area. Figure 11C: Graph showing the percentage of yarn loss relative to fabric type after five washes. Figure 11D: Graph showing the quantitative mass of yarn on each fabric before and after five washes according to fabric type.

Figure 12 is a graph showing the quantitative UV/Vis experiment of a fabric coated with low molecular weight active yarn and polyoxyethylene (20) monooleate solution. The figure shows the quantitative mass of the yarn on the coated fabric relative to the fabric mass (g/m² (GSM)). This mass depends on the weave type, fiber content, and filament denier.

Study on surface charge of silk

Potentiometric titrations were performed on yarn-coated nylon fabrics, Archroma RPU-coated fabrics, and a nylon fabric control. Different nylon fabrics were coated with either active yarn (20 g/L) and polyoxyethylene (20) dehydrated sorbitan monooleate (2 g/L) or a solution containing 2% Archroma RPU liquid. Samples of each fabric were washed five times in a pre-wash machine using AATCC non-softening, non-brightening detergent. For the titration process, 0.1 M sodium chloride was used as the counterion, and hydrochloric acid or sodium hydroxide was used as the titrant.

As shown in Figures 13A-13C, the resulting titration curves indicate that the silk-coated fabric exhibits a greater negative charge at pH 5 (ΔC = -0.00316C ^g⁻¹ ) compared to the untreated fabric (ΔC = 0.00008C ^g⁻¹ ) or the fabric coated in Arcroa RPU liquid (ΔC = 0.00055C ^g⁻¹ ). Without being bound by any particular theory, this suggests that the silk-coated surface possesses a greater negative charge after washing compared to the untreated control or the positively charged Arcroa RPU-coated fabric.

Figures 13A-13C comprise a series of graphs showing the potentiometric titration curves of charge density at pH 5 for unfinished heavy double-knit nylon fabrics (Figure 13A), heavy double-knit nylon fabrics treated with reactive yarns (Figure 13B), and heavy double-knit nylon fabrics treated with Archroma RPU wetting agent (Figure 13C). Each fabric has titration curves obtained at unwashed (Figures 13A-13C, left) and after five washes (Figures 13A-13C, right). The change in charge density at pH 5 after washing is expressed as ΔC.