KR20170071792A - Functional coating composition and fabric using the same - Google Patents

Abstract

The present invention relates to a coating composition and a fabric using the coating composition, and more particularly, to a functional coating composition comprising an adhesive protein to which a functional peptide is added at an amine terminus or a carbon terminus and a fiber fabric using the functional coating composition. The coating composition of the present invention is stably coated on the surface of various daily articles such as a mobile phone liquid crystal protective film, a food packaging material, and a medical instrument as well as a fabric, thereby securing various functions such as antibacterial, antiviral, antioxidant, anti- There is an effect that can be done.

Description

BACKGROUND OF THE INVENTION 1. Field of the Invention [0001] The present invention relates to a functional coating composition,

The present invention relates to a functional coating composition based on a physiological functional adhesive, a functional fiber fabric using the functional coating composition, and a manufacturing method thereof. More particularly, the present invention relates to a coating composition comprising a physiological functional peptide introduced into a molecular skeleton of a mussel adhesive protein, a method of introducing physiological functionality into various fabrics using the coating composition, and a functional fabric thereof. Further, the present invention relates to an adhesive composition having improved adhesion and coating properties by introducing acrylate into the molecular skeleton of the adhesive protein.

In general, a coating method is applied to a surface of a fiber fabric drawn in a predetermined direction by controlling the height of a knife disposed in the transverse direction of the coated coating, It is a method of applying a coating agent composed of polyurethane, acrylic, silicone or the like according to the type and purpose of the fabric, and then passing through a dryer.

Recently, since various functionalities are required for textile fabrics, graphite, titanium, paint and the like, which are functional additives, are added to conventional polyurethane, acrylic, and silicone coating agents in order to impart various functions such as triboelectricity and antibacterial property, Method is applied.

Acrylic resin or polyurethane resin, which is a common textile fabric coating agent, has been used harmful organic solvent. To overcome this problem, environmentally friendly coating technology such as hydrophilic acrylic resin and hydrophilic urethane resin has been developed. However, There is a limit to commercialization due to problems such as sex. Hydrophilic acrylic resin and the like are disadvantageous in manufacturing cost and workability as compared with general acrylic resin or urethane resin, and also have problems in adhesiveness and miscibility with various additives with additives.

The present invention relates to a fiber coating agent using the above urethane resin, and a coating method for imparting functionality to fibers by using an aqueous urethane is disclosed in Korean Patent Registration No. 10-0822641, and graphite is added to the above- Korean Patent Registration No. 10-1220687 is further disclosed.

Korean Patent Registration No. 10-1220687 discloses a process for producing an aqueous urethane resin by reacting an aliphatic isocyanate with an ether type polyol to prepare an aqueous urethane having a solid content of 30 to 50% and a viscosity of 100 cps or less, adding graphite of 4 탆 or less to the aqueous urethane, The present invention relates to a functional fiber production method and a functional fiber which improve thermal insulation, water resistance, antimicrobial property, triboelectric property and the like through the process.

The aqueous urethane-graphite-added fiber coating agent used in the representative functional coating technology of Korean Patent Registration No. 10-1220687 has the following disadvantages. The aqueous polyurethane coating agent has poor flexibility, slip resistance, tensile / tearing resistance, and low solubility of graphite in a thin fiber fabric having a fiber fabric thickness of 50 D or less. It contains a large amount of water, so there is a small amount of solid in the coating agent, the adhesion to the surface of the fiber fabric is low, and the application power is low.

The functional coating composition of the present invention is composed of a pure protein adhesive. It can improve various coating disadvantages of the prior art as well as add various functionalities to the protein adhesive itself. Therefore, it is necessary to add functionalities such as antimicrobial and antioxidant And the advantage of being able to be coated regardless of the type and thickness of the fiber fabric is provided.

The molecular skeleton of the antimicrobial adhesive provided in one example of the present invention has an amphoteric characteristic and can be used as an additive in a conventional functional fabric coating product, and can be used as a water-soluble or oil-soluble coating agent.

The functional coating composition of the present invention has antibacterial, antiviral, UV absorption, and triboelectrification characteristics for a long period of time as compared with the prior art, and at the same time, the functional coating composition is not easily damaged by external environment or pressure It has durability. We developed a functional coating technology that is environmentally friendly because it is easy to apply to various products and is biodegraded under certain conditions and uses water as a coating or adhesive solvent.

Korean Patent Publication No. 10-1438711 Korean Patent Registration No. 10-0822641 Korean Patent Registration No. 10-1220687 Korean Patent Registration No. 10-0717903 Korean Patent Publication No. 10-2002-0062908

The present invention has been made to solve the above-mentioned problems, and it is an object of the present invention to provide an adhesive or coating composition which has an excellent coating ability on various fabric and fabric thicknesses, but generally shortens adhesion time or coating time of adhesive proteins, And to provide the above objects.

The present invention also relates to an antibacterial / antiviral / anti-atopic adhesive protein in which various functional peptides such as antimicrobial, anti-atopic, antiviral and other functional peptides are fused to the carbon terminal or amine terminal of the adhesive protein and a coating or bonding composition . In the present invention, the functional peptide means a substance having three or more amino acids capable of performing various physiological functions such as antibacterial, anticancer, anti-immunity, antiviral, anti-atopic,

In addition, the present invention provides various functional surface coatings by a simple method by introducing an acrylate group together with chemical modification of the tyrosine residue of the mussel adhesive protein with DOPA, and it is possible to coat various functional surfaces with a water-soluble coating composition for a long time under harsh conditions And to develop an environmentally friendly coating material capable of sustainability.

Another object of the present invention is to provide a photocurable antimicrobial coating material which can be applied to various processes such as a liquid crystal film or an electric appliance by the introduction of a photocurable acrylate.

Certain advantages and novel features of the present invention will become more apparent from the following detailed description and preferred embodiments with reference to the accompanying drawings.

The present invention provides a coating composition comprising an adhesive protein to which a functional peptide is added at the amine terminus or the carbon terminus.

According to one embodiment of the present invention, the adhesive protein may be selected from the group consisting of a mussel-derived adhesive protein, a barnacle-derived adhesive protein, and combinations thereof, but is not limited thereto. The adhesive protein derived from barnacle is preferably composed of the amino acid sequence of SEQ ID NO: 10, but is not limited thereto.

According to another embodiment of the present invention, an acrylate group or a urethane group may be introduced into the molecular skeleton of the adhesive protein. The adhesive protein is preferably a mussel-derived adhesive protein consisting of an amino acid sequence selected from the group consisting of SEQ ID NOS: 21 to 25, but is not limited thereto.

According to another embodiment of the present invention, it is preferable that the adhesive protein is mixed with a mussel-derived adhesive protein and a barnacle-derived adhesive protein at a mixing ratio (wt / wt) of 50:50.

According to one embodiment of the present invention, the coating composition of the present invention may further include a functional peptide having a function selected from the group consisting of antibacterial, antiviral, antioxidant, anti-ultraviolet, antistatic, anticancer and anticancer. Preferably, the antibacterial functional peptide has a function of acting on the cell membrane to destroy the cell membrane. According to a preferred embodiment of the present invention, the antibacterial functional peptide is selected from the group consisting of KLWKKWAKKWLKLWKA (SEQ ID NO: 26), FALALKALKKL (SEQ ID NO: 27), ILRWPWWPWRRK (SEQ ID NO: 28), AKRHHGYKRKFH (SEQ ID NO: 29), KWKLFKKIGAVLKVL (SEQ ID NO: 31), IWSILAPLGTTLVKLVAGIGQQKRK (SEQ ID NO: 32), GIGAVLKVLTTGLPALISWI (SEQ ID NO: 33), SWLSKTAKKGAVLKVL (SEQ ID NO: 34), KKLFKKILKYL (SEQ ID NO: 35), GLKKLISWIKRAAQQG But are not limited thereto. According to another preferred embodiment of the present invention, the antioxidant or anti-UV functional peptide may be composed of an amino acid sequence of ACQ (SEQ ID NO: 38) or PHCKRM (SEQ ID NO: 39), but is not limited thereto.

According to one embodiment of the present invention, the coating composition of the present invention may further comprise a hydrophilic resin. The hydrophilic resin may be selected from the group consisting of hydrophilic acrylates, urethanes, polyesters, and combinations thereof, but is not limited thereto. According to one embodiment of the present invention, the hydrophilic resin may be photocurable by a photocuring initiator, and the photocuring initiator may be benzoyl peroxide, but is not limited thereto.

The present invention also provides a functionalized surface coated with the coating composition of the present invention as described above.

According to one embodiment of the present invention, the functional surface may be formed of a material selected from the group consisting of a synthetic material, a biomaterial, a metal, a nonmetal, a glass, and a combination thereof, but is not limited thereto.

According to another embodiment of the present invention, the functional surface may be selected from the group consisting of a flat surface, a concave surface, a porous surface, a convex surface and a spherical surface, but is not limited thereto.

According to a preferred embodiment of the present invention, the functional surface may be a fiber fabric but is not limited thereto.

A functional coating composition based on an adhesive protein and an acrylated adhesive protein to which a functional peptide is added by gene recombination technology, a photocurable functional coating composition in which the above-mentioned adhesive protein and a urethane or acrylate resin are mixed, It is coated on the surface of various daily necessities such as mobile phone liquid crystal protective film, food packaging material, and medical instrument, and thus, various functions such as antimicrobial, antiviral, antioxidant, anti-ultraviolet ray and antistatic charging ability can be secured. Particularly, the present invention is based on the strong adhesion of adhesive proteins such as mussels and barnacles, and maintains essential functions such as antimicrobial activity, antioxidant property, antistatic chargeability, and the like in everyday life, It is possible to prevent a phenomenon in which the functionality is suppressed, such as a decrease in the antibacterial activity caused by the bacteria.

The above-described and other features and advantages of the present invention will be apparent upon consideration of the following embodiments and drawings provided for illustrative purposes.
FIG. 1 shows the results of isolation and purification of an antimicrobial adhesive protein having a spacer and a functional peptide introduced at the carbon end of a mussel adhesive protein in E. coli. A size marker is used to confirm that an antimicrobial adhesive protein with spacer and antimicrobial peptides is added to the mussel adhesive protein.
Fig. 2 shows a step of introducing an acrylate functional group into the side chain of the mussel adhesive protein molecule.
Fig. 3 shows NMR analysis results of the acrylated mussel adhesive protein. NMR analysis of the mussel adhesive protein and the acrylated mussel adhesive protein revealed that the hydrogen peak of the acrylate was confirmed and that the acrylate group was introduced into the molecular skeleton of the mussel adhesive protein by the acrylation process of FIG.
4 shows the antibacterial effect of the antimicrobial peptide with the concentration of the antimicrobial adhesive protein introduced therein. Antimicrobial adhesive was dissolved in distilled water to prepare coating solution having different concentration, and then coated on polystyrene surface, and then the antibacterial activity was measured.
FIG. 5 shows the result of measuring the antibacterial effect of the surface coated with the antibacterial adhesive on a time basis.
FIG. 6 is a result of spectroscopic analysis of the fabric surface after coating the fabric with an antibacterial adhesive. The antimicrobial coating was found to be good regardless of the method by coating the antimicrobial coating solution on the fabric and coating the fabric after immersing the fabric in the antimicrobial coating solution for a sufficient time.
Fig. 7 shows the result of measuring the antibacterial activity of the antimicrobial coated surface and the polyester fiber fabric. The concentration of the antimicrobial coating solution was 1 mg / mL, indicating that the antimicrobial effect was irrespective of the type of fabric, but the staphylococcus was not completely removed.
8 is a result of coating the fiber cloth with a high concentration of the antibacterial coating solution and measuring the antibacterial activity. It can be seen that the antimicrobial activity varies depending on the coating time, and it can be seen that most of the staphylococci are removed by coating over 24 hours.
9 shows the result of analysis of the surface of the antimicrobially coated fiber fabric with an electron microscope. Staphylococci are rarely present on the surface of antimicrobially coated fiber fabrics, whereas many staphylococci can be observed on the surface of general fabrics.

The present invention relates to a functional coating composition based on a bioadhesive, and provides a functional fiber fabric prepared by coating a variety of textile fabrics using the coating agent and a copper coating method. The present invention provides a coating composition to an adhesive protein to which a functional peptide such as antibacterial, antiviral, anti-ultraviolet, antistatic, anti-staining, and the like is added to an adhesive protein capable of self-adhesive or other adhesive in a humid or dry environment do.

The present invention also provides an acrylated adhesive protein prepared by introducing an acrylate group into a molecular skeleton of the above-mentioned adhesive protein, and an adhesive or coating composition based thereon.

In addition, the present invention provides an adhesive or coating composition improved in the above-described protein adhesive structure so that the above-mentioned adhesive protein or functional peptide added to the acrylated adhesive protein exerts the maximum effect on the coated surface.

According to one embodiment of the present invention, a functional coating composition capable of performing simple and efficient coating on various surfaces by introducing an acrylate group into the tyrosine portion of the adhesive protein to which the functional peptide has been added is DOPA-substituted.

It can also be applied to UV coatings or other processes that are widely used in the industry by providing an adhesive or coating composition based on acrylate-incorporated adhesive proteins.

Hereinafter, the present invention will be described in detail.

The present invention provides a functional coating composition characterized by a protein adhesive in which a functional peptide is added to the nitrogen or carbon terminus of an adhesive protein existing in nature or a recombinantly designed adhesive protein.

The present invention provides a functional coating composition characterized by an acrylated adhesive protein having an acrylate group introduced into a molecular skeleton of an adhesive protein to which various functional peptides are added.

The present invention provides a functional coating composition characterized by being mixed with an adhesive resin alone or a water-soluble acrylate-based adhesive resin or a water-soluble urethane-based resin.

According to one embodiment of the present invention, any suitable adhesive protein may be used as the adhesive material of the present invention.

The adhesive protein applied to the adhesive protein of the present invention includes all proteins capable of self-adhesion. Self-adhesive protein refers to a protein that is inherently adhesive or capable of being adhered or coated without the addition of a separate curing agent through chemical modification. Examples of commercially available self-adhesive proteins include, but are not limited to MAPTrix ™, a mussel-derived recombinant adhesive protein marketed by Colodis Biosciences, Inc., North Ogsta, South Carolina. Examples of adhesive proteins to which adhesiveness has been imparted through chemical modification include proteins modified with acrylate. For example, there are acrylated collagen or mussel adhesive proteins.

In an embodiment of the present invention, an antimicrobial coating composition comprising mussel adhesive protein, barnacle adhesive protein, shell adhesive protein, and adhesive protein wherein the molecular skeleton of the above-mentioned adhesive protein is acrylated, is provided as a self-adhesive protein .

The MAPTrix (TM) provided in the present invention is a recombinantly functionalized mussel or barnacle-derived adhesive protein. In the present invention, the adhesive protein may be used as it is, or it may be used as foot protein 3 (FP-3) described in SEQ ID NO: 1, 2, 3 or 4 or foot protein 5 (SEQ ID NO: (FP-5), carbon of foot protein 6 (FP-6) described in SEQ ID NO: 9, first peptide corresponding to the carbon end or amine end or both of the barnyard adhesive protein described in SEQ ID NO: At least one second peptide selected from the group consisting of SEQ ID NOS: 11, 12, 13, 14 and 15, FP-2 (SEQ ID NO: 20) and fragments of each protein can be fused . The protein selected as the second peptide may further comprise a spacer group at the carbon or amine terminus, and the preferred spacer group may be selected from the spacer described in SEQ ID NO: 16, 17, 18,

Preferably, the first peptide is FP-5 comprising the amino acid sequence of SEQ ID NO: 5, 6, 7 or 8, or a barbitone adhesion protein comprising the amino acid sequence of SEQ ID NO: 10 and the second peptide is SEQ ID NO: , FP-1 comprising an amino acid sequence of 12, 13, 14 or 15, FP-2 comprising an amino acid sequence of SEQ ID NO: 20. 16, 17, 18 or 19 at the amine or carbon terminus of FP-1 comprising the amino acid sequence of SEQ ID NO: 10, 12 or 14.

In one embodiment of the invention, the functional peptide is required to add various functions to the adhesive protein. The functional peptide may be added to the carbon terminus, amine terminus, or both of the above-mentioned adhesive proteins by gene recombination technology. For example, in the case of the fusion protein FP-151, an antioxidant peptide, an ultraviolet absorbing peptide, an antifouling peptide, and an amphipathic peptide can be added between FP-1 and FP-5 (see SEQ ID NO: 21 to SEQ ID NO: 24). In the case of the fusion protein FP-131, an antioxidant peptide, an ultraviolet absorbing peptide, an antifouling peptide and an amphipathic peptide can be added between FP-1 and FP-3 (see SEQ ID NO: 25). It is also possible to add different functional peptides between both ends or fusion proteins, for example, antimicrobial peptides or antiviral peptides and antiviral peptides, antimicrobial peptides and antioxidative peptides, antimicrobial peptides and anti-ultraviolet peptides at both ends have. For example, it includes antimicrobial peptides such as Magainin or Dermaseptin, which are alpha-helical 23 amino acid peptides separated from the skin of the African frog Xenopus laevis and include human defensins, Antibacterial peptides such as cathelicidin LL-37 and histatin may be added at both ends, but are not limited thereto.

In the present invention, in the case of an antimicrobial peptide added to an adhesive protein, all peptides derived from nature or artificially synthesized can be used. Antibacterial peptides exert their antimicrobial effect through mechanisms that disrupt the cell membranes of microorganisms or penetrate cell membranes and inhibit metabolic functions. In the present invention, all antimicrobial peptides that exhibit an antimicrobial effect by a mechanism of destroying the cell membrane of microorganisms are included. Preferably, the antimicrobial peptide to be added to the adhesive protein can be selected from gram-positive bacteria as well as antimicrobial peptides effective against gram-negative bacteria. KLWKKWAKKWLKLWKA (SEQ ID NO: 26), FALALKALKKL (SEQ ID NO: 27), ILRWPWWPWRRK (SEQ ID NO: 28) AKRHHGYKRKFH (SEQ ID NO: 29) KWKLFKKIGAVLKVL (SEQ ID NO: 30), LVKLVAGIKKLKWK (SEQ ID NO: 31), IWSILAPLGTTLVKLVAGIGQQKRK , GIGAVLKVLTTGLPALISWI (SEQ ID NO: 33), SWLSKTAKKGAVLKVL (SEQ ID NO: 34), KKLFKKILKYL (SEQ ID NO: 35), GLKKLISWIKRAAQQG (SEQ ID NO: 36), WLKKIGKKERVGQHTRDATIQGLGIAQQAANVAATAR (SEQ ID NO: 37).

Another functional adhesive protein provided by the present invention may be selected from the group of peptides having an antioxidative or anti-UV effect. Preferably, it can be selected from ACQ (SEQ ID NO: 38) and PHCKRM (SEQ ID NO: 39).

Another functional adhesive provided by the present invention can be selected from the group of peptides having an antiviral or anticancer effect. In the case of anticancer or antiviral functional adhesives, the peptide contains both natural or artificially designed peptides that have antiviral and anticancer effects simultaneously or separately. Preferably selected from the group consisting of the peptide RRWWCRC (SEQ ID NO: 40), the anticancer peptides THRPPMWSPVWP (SEQ ID NO: 41), KLLLKLLKKLLKLLKKK (SEQ ID NO: 42), FLKLLKKLAAKLF (SEQ ID NO: 43), RLLRRLLRRLLRRLLRRLLR (SEQ ID NO: 44), KLAKLAKKLAKLAK have.

In order to maximize the effect of the functional peptide added to the adhesive protein in the present invention, a functional coating composition is further provided wherein a spacer is further added between the adhesive protein and the functional peptide. As shown in Figure 1, the enzyme-treated mussel adhesive protein, when coated on a textile fabric or other surface adjacent to the antimicrobial peptide, limits the degree of freedom of the antimicrobial peptide to provide an antibacterial effect .

The cell membrane thickness of microorganisms is known to be 4 nm on average. In order for the cell membrane to be destroyed by the antimicrobial peptide, the antimicrobial peptide may have an effective antimicrobial effect when it has a degree of freedom sufficient to allow free interaction with the cell membrane. In order to increase the degree of freedom of the functional peptide, a spacer composed of a peptide having high flexibility between the adhesive protein and the functional peptide can be added.

In the case of the antimicrobial coating example of the present invention, a high concentration of an antibacterial adhesive protein coating solution is required in the absence of a spacer. The high concentration coating solution has a problem in that it can not be economically used and restricts its use. It is necessary to exert the functionality.

In an embodiment of the present invention, a coating composition for improving the degree of freedom of a functional peptide by adding glycine or serine-glycine motif as a spacer between a functional peptide such as an adhesive protein and an antibacterial peptide to maximize the function of the peptide on the coated surface . In the present invention, the length of the spacer has a length of 1 nm to 100 nm. The optimum length of the spacer can be adjusted according to the morphology of the coating surface, but if the spacer peptide length is too long, its function may be deteriorated by peptide folding. Thus, the spacer length is generally from 1 nm to 200 nm, more preferably from 2 nm to 100 nm. In an embodiment of the present invention, the spacer comprises a GGGGGG (SEQ ID NO: 16), SGSGSG (SEQ ID NO: 17), about 5 nm (SGSGSGSG) A functional adhesive protein having a spacer selected from the above.

In order to provide an antibacterial functional coating composition having a broad antibacterial effect in the present invention, a coating composition based on an antibacterial adhesive protein wherein different antibacterial peptides are added to the carbon end and amine end of the adhesive protein is provided. This antimicrobial coating composition is composed of an antibacterial adhesive protein to which a peptide KLWKKWAKKWLKLWKA (SEQ ID NO: 26) having an effect on Gram-negative bacteria at the carbon end and a peptide AKRHHGYKRKFH (SEQ ID NO: 29) having an effect on Gram-positive bacteria at the nitrogen end is added.

The present invention provides a coating composition comprising a mixture of an antibacterial peptide-added adhesive protein and an anti-UV or antioxidant peptide-added adhesive protein to provide a coating surface having an antimicrobial effect and an antioxidative effect or an anti-UV effect. In another embodiment, an antimicrobial peptide is attached to an amine or a carbon terminus to an adhesive protein, and an anti-ultraviolet peptide is added between a carbon or amine terminus or a fusion bonding protein to provide a coating composition having antimicrobial and antioxidant / anti-ultraviolet functions at the same time . The antimicrobial peptide is the peptide KLWKKWAKKWLKLWKA (SEQ ID NO: 26) and the antioxidant / anti-ultraviolet peptide provides the coating composition selected from ACQ (SEQ ID NO: 38), PHCKRM (SEQ ID NO: 39)

In the present invention, among antimicrobial adhesive proteins, tyrosine residues are converted into DOPA and further to dopaquinone through chemical modification, and thus modified dopa and dopaquinone are known to play a very important role in adhesion to the surface. Chemical modification of recombinant mussel adhesive proteins was carried out using mushroom-derived tyrosinase enzyme capable of mediating these chemical modifications. The chemically modified antimicrobial mussel adhesive protein can be attached to a variety of materials such as metals, plastics, and glass.

The concentration of the coating composition based on the antibacterial adhesive protein is 0.1 to 3% (wt / wt), and when it is mixed with acrylate or urethane resin, the effective concentration of the antibacterial adhesive protein can be increased or decreased. The concentration of the antimicrobial coating composition is preferably 0.1 to 1% (wt / wt), preferably the antimicrobial coating composition concentration is 0.1 to 3% (wt / wt), more preferably 0.1 to 0.3% (wt / wt).

The addition of a curing agent to an antimicrobial coating composition comprising an antimicrobial adhesive protein of the present invention can rapidly cure the coating composition to improve the productivity of the coating process that the surface coating can complete.

In general, the hardening rate of adhesive proteins present in nature is relatively slow. For example, mussel adhesive proteins extracted from mussels or chemically modified adhesive proteins of recombinantly designed mussel adhesive proteins are adhered to the surface by DOPA. The time required for complete coating in neutral or alkaline solvent conditions is at least 6 hours Or more. On the other hand, coatings generally require coating times in the order of a few minutes.

The acrylate used in the present invention can basically be introduced into the molecular skeleton of the adhesive protein. The antimicrobial coating composition provided in the present invention is composed of an antimicrobial adhesive protein into which an acrylate selected from at least one of urethane acrylate, polyester acrylate and epoxy acrylate is introduced.

The UV photocurable antimicrobial coating composition of the present invention is a UV photocurable coating comprising an antimicrobial adhesive protein. As photoinitiators, benzoyl peroxide, Irgacure 184, and the like may be used, but are not limited thereto. The weight ratio of the acrylate to the antibacterial adhesive protein is mixed at a ratio of 1: 0.01, preferably 1: 0.001.

An embodiment of the present invention provides a surface coated with the above-described functional coating composition. The surface coated with the coating composition provided by the present invention provides antifouling, antibacterial, antiviral, antioxidant, anti-cancer or anti-UV functions. All surfaces that can be coated or adhered by DOPA, acrylate, urethane or a combination thereof such as metal, non-metal, plastic, glass, composite material, material derived from living body, hybrid material composed of biomaterial and synthetic material, Surface.

In addition, the surface to which the present invention is applied is provided with various functions such as antimicrobial, antifouling, antioxidant, anti-ultraviolet ray, anti-electrostatic friction and the like on various surfaces such as flat surface, concave surface, porous surface and spherical surface.

In an embodiment of the present invention, an antibacterial textile fabric coated with a functional coating composition is provided. The textile fabric to which the present invention is applied may typically be polyester, nylon, or all fiber fabrics such as rayon. The amount of the coating composition or the UV photocurable antimicrobial composition applied to the fiber fabric can be appropriately selected in consideration of the amount of the functional adhesive protein, the kind of the fabric to be coated, the surface property, and the like.

The antimicrobial adhesive protein solution was chemically modified with tyrosinase and DOPA was introduced into the adhesive protein. The solution was lyophilized and dissolved in distilled water, and the antimicrobial coating solution was applied to the polyester fabric and the antibacterial functional coating was completed. The coated fabric was dried to produce an antibacterial fabric. The antimicrobial activity of the coated fabric was examined by examining the bacterial reduction rate on the uncoated surface and the coated surface of Escherichia coli and Staphylococcus aureus which are gram negative and positive bacteria.

The following examples are provided to illustrate preferred embodiments of the present invention and the present invention is not limited in scope by the following specific embodiments which are provided for illustrative purposes only. As disclosed in the present invention, functionally equivalent products, compositions and methods are obviously included within the scope of the present invention.

Example 1 Preparation of Expression Vector of Antibacterial Peptide Fused Mussel Adhesion Protein

For the production of the antibacterial mussel adhesive protein, a genetic sequence to which an antimicrobial peptide sequence was added at the carbon terminal portion of the mussel adhesive protein was designed and the synthesis of the nucleic acid encoding the antibacterial peptide as shown in Table 1 was commissioned to produce the expression vector in Kosumogentech . The constructed vector was transformed with E. coli BL21 (DE3), and the added antimicrobial sequences are shown in Table 1.

Preparation of Antibacterial Peptide Fused Mussel Adhesion Protein

1) E. coli BL21 (DE3) culture

E. coli BL21 (DE3) was cultured in LB (5 g / liter yeast extract, 10 g / liter Tryptone and 10 g / liter NaCl) medium and when the absorbance of the culture reached 0.6 at 600 nm, 1 mM to induce the expression of recombinant antimicrobial peptide fusion mussel adhesive protein. The E. coli BL21 (DE3) culture was centrifuged at 13,000 rpm for 4 to 10 minutes to obtain cell pellets, which were stored at -80 ° C.

2) Expression of Antibacterial Mussel Adhesion Protein

The cell pellet was diluted with 100 μg of SDS-PAGE buffer (0.5 M Tris-HCl, pH 6.8, 10% glycerol, 5% SDS, 5% β-mercaptoethanol, 0.25% bromophenol blue) and boiled at 100 ° C. for 5 minutes to denature . In the case of SDS-PAGE, the sample was electrophoresed on a 15% SDS-polyacrylamide gel, and protein bands were detected using Coomasie blue staining (see electrophoresis analysis result of FIG. 1).

3) Purification of antimicrobial peptide fusion mussel adhesive protein

The cell pellet obtained in item 1 was stirred using lysis buffer (2.4 g / L sodium phosphate monobasic, 5.6 g / L sodium phosphate dibasic, 10 mM EDTA and 1% Triton X-100), and cells were disrupted using a high pressure crusher Respectively. The lysate was centrifuged at 9,000 rpm for 20 minutes to obtain an insoluble protein aggregate containing mussel adhesive protein. The antimicrobial peptide fusion mussel adhesive protein was extracted from the insoluble protein aggregate using 25% acetic acid and centrifuged at 9,000 rpm for 20 minutes to recover the supernatant containing the mussel protein. The recovered supernatant was elevated to pH 12.8 using 10N NaOH, centrifuged under the same conditions, and the supernatant was recovered. The supernatant was neutralized to pH 6-7 using acetic acid and then centrifuged under the same conditions to obtain a precipitate of the antibacterial peptide fusion mussel adhesive protein. The resulting precipitate was dissolved in an appropriate amount of purified water and then lyophilized to obtain a lyophilized product of an antimicrobial peptide fusion mussel adhesive protein having a purity of 90% or more.

Example 2. Acrylation of Antimicrobial Adhesive

Hydrochloric acid was added to distilled water and 10 mL of an acidic solution whose acidity was adjusted to pH 4.0 was prepared. 10 mg of the antibacterial adhesive MAPTrix (TM) obtained in Example 3 and 10 mg of glycidyl acrylate were completely dissolved in each 1 mL of the solution, Stark solution is prepared. Prepare a 0.2 wt% antimicrobial MAPTrix ™ solution by mixing 3.875 mL of sodium phosphate buffer and 1 mL of MAPTrix ™ solution (1 wt%) in a 10 mL vial. 0.125 mL of glycidyl acrylate (1 wt% solution) is added to 0.2 wt% of MAPTrix ™ solution so that the acrylate / Lysine molar ratio is 0.1. The temperature of the reaction mussel is heated to 50 DEG C and subjected to an acrylation reaction for 8 hours. At the end of the reaction, dialysis is performed at 4 ° C using a UF membrane with a molecular weight cut off of 13 kDa.

After the dialysis, the solution was checked by NMR or spectroscopic analysis for acrylation. As shown in FIG. 3, the introduction rate of acryl was different depending on the acidity of the solvent. In the alkaline solvent (pH 8.5), the introduction rate of the acrylic group was low and the introduction rate of the acrylic group was high in the acidic solvent (pH 5.0).

Example 3. Measurement of antibacterial activity of antibacterial adhesive

To measure the antibacterial activity of the antibacterial adhesive protein obtained in Example 1, a coating solution was prepared. First, tyrosinase (SigmaAldrich) was added to 10 mM sodium borate (pH 5.5) solution at a concentration of 0.1 mg / mL to give a self-adhesive force. The mussel adhesive protein solution was added to 300 mL sodium acetate buffer solution. Oxygen was sufficiently dissolved in the mussel adhesive protein solution through oxygen bubbling, and the prepared tinacirotic solution was added to the mussel adhesive protein solution to impart the DOPA group to the mussel adhesive protein. After chemical modification with Tinacryrozyme for 1 hour, the base is removed and lyophilized is used for the production of antimicrobial coating solution.

The antimicrobial coating agent is prepared by using distilled water at a concentration of 10 to 0.01 mg / ml.

First, the plastic surface was coated with the antimicrobial peptide AMP 1 (KLWKKWAKKWLKLWKA, SEQ ID NO: 26), AMP2 (ILRWPWWPWRRK, SEQ ID NO: 28) and AMP 3 (AKRHHGYKRKFH, SEQ ID NO: 29), and then staphylococcus, After 30 minutes and 24 hours after the application, the surface of the plastic was washed with PBS solution, and living bacteria were collected, and the concentration of the strain was measured to calculate the reduction rate of the strain, and the antibacterial activity was measured. FIG. 4 shows the antibacterial activity according to the coating concentration of each antibacterial adhesive protein, and FIG. 5 shows the antibacterial activity according to the coating time of the antibacterial adhesive protein. As shown in Fig. 4, the three kinds of antimicrobial peptides have antimicrobial effects irrespective of the strain type even though they are immobilized on the surface. Depending on the type of antimicrobial peptide, the concentration for complete sterilization is different. Regardless of the concentration, AMP 1 (KLWKKWAKKWLKLWKA, SEQ ID NO: 26) completely removes all bacteria and all antimicrobial peptides have a complete antibacterial effect on E. coli. The longer the coating time, the greater the antibacterial effect. That is, the surface concentration of the antimicrobial peptide is proportional to the coating time.

Example 4. Antibacterial Coating of Fiber Fabric

An antibacterial coating solution was prepared by dissolving the antibacterial adhesive protein obtained in Example 3 in distilled water at a concentration of 1 mg / mL, 5 mg / mL, and 10 mg / mL. The antimicrobial coating of polyester fabric was done in two ways. First, the antimicrobial coating solution was sprayed onto the fabric, coated, and then the fabric surface was coated for 1 hour, followed by natural drying in a clean bench. In the second method, the fabric was completely immersed in the antimicrobial coating solution and allowed to be coated for 1 hour, 12 hours and 24 hours. The fabric was taken out and dried naturally on a clean bench.

Spectroscopic analysis was carried out using an FT-IR instrument to confirm the antimicrobial coating on the completely dried fabric. FIG. 6A shows that the antimicrobial coating time was 24 hours, and the B was 1 hour. As a result of the spectroscopic analysis of the fabric, it can be seen that the longer the antimicrobial coating time, the thicker the antimicrobial adhesive was coated on the surface of the fabric.

Example 5: Antibacterial activity measurement of antibacterial coating fabric

The surface of the fabric prepared in Example 4 was coated with the antibacterial coating solution prepared in Example 3. The pre-cultured staphylococcus test solution was diluted with PBS to 10 ^ 4 CFU / ml, and 10 pieces of 0.5 cm x 0.5 cm of the antimicrobial fiber fabric were placed in a tube containing Staphylococcus, Pseudomonas aeruginosa, and E. coli and cultured for 24 hours And the antimicrobial activity was measured. The antimicrobial activity was measured by a quantitative standard test according to JIS L 1902, an international standard. As shown in FIG. 7, when the antibacterial adhesive protein was low in concentration (1 mg / mL), the antimicrobial-coated fiber fabric had a reduction in staphylococci by 80% as compared with the control, but the fabric treated with the high- Respectively.

Example 6. Electron Microscopic Observation of Antibacterial Coated Fabric

The strain was added to the antibacterial coated fabric as in Example 5, and a 1 cm x 1 cm fabric sample was prepared. The microorganism was analyzed by electron microscopy to determine whether the actual strain was removed from the surface of the coated fabric. The surface of the antimicrobially coated fabric and the untreated fabric was observed with an electron microscope to confirm presence of staphylococci on the fabric surface (see FIG. 9). Staphylococci were rarely observed in the antimicrobial coated fabric, but many staphylococci were observed on the surface of the control uncoated plain fabric.

Example 7. Coating composition of an acrylated antimicrobial adhesive protein

The antimicrobial film was prepared by exposing the acrylated antibacterial adhesive to two UV bulbs in a UV room (wavelength of 285 nm) heated to 90 캜 and curing reaction for 10 minutes.

The antibacterial activity of the prepared antimicrobial film was tested for E. coli according to the same method and procedure as in Example 2 above. As compared with the uncoated control group, the growth of major host bacteria such as Escherichia coli, Staphylococcus aureus, Pneumococcus and Candida bacteria on the surface of the film coated with the acrylic antibacterial adhesive was not observed.

<110> Kollodis BioSciences, Inc.          LEE, SANG JAE <120> FUNCTIONAL COATING COMPOSITION AND FABRIC USING THE SAME <130> 2015-12-15 <160> 45 <170> Kopatentin 2.0 <210> 1 <211> 52 <212> PRT <213> Artificial Sequence <220> Foot protein type 3 (FP-3, Mytilus edulis) <400> 1 Ala Asp Tyr Tyr Gly Pro Lys Tyr Gly Pro Pro Arg Arg Tyr Gly Gly   1 5 10 15 Gly Asn Tyr Asn Arg Tyr Gly Gly Ser Arg Arg Tyr Gly Gly Tyr Lys              20 25 30 Gly Trp Asn Asn Gly Trp Lys Arg Gly Arg Trp Gly Arg Lys Tyr Tyr          35 40 45 Glu Phe Glu Phe      50 <210> 2 <211> 46 <212> PRT <213> Artificial Sequence <220> Foot protein type 3 (FP-3, Mytilus galloprovincialis: mgfp-3A) <400> 2 Ala Asp Tyr Tyr Gly Pro Lys Tyr Gly Pro Pro Arg Arg Tyr Gly Gly   1 5 10 15 Gly Asn Tyr Asn Arg Tyr Gly Arg Arg Tyr Gly Gly Tyr Lys Gly Trp              20 25 30 Asn Asn Gly Trp Lys Arg Gly Arg Trp Gly Arg Lys Tyr Tyr          35 40 45 <210> 3 <211> 50 <212> PRT <213> Artificial Sequence <220> Foot protein type 3 (FP-3, Mytilus edulis: mefp-3F) <400> 3 Ala Asp Tyr Tyr Gly Pro Asn Tyr Gly Pro Pro Arg Arg Tyr Gly Gly   1 5 10 15 Gly Asn Tyr Asn Arg Tyr Asn Gly Tyr Gly Gly Gly Arg Arg Tyr Gly              20 25 30 Gly Tyr Lys Gly Trp Asn Asn Gly Trp Asn Arg Gly Arg Arg Gly Lys          35 40 45 Tyr Trp      50 <210> 4 <211> 44 <212> PRT <213> Artificial Sequence <220> Foot protein type 3 (FP-3, Mytilus californianus) <400> 4 Gly Ala Tyr Lys Gly Pro Asn Tyr Asn Tyr Pro Trp Arg Tyr Gly Gly   1 5 10 15 Lys Tyr Asn Gly Tyr Lys Gly Tyr Pro Arg Gly Tyr Gly Trp Asn Lys              20 25 30 Gly Trp Asn Lys Gly Arg Trp Gly Arg Lys Tyr Tyr          35 40 <210> 5 <211> 75 <212> PRT <213> Artificial Sequence <220> Foot protein type 5 (FP-5, Mytilus edulis) <400> 5 Ser Ser Glu Glu Tyr Lys Gly Gly Tyr Tyr Pro Gly Asn Ala Tyr His   1 5 10 15 Tyr His Ser Gly Gly Ser Tyr His Gly Ser Gly Tyr His Gly Gly Tyr              20 25 30 Lys Gly Lys Tyr Tyr Gly Lys Ala Lys Lys Tyr Tyr Tyr Lys Tyr Lys          35 40 45 Asn Ser Gly Lys Tyr Lys Tyr Leu Lys Lys Ala Arg Lys Tyr His Arg      50 55 60 Lys Gly Tyr Lys Lys Tyr Tyr Gly Gly Ser Ser  65 70 75 <210> 6 <211> 76 <212> PRT <213> Artificial Sequence <220> &Lt; 223 > Foot protein 5 (FP-5, Mytilus edulis) <400> 6 Ser Ser Glu Glu Tyr Lys Gly Gly Tyr Tyr Pro Gly Asn Thr Tyr His   1 5 10 15 Tyr His Ser Gly Gly Ser Tyr His Gly Ser Gly Tyr His Gly Gly Tyr              20 25 30 Lys Gly Lys Tyr Tyr Gly Lys Ala Lys Lys Tyr Tyr Tyr Lys Tyr Lys          35 40 45 Asn Ser Gly Lys Tyr Lys Tyr Leu Lys Lys Ala Arg Lys Tyr His Arg      50 55 60 Lys Gly Tyr Lys Lys Tyr Tyr Gly Gly Gly Ser Ser  65 70 75 <210> 7 <211> 71 <212> PRT <213> Artificial Sequence <220> &Lt; 223 > Foot protein 5 (FP-5, Mytilus coruscus) <400> 7 Tyr Asp Asp Tyr Ser Asp Gly Tyr Tyr Pro Gly Ser Ala Tyr Asn Tyr   1 5 10 15 Pro Ser Gly Ser His Trp His Gly His Gly Tyr Lys Gly Lys Tyr Tyr              20 25 30 Gly Lys Gly Lys Lys Tyr Tyr Tyr Lys Phe Lys Arg Thr Gly Lys Tyr          35 40 45 Lys Tyr Leu Lys Lys Ala Arg Lys Tyr His Arg Lys Gly Tyr Lys Lys      50 55 60 His Tyr Gly Gly Ser Ser Ser  65 70 <210> 8 <211> 76 <212> PRT <213> Artificial Sequence <220> &Lt; 223 > Foot protein 5 (FP-5, Mytilus galloprovincialis) <400> 8 Ser Ser Glu Glu Tyr Lys Gly Gly Tyr Tyr Pro Gly Asn Thr Tyr His   1 5 10 15 Tyr His Ser Gly Gly Ser Tyr His Gly Ser Gly Tyr His Gly Gly Tyr              20 25 30 Lys Gly Lys Tyr Tyr Gly Lys Ala Lys Lys Tyr Tyr Tyr Lys Tyr Lys          35 40 45 Asn Ser Gly Lys Tyr Lys Tyr Leu Lys Lys Ala Arg Lys Tyr His Arg      50 55 60 Lys Gly Tyr Lys Lys Tyr Tyr Gly Gly Gly Ser Ser  65 70 75 <210> 9 <211> 99 <212> PRT <213> Artificial Sequence <220> &Lt; 223 > Foot protein 6 (FP-6, Mytilus edulis) <400> 9 Gly Gly Asn Tyr Arg Gly Tyr Cys Ser Asn Lys Gly Cys Arg Ser   1 5 10 15 Gly Tyr Ile Phe Tyr Asp Asn Arg Gly Phe Cys Lys Tyr Gly Ser Ser              20 25 30 Ser Tyr Lys Tyr Asp Cys Gly Asn Tyr Ala Gly Cys Cys Leu Pro Arg          35 40 45 Asn Pro Tyr Gly Arg Val Lys Tyr Tyr Cys Thr Lys Lys Tyr Ser Cys      50 55 60 Pro Asp Phe Tyr Tyr Tyr Asn Asn Lys Gly Tyr Tyr Tyr Tyr Asn  65 70 75 80 Asp Lys Asp Tyr Phe Asn Cys Gly Ser Tyr Asn Gly Cys Cys Leu Arg                  85 90 95 Ser Gly Tyr             <210> 10 <211> 56 <212> PRT <213> Semibalanus balanoides <400> 10 Met Arg Val Ile Leu Phe Ala Met Leu Ile Gly Gly Ser Leu Ala Cys   1 5 10 15 Gln Asn Arg Leu Glu Thr Leu Val Glu Glu Ala Thr Gly Asn Ala Gly              20 25 30 Asp Leu Ser Thr Asn Val His Glu Glu Cys Asn Ser Gln Val Gly Thr          35 40 45 Phe Asn Ala Val His Ala Pro Gln      50 55 <210> 11 <211> 10 <212> PRT <213> Artificial Sequence <220> Decapeptide (FP-1, Mytilus edulis) <400> 11 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys   1 5 10 <210> 12 <211> 20 <212> PRT <213> Artificial Sequence <220> 2 time repeated decapeptide (FP-1, Mytilus edulis) <400> 12 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro   1 5 10 15 Pro Thr Tyr Lys              20 <210> 13 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> 3 times repeated decapeptide (FP-1, Mytilus edulis) <400> 13 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro   1 5 10 15 Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys              20 25 30 <210> 14 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> 4 times repeated decapeptide (FP-1, Mytilus edulis) <400> 14 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro   1 5 10 15 Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys              20 25 30 Pro Ser Tyr Pro Pro Thr Tyr Lys          35 40 <210> 15 <211> 60 <212> PRT <213> Artificial Sequence <220> <223> 6 times repeated decapeptide (FP-1, Mytilus edulis) <400> 15 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro   1 5 10 15 Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys              20 25 30 Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr          35 40 45 Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys      50 55 60 <210> 16 <211> 6 <212> PRT <213> Artificial Sequence <220> <223> Spacer group <400> 16 Gly Gly Gly   1 5 <210> 17 <211> 6 <212> PRT <213> Artificial Sequence <220> <223> Spacer group <400> 17 Ser Gly Ser Gly Ser Gly   1 5 <210> 18 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Spacer group <400> 18 Ser Gly Ser Gly Ser Gly Ser Gly Ser Gly Ser Gly   1 5 10 <210> 19 <211> 24 <212> PRT <213> Artificial Sequence <220> <223> Spacer group <400> 19 Ser Gly Ser Gly Ser Gly Ser Gly Ser Gly Ser Gly Ser Gly Ser Gly   1 5 10 15 Ser Gly Ser Gly Ser Gly Ser Gly              20 <210> 20 <211> 39 <212> PRT <213> Artificial Sequence <220> Partial sequence of foot protein type 2 (FP-2, Mytilus          californianus) <400> 20 Glu Val His Ala Cys Lys Pro Asn Pro Cys Lys Asn Asn Gly Arg Cys   1 5 10 15 Tyr Pro Asp Gly Lys Thr Gly Tyr Lys Cys Lys Cys Val Gly Gly Tyr              20 25 30 Ser Gly Pro Thr Cys Ala Cys          35 <210> 21 <211> 120 <212> PRT <213> Artificial Sequence <220> <223> hybrid mussel adhesive protein (FP-151, MEFP-5 based) <400> 21 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro   1 5 10 15 Pro Thr Tyr Lys Ser Ser Glu Glu Tyr Lys Gly Gly Tyr Tyr Pro Gly              20 25 30 Asn Ala Tyr His Tyr His Ser Gly Gly Ser Tyr His Gly Ser Gly Tyr          35 40 45 His Gly Gly Tyr Lys Gly Lys Tyr Tyr Gly Lys Ala Lys Lys Tyr Tyr      50 55 60 Tyr Lys Tyr Lys Asn Ser Gly Lys Tyr Lys Tyr Leu Lys Lys Ala Arg  65 70 75 80 Lys Tyr His Arg Lys Gly Tyr Lys Tyr Tyr Gly Gly Ser Ser Ala Lys                  85 90 95 Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr             100 105 110 Tyr Lys Gly Gly Gly Gly Gly Gly Gly         115 120 <210> 22 <211> 166 <212> PRT <213> Artificial Sequence <220> <223> hybrid mussel adhesive protein (FP-151, MEFP-5 based) <400> 22 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro   1 5 10 15 Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys              20 25 30 Pro Ser Tyr Pro Pro Thr Tyr Lys Ser Ser Glu Glu Tyr Lys Gly Gly          35 40 45 Tyr Tyr Pro Gly Asn Ala Tyr His Tyr His Ser Gly Gly Ser Tyr His      50 55 60 Gly Ser Gly Tyr His Gly Gly Tyr Lys Gly Lys Tyr Tyr Gly Lys Ala  65 70 75 80 Lys Lys Tyr Tyr Tyr Lys Tyr Lys Tyr Leu                  85 90 95 Lys Lys Ala Arg Lys Tyr His Arg Lys Gly Tyr Lys Tyr Tyr Gly Gly             100 105 110 Ser Ser Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Ser Ser         115 120 125 Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys     130 135 140 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ser Gly Ser Gly Ser Gly 145 150 155 160 Ser Gly Ser Gly Ser Gly                 165 <210> 23 <211> 194 <212> PRT <213> Artificial Sequence <220> <223> hybrid mussel adhesive protein (FP-151, MEFP-5 based) <400> 23 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro   1 5 10 15 Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys              20 25 30 Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr          35 40 45 Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ser Ser Glu Glu      50 55 60 Tyr Lys Gly Gly Tyr Tyr Pro Gly Asn Ala Tyr His Tyr His Ser Gly  65 70 75 80 Gly Ser Tyr His Gly Ser Gly Tyr His Gly Gly Tyr Lys Gly Lys Tyr                  85 90 95 Tyr Gly Lys Ala Lys Lys Tyr Tyr Tyr Lys Tyr Lys Asn Ser Gly Lys             100 105 110 Tyr Lys Tyr Leu Lys Lys Ala Arg Lys Tyr His Arg Lys Gly Tyr Lys         115 120 125 Tyr Tyr Gly Gly Ser Ser Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys     130 135 140 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro 145 150 155 160 Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys                 165 170 175 Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr             180 185 190 Tyr Lys         <210> 24 <211> 196 <212> PRT <213> Artificial Sequence <220> <223> hybrid mussel adhesive protein (FP-151, MGFP-5 based) <400> 24 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro   1 5 10 15 Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys              20 25 30 Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr          35 40 45 Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ser Ser Glu Glu      50 55 60 Tyr Lys Gly Gly Tyr Tyr Pro Gly Asn Thr Tyr His Tyr His Ser Gly  65 70 75 80 Gly Ser Tyr His Gly Ser Gly Tyr His Gly Gly Tyr Lys Gly Lys Tyr                  85 90 95 Tyr Gly Lys Ala Lys Lys Tyr Tyr Tyr Lys Tyr Lys Asn Ser Gly Lys             100 105 110 Tyr Lys Tyr Leu Lys Lys Ala Arg Lys Tyr His Arg Lys Gly Tyr Lys         115 120 125 Lys Tyr Tyr Gly Gly Gly Ser Ser Ala Lys Pro Ser Tyr Pro Pro Thr     130 135 140 Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser 145 150 155 160 Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys                 165 170 175 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro             180 185 190 Pro Thr Tyr Lys         195 <210> 25 <211> 177 <212> PRT <213> Artificial Sequence <220> <223> hybrid mussel adhesive protein (FP-131) <400> 25 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro   1 5 10 15 Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys              20 25 30 Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr          35 40 45 Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Gly Cys Arg Ala      50 55 60 Asp Tyr Tyr Gly Pro Lys Tyr Gly Pro Pro Arg Arg Tyr Gly Gly Gly  65 70 75 80 Asn Tyr Asn Arg Tyr Gly Gly Ser Arg Arg Tyr Gly Gly Tyr Lys Gly                  85 90 95 Trp Asn Asn Gly Trp Lys Arg Gly Arg Trp Gly Arg Lys Tyr Tyr Glu             100 105 110 Phe Glu Phe Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro         115 120 125 Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr     130 135 140 Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr 145 150 155 160 Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Lys                 165 170 175 Leu     <210> 26 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (KLWKKWAKKWLKLWKA) <400> 26 Lys Leu Trp Lys Lys Trp Ala Lys Lys Trp Leu Lys Leu Trp Lys Ala   1 5 10 15 <210> 27 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (FALALKALKKL) <400> 27 Phe Ala Leu Ala Leu Lys Ala Leu Lys Lys Leu   1 5 10 <210> 28 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (ILRWPWWPWRRK) <400> 28 Ile Leu Arg Trp Pro Trp Trp Pro Trp Arg Arg Lys   1 5 10 <210> 29 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (AKRHHGYKRKFH) <400> 29 Ala Lys Arg His His Gly Tyr Lys Arg Lys Phe His   1 5 10 <210> 30 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (KWKLFKKIGAVLKVL) <400> 30 Lys Trp Lys Leu Phe Lys Lys Ile Gly Ala Val Leu Lys Val Leu   1 5 10 15 <210> 31 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (LVKLVAGIKKFLKWK) <400> 31 Leu Val Lys Leu Val Ala Gly Ile Lys Lys Phe Leu Lys Trp Lys   1 5 10 15 <210> 32 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (IWSILAPLGTTLVKLVAGIGQQKRK) <400> 32 Ile Trp Ser Ile Leu Ala Pro Leu Gly Thr Thr Leu Val Lys Leu Val   1 5 10 15 Ala Gly Ile Gly Gln Gln Lys Arg Lys              20 25 <210> 33 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (GIGAVLKVLTTGLPALISWI) <400> 33 Gly Ile Gly Ala Val Leu Lys Val Leu Thr Thr Gly Leu Pro Ala Leu   1 5 10 15 Ile Ser Trp Ile              20 <210> 34 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (SWLSKTAKKGAVLKVL) <400> 34 Ser Trp Leu Ser Lys Thr Ala Lys Lys Gly Ala Val Leu Lys Val Leu   1 5 10 15 <210> 35 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (KKLFKKILKYL) <400> 35 Lys Lys Leu Phe Lys Lys Ile Leu Lys Tyr Leu   1 5 10 <210> 36 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (GLKKLISWIKRAAQQG) <400> 36 Gly Leu Lys Lys Leu Ile Ser Trp Ile Lys Arg Ala Gln Gln Gly   1 5 10 15 <210> 37 <211> 38 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide          (WLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATAR) <400> 37 Trp Leu Lys Lys Ile Gly Lys Lys Ile Glu Arg Val Gly Gln His Thr   1 5 10 15 Arg Asp Ala Thr Ile Gln Gly Leu Gly Ile Ala Gln Gln Ala Ala Asn              20 25 30 Val Ala Ala Thr Ala Arg          35 <210> 38 <211> 3 <212> PRT <213> Artificial Sequence <220> <223> Anti-oxidant peptide (ACQ) <400> 38 Ala Cys Gln   One <210> 39 <211> 6 <212> PRT <213> Artificial Sequence <220> <223> Anti-oxidant peptide (PHCKRM) <400> 39 Pro His Cys Lys Arg Met   1 5 <210> 40 <211> 7 <212> PRT <213> Artificial Sequence <220> The anti-viral peptide (RRWWCRC) <400> 40 Arg Arg Trp Trp Cys Arg Cys   1 5 <210> 41 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Anti-cancer peptide (THRPPMWSPVWP) <400> 41 Thr His Arg Pro Pro Met Trp Ser Pro Val Trp Pro   1 5 10 <210> 42 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Anti-cancer peptide (KLLLKLLKKLLKLLKKK) <400> 42 Lys Leu Leu Leu Lys Leu Leu Lys Lys Leu Leu Lys Leu Leu Lys Lys   1 5 10 15 Lys     <210> 43 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Anti-cancer peptide (FLKLLKKLAAKLF) <400> 43 Phe Leu Lys Leu Leu Lys Lys Leu   1 5 10 <210> 44 <211> 20 <212> PRT <213> Artificial Sequence <220> Anti-cancer peptide (RLLRRLLRRLLRRLLRRLLR) <400> 44 Arg Leu Leu Arg Arg Leu Leu Arg Arg Leu Leu Arg Arg Leu Leu Arg   1 5 10 15 Arg Leu Leu Arg              20 <210> 45 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Anti-cancer peptide (KLAKLAKKLAKLAK) <400> 45 Lys Leu Ala Lys Leu Ala Lys Lys Leu Ala Lys   1 5 10

Claims (18)

And an adhesive protein to which a functional peptide is added at an amine terminal or a carbon terminal. The method according to claim 1,
Wherein the adhesive protein is selected from the group consisting of mussel-derived adhesive proteins, barnacle-derived adhesive proteins, and combinations thereof. The method of claim 2,
Wherein an acrylate group or a urethane group is introduced into the molecular skeleton of the adhesive protein. The method according to claim 1,
Wherein the adhesive protein is an adhesive protein derived from a mussel consisting of an amino acid sequence selected from the group consisting of SEQ ID NOS: 21 to 25. The method of claim 2,
Wherein the adhesive protein derived from barnacle is composed of the amino acid sequence of SEQ ID NO. The method of claim 2,
Wherein the adhesive protein is a mixture of a mussel-derived adhesive protein and a barnacle-derived adhesive protein at a mixing ratio (wt / wt) of 50:50. The method according to claim 1,
Wherein the functional peptide further comprises a functional peptide having a function selected from the group consisting of antimicrobial, antiviral, antioxidant, anti-ultraviolet, antistatic and anticancer properties. The method of claim 7,
Wherein the antimicrobial functional peptide has a function of acting on the cell membrane to destroy the cell membrane. The method of claim 7,
The antimicrobial functional peptide may be selected from the group consisting of KLWKKWAKKWLKLWKA (SEQ ID NO: 26), FALALKALKKL (SEQ ID NO: 27), ILRWPWWPWRRK (SEQ ID NO: 28), AKRHHGYKRKFH (SEQ ID NO: 29), KWKLFKKIGAVLKVL (SEQ ID NO: 30), LVKLVAGIKKLKWK A coating composition comprising an amino acid sequence selected from the group consisting of GIGAVLKVLTTGLPALISWI (SEQ ID NO: 33), SWLSKTAKKGAVLKVL (SEQ ID NO: 34), KKLFKKILKYL (SEQ ID NO: 35), GLKKLISWIKRAAQQG (SEQ ID NO: 36) and WLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATAR . The method of claim 7,
Wherein said antioxidant or anti-UV functional peptide comprises an amino acid sequence of ACQ (SEQ ID NO: 38) or PHCKRM (SEQ ID NO: 39). The method according to claim 1,
A coating composition, further comprising a hydrophilic resin. The method of claim 11,
Wherein the hydrophilic resin is selected from the group consisting of hydrophilic acrylates, urethanes, polyesters, and combinations thereof. The method of claim 11,
Wherein the hydrophilic resin is photo-curable by a photo-curing initiator. 14. The method of claim 13,
Wherein the photocurable initiator is benzoyl peroxide. A functionalized surface coated with the coating composition of any one of claims 1 to 14. 16. The method of claim 15,
Wherein the functional surface comprises a material selected from the group consisting of synthetic materials, biomaterials, metals, non-metals, glass, and combinations thereof. 16. The method of claim 15,
Wherein the functional surface is selected from the group consisting of a flat surface, a concave surface, a porous surface, a convex surface, and a spherical surface. 18. The method of claim 16,
Wherein the material is a textile fabric.

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