WO2024258965A2 - Synthetic antifreeze glycoproteins with ice-binding activity - Google Patents

Abstract

The present disclosure is concerned with peptides comprising alanine residues and glycosylated residues (e.g., glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues) in a particular ratio (e.g, from about 3:2 to about 4:1), wherein the peptide has a minumum chain length, such as, for example a chain length of at least 30 amino acid residues. The disclosed peptides beneficially inhibit ice crystal formation, and, therefore, offer utility in a wide range of applications, including, but not limited to biomedical cryopreservation, food technology, agriculture, cosmetics, and building materials. Thus, the disclosed peptides can be formulated into a composition (e.g, a cryoprotectant composition, an agricultural formulation, a cosmetic composition) or a food product, or, alternatively, can be attached or coated onto a surface for use in structural applications. This abstract is intended as a scanning tool for purposes of searching in the particular art and is not intended to be limiting of the present invention.

Description

SYNTHETIC ANTIFREEZE GLYCOPROTEINS WITH ICE-BINDING ACTIVITY CROSS-REFERENCE TO RELATED APPLICATIONS [0001] This Application claims the benefit of U.S. Application No.63/507,770, filed on June 13, 2023, U.S. Application No.63/613,382, filed on December 21, 2023, and U.S. Application No.63/650,185, filed on May 21, 2024, the contents of which are incorporated herein by reference in their entireties. STATEMENT REGARDING FEDERALLY FUNDED RESEARCH [0001] This invention was made with government support under R35 GM147262 awarded by the National Institutes of Health, and 1848054 awarded by the National Science Foundation. The government has certain rights in the invention. BACKGROUND [0002] Extremophile organisms in cold climates produce specialized antifreeze proteins to defend their tissues against freezing damage. These proteins depress the freezing point of plasma and water, and alter ice crystal shape and size (Brockbank, K.G.M.; et al., (2011) In Vitro Cellular and Developmental Biology - Animal.47210–217). The latter property prevents growth of large crystals that would otherwise cause mechanical damage to animal tissues. There is also limited evidence of cell membrane interactions that could stabilize the bilayer and prevent leakage during thermal transitions (Hays, L. M.; et al., (1996) Antifreeze Glycoproteins Inhibit Leakage from Liposomes during Thermotropic Phase Transitions;; Vol. 93; Hays, L. M.; et al., (1997) News Physiol. Sci., 12(4), 189–194; Wu, Y.; et al., (2001) Comp. Biochem. Physiol. - B Biochem. Mol. Biol.128(2), 265–273). [0003] Since their discovery, antifreeze proteins have been of great interest for application as cryoprotectants in food technology, agriculture, fisheries, coatings, and in the petroleum industry (Voets, I. K.; (2017) Soft Matter 13(28), 4808–4823). Antifreeze proteins have even come to the consumer market as ice cream additives that improve texture (Meldolesi, A. GM.; (2009) Nat. Biotechnol.27(8), 682–682). A particularly impactful potential application is in biomedical cryopreservation. Cryopreservation and banking of cells and tissues valuable for regenerative medicine and research purposes is essential to prevent growth of bacteria and to halt cellular metabolism (Cao, E.; et al., (2003) Biotechnol. Bioeng.82(6), 684–690). However, freeze-thaw procedures are associated with loss of viability and changes in cellular morphology and function (Jang, T. H. (2017) Integr. Med. Res.6(1), 12–18; Fahy, G. M.; et al., (1990) Cryobiology 27(5), 492–510; Bojic, S.; et al., (2021) BMC Biology.1956). For decades, there has been great interest in application of antifreeze proteins to improve post- thaw viability of cells, tissues, and even whole organs. [0004] Five classes of structurally diverse antifreeze proteins have been identified to date. A subgroup of these proteins bears pendent sugar residues and are therefore termed antifreeze glycoproteins (AFGPs). AFGPs are the most potent antifreeze molecules ever discovered (Budke, C.; et al., (2014) Cryst. Growth Des.14(9) 4285–4294; Knight, C. A.; et al., (1984) Nature 308(5956), 295–296; Harding, M. M.; et al., (2003) Eur. J. Biochem.270(7) 1381– 1392). The proteins are a fascinating and rare example of convergent evolution (Chen, L.; et al., (1997) Proc. Natl. Acad. Sci. U. S. A.94(8) 3817-3822). AFGPs were first reported and investigated in a series of studies from 1957–1970 where they were identified as the major serum protein of both Antarctic notothenioids and Arctic cod (DeVries, A. L.; et al., (1970) J. Biol. Chem.245 (11), 2901–2908; DeVries, A. L.; et al., (1969) Science (80-. ) 163(3871) 1073–1075; Scholander, P. F.; et al., (1957) J. Cell. Comp. Physiol., 49(1), 5–24; GORDON, M. S.; et al., (1962) Biol. Bull.122 (1), 52–62). Later, AFGPs were identified in two species of mountain ticks (Harding, M. M.; et al., (2003) Eur. J. Biochem.270(7) 1381–1392; Neelakanta, G.; et al., (2010) J. Clin. Invest.120(9), 3179–3190). [0005] AFGPs are relatively simple in structure, consisting of a highly conserved Ala-Ala- Thr repeat. The Thr residue is α-glycosylated with the disaccharide βGal(1→3)αGalNAc (FIG.1A)(DeVries, A. L.; et al., (1969) Science (80-..163(3871) 1073–1075; Graham, L. A.; Davies, P. L.; (2005) Science (80-. ).310 (5747), 461–461; Urbańczyk, M.; et al., (2017) Amino Acids, 49 (2), 209–222). Isoforms with molecular weights (MWs) ranging from 2.6– 33.7 kDa, classified as AFGP8–AFGP1, are encoded within polyprotein genes (Knight, C. A.; et al., (1984) Nature 308(5956), 295–296; Chen, L.; et al., (1997) Proc. Natl. Acad. Sci. U. S. A.94(8) 3817-3822). AFGPs adopt an extended helical conformation (FIG.1) as evidenced by temperature-varied circular dichroism (CD)(Raymond, J. A.; et al., (1977) Biopolymers 16(11), 2575–2578; Tseng, P. H.; J et al., (2001) Chem. - A Eur. J. (3), 585– 590; Nagel, L.; et al., (2011) Amino Acids 41 (3), 719–732), light scattering (Ahmed, A. I.; et al., (1975) J. Biol. Chem.250(9), 3344–3347), Raman (Tomimatsu, Y.; et al., (1976) J. Biol. Chem.251(8), 2290–2298), and nuclear magnetic resonance (NMR) studies (Franks, F.; Morris, E. R. (1978) Biochim. Biophys. Acta - Gen. Subj.540 (2), 346–356; Mimura, Y.; et al., (1992) Int. J. Biol. Macromol.14(5), 242–248). Compared to the well-known protein alpha helix, which is right-handed and has 3.6 residues per turn, AFGPs take on a more relaxed left-handed form with 3 residues per turn (Urbańczyk, M.; et al., (2017) Amino Acids, 49 (2), 209–222; Adzhubei, A. A.; et al., (2013) J. Mol. Biol.425 (12), 2100–2132). This structure is known as a polyproline type II (PPII) helix since it is also observed in Pro-rich proteins such as collagen and mucins(Lopes, J. L. S.; et al., (2014) Protein Sci.23(12), 1765– 1772; Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461). [0006] AFGPs’ most well-established antifreeze properties are ice recrystallization inhibition (IRI) and thermal hysteresis (TH). IRI properties cause a reduction in ice crystal mean grain size (MGS) as compared to untreated ice. I.e., the AFGPs prevent formation of large crystals (Berger, T.; et al., (2019) J. Am. Chem. Soc.141(48), 19144–19150; Tsuda, S.; et al., (2020) Biomolecules 10(3) 423). The precise molecular mechanisms of action are still debated, but presumably, the proteins bind to ice surfaces (Berger, T.; et al., (2019) J. Am. Chem. Soc.141(48), 19144–19150; Tsuda, S.; et al., (2020) Biomolecules 10(3), 423; Pandey, P.; et al., (2019) Phys. Chem. Chem. Phys.21(7) 3903–3917; Mochizuki, K.; et al., (2018) J. Am. Chem. Soc.140(14), 4803–4811; Meister, K.; et al., (2018) J. Am. Chem. Soc.140 (30), 9365–9368). TH properties result in a gap between solution freezing and melting points (DeVries, A. L.; et al., (1970) J. Biol. Chem. 245 (11), 2901–2908; Urbańczyk, M.; et al., (2017) Amino Acids, 49 (2), 209–222; DeVries, A. L. (1971) Science (80-. ).172 (3988) 1152–1155). AFGPs also induce a non-colligative freezing point depression reaching -1.8˚C at < 10 μM with observable effects at concentrations 300–500x lower than dissolved sugars (Carvajal-Rondanelli, et al., (2011) Journal of the Science of Food and Agriculture 91(14) 2507-2510) and 100,000x that of NaCl (Bar Dolev, M.; et al., (2016) Annu. Rev. Biochem.85 515–542). While TH is important for aquatic creatures in icy oceans, materials with IRI activity are of great interest for cryopreservation in biomedical, agricultural, and food industry settings (Bar Dolev, M.; et al., (2016) Annu. Rev. Biochem.85515–542; Eskandari, A.; et al., (2020) Biomolecules 10 (12) 1–18). Membrane binding activity is also proposed as a mechanism of action but further studies are needed (Hays, L. M.; et al., (1996) Proc. Natl. Acad. Sci. U. S. A.93(13)6835-6840; Hays, L. M.; et al., (1997) News Physiol. Sci., 12(4), 189–194; Wu, Y.; et al., (2001) Comp. Biochem. Physiol. - B Biochem. Mol. Biol.128(2), 265–273; Sun, Y.; et al., (2022) Biomacromolecules 23 (3), 1214–1220). [0007] There are no current commercial sources of AFGPs. Isolation of the proteins from polar fish blood is expensive and yields heterogeneous mixtures of isoforms of varied molecular weight. Fractionation processes performed in research lab settings have revealed high MW AFGPs have much higher antifreeze activity than low molecular weight AFGPs, but the purification methods are laborious and impractical for routine use (Wu, Y.; et al., (2001) Comp. Biochem. Physiol. - B Biochem. Mol. Biol.128(2), 265–273; Knight, C. A.; et al., (1984) Nature 308(5956), 295–296). Overall, animal-sourced AFGPs cannot supply commercial cryopreservation needs nor even limited mechanism of action studies. Short peptides have been prepared by solid-phase synthesis or step-growth polymerizations but these techniques are also laborious, low yielding, and only relevant to low-activity, low- molecular weight AFGPs (Voets, I. K., 2017 Soft Matter 13 (28), 4808–4823; Urbańczyk, M.; et al., (2017) Amino Acids, 49 (2), 209–222; Tseng, P. H.; J et al., (2001) Chem. - A Eur. J. (3), 585–590; Eniade, A.; Ben, R. N. (2001) Biomacromolecules 2(2) 557–561; Graham, B.; et al., (2017) Angew. Chemie Int. Ed.56(50) 15941–15944; Ben, R. N.; et al., (1999) Org. Lett.1(11) 1759–1762; Liu, S.; Ben, R. N. (2005) Org. Lett.7(12) 2385–2388; Tsuda, T.; Nishimura, S. I. (1996) Chem. Commun. No.24, 2779–2780; Huang, M. L.; et al., (2012) Proc. Natl. Acad. Sci. U. S. A.109 (49), 19922–19927; Filira, F.; et al., (1990) Int. J. Biol. Macromol.12(1) 41–49; Tachibana, Y.; et al., (2004) Angew. Chemie - Int. Ed.43(7) 856– 862; Tachibana, Y.; et al., (2002) Tetrahedron 58(51) 10213–10224; Wilkinson, B. L.; et al., (2012) Angew. Chemie - Int. Ed.51(15) 3606–3610; Eniade, A.; et al., (2001) Bioconjug. Chem.12(5), 817–823). Additionally, many of these peptides utilized non-native glycan linkages and chemical groups that could affect bioactivity or biocompatibility. [0008] A variety of AFGP-mimetic polymers have been investigated. The simplest mimics capture AFGPs’ high density of hydroxyl groups while more recent efforts have focused on the PPII structure. Polyhydroxylated structures include poly(vinyl alcohol) (PVA) and hydroxyethyl starch (HES). These molecules have a high capacity for hydrogen bonding to water which can result in a thermally inert glassy ice state during cooling (Stolzing, A.; N et al., (2012) Transfus. Apher. Sci.46(2) 137–147). PVA is also proposed to bind to ice (Naullage, P. M.; Molinero, V. (2020) J. Am. Chem. Soc.142 (9), 4356–4366). PVA is reportedly orders of magnitude less active than even the least active low MW AFGPs, which might be explained by the inherent backbone flexibility as compared to the rigid PPII structure of AFGPs (Naullage, P. M.; Molinero, V. (2020) J. Am. Chem. Soc.142 (9), 4356– 4366; Naullage, P. M.; et al., (2020) J. Chem. Phys..153, 174106; Hudait, A.; et al., (2019) J. Am. Chem. Soc.141(19) 7887–7898; Deller, R. C.; et al., (2016) Biomater. Sci.4(7) 1079– 1084; Deller, R. C.; et al., (2014) Nat Commun 53244; Tekin, K.; Daşkın, A. (2019) Cryobiology 8960–67; Six, K. R.; et al., (2019) Transfusion 59(9) 3029–3031). Nonetheless, PVA has shown promise in cryopreservation application in combination with traditional cryoprotectants (Deller, R. C.; et al., (2016) Biomater. Sci.4(7) 1079–1084; Deller, R. C.; et al., (2014) Nat Commun 53244; Tekin, K.; Daşkın, A. (2019) Cryobiology 8960–67; Six, K. R.; et al., (2019) Transfusion 59(9) 3029–3031; Fayter, A. E. R.; et al., (2020) Eur. Polym. J. 140, 110036. https://doi.org/10.1016/J.EURPOLYMJ.2020.110036). Other investigated mimics include (glyco)polymers based on hydrocarbon backbones (Graham, B.; et al., (2018) J. Am. Chem. Soc.140(17) 5682–5685; Mitchell, D. E.; et al., (2015) Chem. Commun.51, 12977-12980 and supplementary information; Gibson, M. I.; et al., (2009) Biomacromolecules 10(2) 328–333), peptoids (Huang, M. L.; et al., (2012) Proc. Natl. Acad. Sci. U. S. A.109 (49), 19922–19927), and surfactant-sugar conjugates (Acker, J. P.; et al., (2015) Transfus. Med. Rev.29(4) 277). However, these cannot adopt the PPII structure, required non-native linkages, and most have shown little to no IRI activity [0009] Despite efforts to develop AFGP mimics, none have achieved comparable potency to AFGPs. Therefore, there remains a need for bioinspired synthetic polymers that effectively inhibit the growth of ice crystals. SUMMARY [0010] In accordance with the purpose(s) of the invention, as embodied and broadly described herein, the invention, in one aspect, relates to peptides comprising alanine residues and glycosylated residues (e.g., glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues) in a particular ratio (e.g., from about 3:2 to about 4:1). As detailed herein, the peptide has a particular chain length, such as, for example a chain length of at least 30 amino acid residues. The disclosed peptides beneficially inhibit ice crystal formation, and, therefore, offer utility in a wide range of applications, including, but not limited to biomedical cryopreservation, food technology, agriculture, cosmetics, and building materials. Thus, the disclosed peptides can be formulated into a composition (e.g., a cryoprotectant composition, an agricultural formulation, a cosmetic composition) or a food product, or, alternatively, can be attached to a surface for use in structural applications. [0011] Thus, disclosed are peptides comprising a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, and wherein the peptide has a chain length of at least 30 amino acid residues. [0012] Also disclosed are cryoprotectant compositions comprising an effective amount of a disclosed peptide and one or more selected from: (a) a non-antifreeze protein; (b) a microbe; (c) a cell component; and (d) a cell. [0013] Also disclosed are food products comprising a disclosed peptide. [0014] Also disclosed are agriculture compositions comprising a disclosed peptide. [0015] Also disclosed are solid or semi-solid supports comprising a surface covalently attached to a residue of a disclosed peptide. [0016] Also disclosed are cosmetic compositions comprising a disclosed peptide. [0017] Also disclosed are methods of inhibiting ice crystal formation in a sample, the method comprising contacting the sample with an effective amount of a disclosed peptide. [0018] Also disclosed are kits comprising a disclosed peptide and one or more selected from: (a) a biological material; (b) a food product; (c) an agricultural product; (d) a solid or semi-solid support; and (e) a cosmetic. [0019] While aspects of the present invention can be described and claimed in a particular statutory class, such as the system statutory class, this is for convenience only and one of skill in the art will understand that each aspect of the present invention can be described and claimed in any statutory class. Unless otherwise expressly stated, it is in no way intended that any method or aspect set forth herein be construed as requiring that its steps be performed in a specific order. Accordingly, where a method claim does not specifically state in the claims or descriptions that the steps are to be limited to a specific order, it is no way intended that an order be inferred, in any respect. This holds for any possible non-express basis for interpretation, including matters of logic with respect to arrangement of steps or operational flow, plain meaning derived from grammatical organization or punctuation, or the number or type of aspects described in the specification. BRIEF DESCRIPTION OF THE FIGURES [0020] The accompanying figures, which are incorporated in and constitute a part of this specification, illustrate several aspects and together with the description serve to explain the principles of the invention. [0021] FIG.1A-F show a representative chemical structure and cartoon representation of a native AFGP and schematic for preparation of sAFGPs. [0022] FIG.2A-D show representative characterization of sAFGP molar masses and conformations. [0023] FIG.3A-D show representative ice binding properties of sAFGPs with varying amino acid compositions. [0024] FIG.4A-C show representative ice binding data for sAFGPs composed of the native 1:2 glycoT:A ratio and with varied chain lengths and varied glycan structures. [0025] FIG.5A-C show representative cellular internalization, biodegradation, and cytocompatibility of sAFGPs with the native 1:2 glycoT:A composition and bearing the native disaccharide. [0026] FIG.6 shows a representative cartoon and data of cryopreservation of hRBCs in sAFGP supplemented HES solutions or PBS alone. [0027] FIG.7 shows representative infrared spectroscopy data of complete monomer consumption. [0028] FIG.8A-C show representative infrared spectroscopy data of prepared N- carboxyanhydrides (NCA). [0029] FIG.9A-G show representative infrared spectroscopy data of prepared sAFGPs. [0030] FIG.10 shows a representative GPC/MALS trace for ( βGal ^GalNAcT_0.33-s-A_0.66)_78. [0031] FIG.11 shows a representative CD spectra of ( βGal ^GalNAcT0.33-s-A0.66)57 in PBS versus ultrapure water water at 25 °C. [0032] FIG.12 shows a representative CD spectra of ( βGal ^GalNAcT_0.33-s-A_0.66)₉₃ at varied temperatures in ultrapure water. [0033] [0034] FIG.13 shows a representative CD spectra of ( βGalTy-s-Ax)n at various amino acid concentrations. [0035] FIG.14 shows a representative CD spectra of ( βGalNAcT_y-s-A_x)_n at various amino acid concentrations_. [0036] FIG.15 shows representative images of ice shaping of ( βGal ^GalNAcT_0.33-s-A_0.66)_n DP = 28, 57, 170 at 0.5 mg/mL. [0037] FIG.16 shows representative images of ice shaping of (glycoT_0.33-s-A_0.66)₉₃ at 0.5 mg/mL. [0038] FIG.17 shows representative quantified IRI data as % MGS relative to PBS for ( βGal ^GalNAcT0.33-s-A0.66)^170, PVA, and DMSO. [0039] FIG.18 shows representative images of internalization AF594-( ^Gal βGalNAcT0.33- s-A0.66)57 in Raji cells. [0040] FIG.19 shows a representative image of SDS-Page used to determine the concentration of sAFGP needed for protease digestion studies. [0041] FIG.20 shows representative data demonstrating cryopreservation of HEK293 cells with varying treatments_. [0042] FIG.21 shows representative data demonstrating cryopreservation of hRBC cells with HES concentrations_. [0043] FIG.22 shows representative images of cooling splat assays and IRI activity for ( ^Gal βGalNAcT_0.33-s-A_0.66)₂₈. [0044] FIG.23 shows representative images of cooling splat assays and IRI activity for ( ^Gal βGalNAcT0.33-s-A0.66)57. [0045] FIG.24 shows representative images of cooling splat assays and IRI activity for ( ^Gal βGalNAcT0.33-s-A0.66)170. [0046] FIG.25 shows representative images of cooling splat assays and IRI activity for ( βGal ^GalNAcT_0.5-s-A_0.5)₅₂. [0047] FIG.26 shows representative images of cooling splat assays and IRI activity for ( βGal ^GalNAcT_0.66-s-A_0.33)₄₆. [0048] FIG.27 shows representative images of cooling splat assays and IRI activity for ( ^GalNAcT0.33-s-A0.66)99. [0049] FIG.28 shows representative images of cooling splat assays and IRI activity for ^GalT0.33-s-A0.66)93. [0050] FIG.29 shows representative images of cooling splat assays and IRI activity for ( βGalNAcT_0.33-s-A_0.66)₉₃. [0051] FIG.30 shows representative images of cooling splat assays and IRI activity for ( βGalT_0.33-s-A_0.66)₉₃. [0052] FIG.31 shows representative images of cooling splat assays and IRI activity for 28mer, 57mer and 170mer of ( βGal ^GalNAcT0.33-s-A0.66)n at 70.7 µM. [0053] FIG.32 shows representative images of cooling splat assays and IRI activity for x:y ratios of 1:2, 1:1, and 2:1 ( βGal ^GalNAcTx-s-Ay)n at 70.7 µM. [0054] FIG.33 shows representative images of cooling splat assays and IRI activity for sugar residues αGal, αGalNAc, βGal, and βGalNAc glycoT_0.33-s-A_0.66)₉₃ at 70.7 µM. [0055] FIG.34 shows representative images of cooling splat assays and IRI activity for 28mer, 57mer and 170mer of ( βGal ^GalNAcT_0.33-s-A_0.66)_n at 0.5 mg/mL. [0056] FIG.35 shows representative images of cooling splat assays and IRI activity for sugar residues αGal, αGalNAc, βGal, and βGalNAc glycoT0.33-s-A0.66)93 at 0.5 mg/mL. [0057] FIG.36 shows representative images of cooling splat assays and IRI activity for controls with PBS, 5% DMSO, 10% DMSO, 50 µM PVA and 100 µM PVA. [0058] FIG.37 shows representative images of cooling splat assays and IRI activity for (GalNAcSer_0.2-s-Ala_0.8)₁₅₀ at 0.5 mg/mL in PBS as compared to PBS alone. [0059] FIG.38 shows a representative ¹H NMR spectra of ( βGal ^GalNAcT0.33-s-A0.66)n. [0060] FIG.39 shows a representative ¹H NMR spectra of ( ^GalNAcT0.33-s-A0.66)93. [0061] FIG.40 shows a representative ¹H NMR spectra of ( βGalNAcT_0.33-s-A_0.66)₉₃. [0062] FIG.41 shows a representative ¹H NMR spectra of ( ^GalT_0.33-s-A_0.66)₉₃. [0063] FIG.42 shows a representative ¹H NMR spectra of ( βGalT0.33-s-A0.66)93. [0064] FIG.43 shows cooling splat apparatus. [0065] Additional advantages of the invention will be set forth in part in the description which follows, and in part will be obvious from the description, or can be learned by practice of the invention. The advantages of the invention will be realized and attained by means of the elements and combinations particularly pointed out in the appended claims. It is to be understood that both the foregoing general description and the following detailed description are exemplary and explanatory only and are not restrictive of the invention, as claimed. DETAILED DESCRIPTION [0066] The present invention can be understood more readily by reference to the following detailed description of the invention and the Examples included therein. [0067] Before the present compounds, compositions, articles, systems, devices, and/or methods are disclosed and described, it is to be understood that they are not limited to specific synthetic methods unless otherwise specified, or to particular reagents unless otherwise specified, as such may, of course, vary. It is also to be understood that the terminology used herein is for the purpose of describing particular aspects only and is not intended to be limiting. Although any methods and materials similar or equivalent to those described herein can be used in the practice or testing of the present invention, example methods and materials are now described. [0068] While aspects of the present invention can be described and claimed in a particular statutory class, such as the system statutory class, this is for convenience only and one of skill in the art will understand that each aspect of the present invention can be described and claimed in any statutory class. Unless otherwise expressly stated, it is in no way intended that any method or aspect set forth herein be construed as requiring that its steps be performed in a specific order. Accordingly, where a method claim does not specifically state in the claims or descriptions that the steps are to be limited to a specific order, it is no way intended that an order be inferred, in any respect. This holds for any possible non-express basis for interpretation, including matters of logic with respect to arrangement of steps or operational flow, plain meaning derived from grammatical organization or punctuation, or the number or type of aspects described in the specification. [0069] Throughout this application, various publications are referenced. The disclosures of these publications in their entireties are hereby incorporated by reference into this application in order to more fully describe the state of the art to which this pertains. The references disclosed are also individually and specifically incorporated by reference herein for the material contained in them that is discussed in the sentence in which the reference is relied upon. Nothing herein is to be construed as an admission that the present invention is not entitled to antedate such publication by virtue of prior invention. Further, the dates of publication provided herein may be different from the actual publication dates, which can require independent confirmation. A. DEFINITIONS [0070] As used in the specification and the appended claims, the singular forms “a,” “an” and “the” include plural referent.s unless the context clearly dictates otherwise. Thus, for example, reference to “a peptide,” “a glycosyl moiety,” or “a residue” includes mixtures of two or more such peptides, glycosyl moieties, or residues, and the like. [0071] As used in the specification and in the claims, the term “comprising” can include the aspects “consisting of” and “consisting essentially of.” [0072] Ranges can be expressed herein as from “about” one particular value, and/or to “about” another particular value. When such a range is expressed, another aspect includes from the one particular value and/or to the other particular value. Similarly, when values are expressed as approximations, by use of the antecedent “about,” it will be understood that the particular value forms another aspect. It will be further understood that the endpoints of each of the ranges are significant both in relation to the other endpoint, and independently of the other endpoint. It is also understood that there are a number of values disclosed herein, and that each value is also herein disclosed as “about” that particular value in addition to the value itself. For example, if the value “10” is disclosed, then “about 10” is also disclosed. It is also understood that each unit between two particular units are also disclosed. For example, if 10 and 15 are disclosed, then 11, 12, 13, and 14 are also disclosed. [0073] As used herein, the terms “about” and “at or about” mean that the amount or value in question can be the value designated some other value approximately or about the same. It is generally understood, as used herein, that it is the nominal value indicated ±10% variation unless otherwise indicated or inferred. The term is intended to convey that similar values promote equivalent results or effects recited in the claims. That is, it is understood that amounts, sizes, formulations, parameters, and other quantities and characteristics are not and need not be exact, but can be approximate and/or larger or smaller, as desired, reflecting tolerances, conversion factors, rounding off, measurement error and the like, and other factors known to those of skill in the art. In general, an amount, size, formulation, parameter or other quantity or characteristic is “about” or “approximate” whether or not expressly stated to be such. It is understood that where “about” is used before a quantitative value, the parameter also includes the specific quantitative value itself, unless specifically stated otherwise. [0074] References in the specification and concluding claims to parts by weight of a particular element or component in a composition denotes the weight relationship between the element or component and any other elements or components in the composition or article for which a part by weight is expressed. Thus, in a composition containing 2 parts by weight of component X and 5 parts by weight component Y, X and Y are present at a weight ratio of 2:5, and are present in such ratio regardless of whether additional components are contained in the composition. [0075] A weight percent (wt. %) of a component, unless specifically stated to the contrary, is based on the total weight of the formulation or composition in which the component is included. [0076] As used herein, “thermal hysteresis” or “TH” is intended to refer to the difference between the temperature at which ice crystals grow (the freezing temperature, Tf) and the temperature at which they melt (the melting point, T_m). [0077] As used herein, the terms “optional” or “optionally” means that the subsequently described event or circumstance can or cannot occur, and that the description includes instances where said event or circumstance occurs and instances where it does not. [0078] As used herein, the terms “effective amount” and “amount effective” refer to an amount that is sufficient to achieve the desired result. For example, in the case of a cryoprotectant composition, the “effective amount” can refer to the amount of the peptide that must be present in the composition in order to minimize, prevent, or otherwise delay ice crystal formation. Thus, in various aspects, the effective amount is the amount of the peptide required to reduce crystal mean grain size (MGS) by at least about 10%, about 20%, about 25%, about 30%, about 40%, about 50%, about 60%, about 65%, about 70%, about 75%, or more than about 75%. In various further aspects, the effective amount is the amount of the peptide required such that the majority of the ice crystals present in the sample are hexagonal, square, and/or amorphous crystals (as opposed to spicular crystals). In various further aspects, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, or more than 90% of the ice crystals present in the sample are hexagonal, square, and/or amorphous crystals. [0079] As used herein, “kit” means a collection of at least two components constituting the kit. Together, the components constitute a functional unit for a given purpose. Individual member components may be physically packaged together or separately. For example, a kit comprising an instruction for using the kit may or may not physically include the instruction with other individual member components. Instead, the instruction can be supplied as a separate member component, either in a paper form or an electronic form which may be supplied on computer readable memory device or downloaded from an internet website, or as recorded presentation. [0080] As used herein, “instruction(s)” means documents describing relevant materials or methodologies pertaining to a kit. These materials may include any combination of the following: background information, list of components and their availability information (purchase information, etc.), brief or detailed protocols for using the kit, trouble-shooting, references, technical support, and any other related documents. Instructions can be supplied with the kit or as a separate member component, either as a paper form or an electronic form, which may be supplied on computer readable memory device or downloaded from an internet website, or as recorded presentation. Instructions can comprise one or multiple documents, and are meant to include future updates. [0081] As used herein, the term “derivative” refers to a peptide having a structure derived from the structure of a parent peptide (e.g., a peptide disclosed herein) and whose structure is sufficiently similar to those disclosed herein and based upon that similarity, would be expected by one skilled in the art to exhibit the same or similar activities and utilities as the claimed peptides, or to induce, as a precursor, the same or similar activities and utilities as the claimed peptides. Exemplary derivatives include salts, esters, amides, salts of esters or amides, and N-oxides of a parent peptide. [0082] As used herein, the term “substituted” is contemplated to include all permissible substituents of organic compounds. In a broad aspect, the permissible substituents include acyclic and cyclic, branched and unbranched, carbocyclic and heterocyclic, and aromatic and nonaromatic substituents of organic compounds. Illustrative substituents include, for example, those described below. The permissible substituents can be one or more and the same or different for appropriate organic compounds. For purposes of this disclosure, the heteroatoms, such as nitrogen, can have hydrogen substituents and/or any permissible substituents of organic compounds described herein which satisfy the valences of the heteroatoms. This disclosure is not intended to be limited in any manner by the permissible substituents of organic compounds. Also, the terms “substitution” or “substituted with” include the implicit proviso that such substitution is in accordance with permitted valence of the substituted atom and the substituent, and that the substitution results in a stable compound, e.g., a compound that does not spontaneously undergo transformation such as by rearrangement, cyclization, elimination, etc. It is also contemplated that, in certain aspects, unless expressly indicated to the contrary, individual substituents can be further optionally substituted (i.e., further substituted or unsubstituted). [0083] In defining various terms, “A¹,” “A²,” “A³,” and “A⁴” are used herein as generic symbols to represent various specific substituents. These symbols can be any substituent, not limited to those disclosed herein, and when they are defined to be certain substituents in one instance, they can, in another instance, be defined as some other substituents. [0084] The term “aliphatic” or “aliphatic group,” as used herein, denotes a hydrocarbon moiety that may be straight-chain (i.e., unbranched), branched, or cyclic (including fused, bridging, and spirofused polycyclic) and may be completely saturated or may contain one or more units of unsaturation, but which is not aromatic. Unless otherwise specified, aliphatic groups contain 1-20 carbon atoms. Aliphatic groups include, but are not limited to, linear or branched, alkyl, alkenyl, and alkynyl groups, and hybrids thereof such as (cycloalkyl)alkyl, (cycloalkenyl)alkyl or (cycloalkyl)alkenyl. [0085] The term “alkyl” as used herein is a branched or unbranched saturated hydrocarbon group of 1 to 24 carbon atoms, such as methyl, ethyl, n-propyl, isopropyl, n-butyl, isobutyl, s- butyl, t-butyl, n-pentyl, isopentyl, s-pentyl, neopentyl, hexyl, heptyl, octyl, nonyl, decyl, dodecyl, tetradecyl, hexadecyl, eicosyl, tetracosyl, and the like. The alkyl group can be cyclic or acyclic. The alkyl group can be branched or unbranched. The alkyl group can also be substituted or unsubstituted. For example, the alkyl group can be substituted with one or more groups including, but not limited to, alkyl, cycloalkyl, alkoxy, amino, ether, halide, hydroxy, nitro, silyl, sulfo-oxo, or thiol, as described herein. A “lower alkyl” group is an alkyl group containing from one to six (e.g., from one to four) carbon atoms. The term alkyl group can also be a C1 alkyl, C1-C2 alkyl, C1-C3 alkyl, C1-C4 alkyl, C1-C5 alkyl, C1-C6 alkyl, C1-C7 alkyl, C1-C8 alkyl, C1-C9 alkyl, C1-C10 alkyl, and the like up to and including a C1-C24 alkyl. [0086] Throughout the specification “alkyl” is generally used to refer to both unsubstituted alkyl groups and substituted alkyl groups; however, substituted alkyl groups are also specifically referred to herein by identifying the specific substituent(s) on the alkyl group. For example, the term “halogenated alkyl” or “haloalkyl” specifically refers to an alkyl group that is substituted with one or more halide, e.g., fluorine, chlorine, bromine, or iodine. Alternatively, the term “monohaloalkyl” specifically refers to an alkyl group that is substituted with a single halide, e.g. fluorine, chlorine, bromine, or iodine. The term “polyhaloalkyl” specifically refers to an alkyl group that is independently substituted with two or more halides, i.e. each halide substituent need not be the same halide as another halide substituent, nor do the multiple instances of a halide substituent need to be on the same carbon. The term “alkoxyalkyl” specifically refers to an alkyl group that is substituted with one or more alkoxy groups, as described below. The term “aminoalkyl” specifically refers to an alkyl group that is substituted with one or more amino groups. The term “hydroxyalkyl” specifically refers to an alkyl group that is substituted with one or more hydroxy groups. When “alkyl” is used in one instance and a specific term such as “hydroxyalkyl” is used in another, it is not meant to imply that the term “alkyl” does not also refer to specific terms such as “hydroxyalkyl” and the like. [0087] This practice is also used for other groups described herein. That is, while a term such as “cycloalkyl” refers to both unsubstituted and substituted cycloalkyl moieties, the substituted moieties can, in addition, be specifically identified herein; for example, a particular substituted cycloalkyl can be referred to as, e.g., an “alkylcycloalkyl.” Similarly, a substituted alkoxy can be specifically referred to as, e.g., a “halogenated alkoxy,” a particular substituted alkenyl can be, e.g., an “alkenylalcohol,” and the like. Again, the practice of using a general term, such as “cycloalkyl,” and a specific term, such as “alkylcycloalkyl,” is not meant to imply that the general term does not also include the specific term. [0088] The term “cycloalkyl” as used herein is a non-aromatic carbon-based ring composed of at least three carbon atoms. Examples of cycloalkyl groups include, but are not limited to, cyclopropyl, cyclobutyl, cyclopentyl, cyclohexyl, norbornyl, and the like. The term “heterocycloalkyl” is a type of cycloalkyl group as defined above, and is included within the meaning of the term “cycloalkyl,” where at least one of the carbon atoms of the ring is replaced with a heteroatom such as, but not limited to, nitrogen, oxygen, sulfur, or phosphorus. The cycloalkyl group and heterocycloalkyl group can be substituted or unsubstituted. The cycloalkyl group and heterocycloalkyl group can be substituted with one or more groups including, but not limited to, alkyl, cycloalkyl, alkoxy, amino, ether, halide, hydroxy, nitro, silyl, sulfo-oxo, or thiol as described herein. [0089] The term “polyalkylene group” as used herein is a group having two or more CH₂ groups linked to one another. The polyalkylene group can be represented by the formula — (CH₂)_a—, where “a” is an integer of from 2 to 500. [0090] The terms “alkoxy” and “alkoxyl” as used herein to refer to an alkyl or cycloalkyl group bonded through an ether linkage; that is, an “alkoxy” group can be defined as —OA¹ where A¹ is alkyl or cycloalkyl as defined above. “Alkoxy” also includes polymers of alkoxy groups as just described; that is, an alkoxy can be a polyether such as —OA¹—OA² or — OA¹—(OA²)_a—OA³, where “a” is an integer of from 1 to 200 and A¹, A², and A³ are alkyl and/or cycloalkyl groups. [0091] The term “alkenyl” as used herein is a hydrocarbon group of from 2 to 24 carbon atoms with a structural formula containing at least one carbon-carbon double bond. Asymmetric structures such as (A¹A²)C=C(A³A⁴) are intended to include both the E and Z isomers. This can be presumed in structural formulae herein wherein an asymmetric alkene is present, or it can be explicitly indicated by the bond symbol C=C. The alkenyl group can be substituted with one or more groups including, but not limited to, alkyl, cycloalkyl, alkoxy, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, heteroaryl, aldehyde, amino, carboxylic acid, ester, ether, halide, hydroxy, ketone, azide, nitro, silyl, sulfo-oxo, or thiol, as described herein. [0092] The term “cycloalkenyl” as used herein is a non-aromatic carbon-based ring composed of at least three carbon atoms and containing at least one carbon-carbon double bound, i.e., C=C. Examples of cycloalkenyl groups include, but are not limited to, cyclopropenyl, cyclobutenyl, cyclopentenyl, cyclopentadienyl, cyclohexenyl, cyclohexadienyl, norbornenyl, and the like. The term “heterocycloalkenyl” is a type of cycloalkenyl group as defined above, and is included within the meaning of the term “cycloalkenyl,” where at least one of the carbon atoms of the ring is replaced with a heteroatom such as, but not limited to, nitrogen, oxygen, sulfur, or phosphorus. The cycloalkenyl group and heterocycloalkenyl group can be substituted or unsubstituted. The cycloalkenyl group and heterocycloalkenyl group can be substituted with one or more groups including, but not limited to, alkyl, cycloalkyl, alkoxy, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, heteroaryl, aldehyde, amino, carboxylic acid, ester, ether, halide, hydroxy, ketone, azide, nitro, silyl, sulfo-oxo, or thiol as described herein. [0093] The term “alkynyl” as used herein is a hydrocarbon group of 2 to 24 carbon atoms with a structural formula containing at least one carbon-carbon triple bond. The alkynyl group can be unsubstituted or substituted with one or more groups including, but not limited to, alkyl, cycloalkyl, alkoxy, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, heteroaryl, aldehyde, amino, carboxylic acid, ester, ether, halide, hydroxy, ketone, azide, nitro, silyl, sulfo-oxo, or thiol, as described herein. [0094] The term “cycloalkynyl” as used herein is a non-aromatic carbon-based ring composed of at least seven carbon atoms and containing at least one carbon-carbon triple bound. Examples of cycloalkynyl groups include, but are not limited to, cycloheptynyl, cyclooctynyl, cyclononynyl, and the like. The term “heterocycloalkynyl” is a type of cycloalkenyl group as defined above, and is included within the meaning of the term “cycloalkynyl,” where at least one of the carbon atoms of the ring is replaced with a heteroatom such as, but not limited to, nitrogen, oxygen, sulfur, or phosphorus. The cycloalkynyl group and heterocycloalkynyl group can be substituted or unsubstituted. The cycloalkynyl group and heterocycloalkynyl group can be substituted with one or more groups including, but not limited to, alkyl, cycloalkyl, alkoxy, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, heteroaryl, aldehyde, amino, carboxylic acid, ester, ether, halide, hydroxy, ketone, azide, nitro, silyl, sulfo-oxo, or thiol as described herein. [0095] The term “aromatic group” as used herein refers to a ring structure having cyclic clouds of delocalized π electrons above and below the plane of the molecule, where the π clouds contain (4n+2) π electrons. A further discussion of aromaticity is found in Morrison and Boyd, Organic Chemistry, (5th Ed., 1987), Chapter 13, entitled “Aromaticity,” pages 477-497, incorporated herein by reference. The term “aromatic group” is inclusive of both aryl and heteroaryl groups. [0096] The term “aryl” as used herein is a group that contains any carbon-based aromatic group including, but not limited to, benzene, naphthalene, phenyl, biphenyl, anthracene, and the like. The aryl group can be substituted or unsubstituted. The aryl group can be substituted with one or more groups including, but not limited to, alkyl, cycloalkyl, alkoxy, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, heteroaryl, aldehyde, ─NH₂, carboxylic acid, ester, ether, halide, hydroxy, ketone, azide, nitro, silyl, sulfo-oxo, or thiol as described herein. The term “biaryl” is a specific type of aryl group and is included in the definition of “aryl.” In addition, the aryl group can be a single ring structure or comprise multiple ring structures that are either fused ring structures or attached via one or more bridging groups such as a carbon- carbon bond. For example, biaryl can be two aryl groups that are bound together via a fused ring structure, as in naphthalene, or are attached via one or more carbon-carbon bonds, as in biphenyl. [0097] The term “aldehyde” as used herein is represented by the formula —C(O)H. Throughout this specification “C(O)” is a short hand notation for a carbonyl group, i.e., C=O. [0098] The terms “amine” or “amino” as used herein are represented by the formula — NA¹A², where A¹ and A² can be, independently, hydrogen or alkyl, cycloalkyl, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, or heteroaryl group as described herein. A specific example of amino is ─NH₂. [0099] The term “alkylamino” as used herein is represented by the formula —NH(-alkyl) where alkyl is a described herein. Representative examples include, but are not limited to, methylamino group, ethylamino group, propylamino group, isopropylamino group, butylamino group, isobutylamino group, (sec-butyl)amino group, (tert-butyl)amino group, pentylamino group, isopentylamino group, (tert-pentyl)amino group, hexylamino group, and the like. [00100] The term “dialkylamino” as used herein is represented by the formula —N(-alkyl)₂ where alkyl is a described herein. Representative examples include, but are not limited to, dimethylamino group, diethylamino group, dipropylamino group, diisopropylamino group, dibutylamino group, diisobutylamino group, di(sec-butyl)amino group, di(tert-butyl)amino group, dipentylamino group, diisopentylamino group, di(tert-pentyl)amino group, dihexylamino group, N-ethyl-N-methylamino group, N-methyl-N-propylamino group, N- ethyl-N-propylamino group and the like. [00101] The term “carboxylic acid” as used herein is represented by the formula —C(O)OH. [00102] The term “ester” as used herein is represented by the formula —OC(O)A¹ or — C(O)OA¹, where A¹ can be alkyl, cycloalkyl, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, or heteroaryl group as described herein. The term “polyester” as used herein is represented by the formula —(A¹O(O)C-A²-C(O)O)a— or —(A¹O(O)C-A²-OC(O))a—, where A¹ and A² can be, independently, an alkyl, cycloalkyl, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, or heteroaryl group described herein and “a” is an integer from 1 to 500. “Polyester” is as the term used to describe a group that is produced by the reaction between a compound or peptide having at least two carboxylic acid groups with a compound or peptide having at least two hydroxyl groups. [00103] The term “ether” as used herein is represented by the formula A¹OA², where A¹ and A² can be, independently, an alkyl, cycloalkyl, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, or heteroaryl group described herein. The term “polyether” as used herein is represented by the formula —(A¹O-A²O)_a—, where A¹ and A² can be, independently, an alkyl, cycloalkyl, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, or heteroaryl group described herein and “a” is an integer of from 1 to 500. Examples of polyether groups include polyethylene oxide, polypropylene oxide, and polybutylene oxide. [00104] The terms “halo,” “halogen,” or “halide” as used herein can be used interchangeably and refer to F, Cl, Br, or I. [00105] The terms “pseudohalide,” “pseudohalogen,” or “pseudohalo” as used herein can be used interchangeably and refer to functional groups that behave substantially similar to halides. Such functional groups include, by way of example, cyano, thiocyanato, azido, trifluoromethyl, trifluoromethoxy, perfluoroalkyl, and perfluoroalkoxy groups. [00106] The term “heteroalkyl” as used herein refers to an alkyl group containing at least one heteroatom. Suitable heteroatoms include, but are not limited to, O, N, Si, P and S, wherein the nitrogen, phosphorous and sulfur atoms are optionally oxidized, and the nitrogen heteroatom is optionally quaternized. Heteroalkyls can be substituted as defined above for alkyl groups. [00107] The term “heteroaryl” as used herein refers to an aromatic group that has at least one heteroatom incorporated within the ring of the aromatic group. Examples of heteroatoms include, but are not limited to, nitrogen, oxygen, sulfur, and phosphorus, where N-oxides, sulfur oxides, and dioxides are permissible heteroatom substitutions. The heteroaryl group can be substituted or unsubstituted. The heteroaryl group can be substituted with one or more groups including, but not limited to, alkyl, cycloalkyl, alkoxy, amino, ether, halide, hydroxy, nitro, silyl, sulfo-oxo, or thiol as described herein. Heteroaryl groups can be monocyclic, or alternatively fused ring systems. Heteroaryl groups include, but are not limited to, furyl, imidazolyl, pyrimidinyl, tetrazolyl, thienyl, pyridinyl, pyrrolyl, N-methylpyrrolyl, quinolinyl, isoquinolinyl, pyrazolyl, triazolyl, thiazolyl, oxazolyl, isoxazolyl, oxadiazolyl, thiadiazolyl, isothiazolyl, pyridazinyl, pyrazinyl, benzofuranyl, benzodioxolyl, benzothiophenyl, indolyl, indazolyl, benzimidazolyl, imidazopyridinyl, pyrazolopyridinyl, and pyrazolopyrimidinyl. Further not limiting examples of heteroaryl groups include, but are not limited to, pyridinyl, pyridazinyl, pyrimidinyl, pyrazinyl, thiophenyl, pyrazolyl, imidazolyl, benzo[d]oxazolyl, benzo[d]thiazolyl, quinolinyl, quinazolinyl, indazolyl, imidazo[1,2-b]pyridazinyl, imidazo[1,2-a]pyrazinyl, benzo[c][1,2,5]thiadiazolyl, benzo[c][1,2,5]oxadiazolyl, and pyrido[2,3-b]pyrazinyl. [00108] The terms “heterocycle” or “heterocyclyl” as used herein can be used interchangeably and refer to single and multi-cyclic aromatic or non-aromatic ring systems in which at least one of the ring members is other than carbon. Thus, the term is inclusive of, but not limited to, “heterocycloalkyl”, “heteroaryl”, “bicyclic heterocycle” and “polycyclic heterocycle.” Heterocycle includes pyridine, pyrimidine, furan, thiophene, pyrrole, isoxazole, isothiazole, pyrazole, oxazole, thiazole, imidazole, oxazole, including, 1,2,3- oxadiazole, 1,2,5-oxadiazole and 1,3,4-oxadiazole, thiadiazole, including, 1,2,3-thiadiazole, 1,2,5-thiadiazole, and 1,3,4-thiadiazole, triazole, including, 1,2,3-triazole, 1,3,4-triazole, tetrazole, including 1,2,3,4-tetrazole and 1,2,4,5-tetrazole, pyridazine, pyrazine, triazine, including 1,2,4-triazine and 1,3,5-triazine, tetrazine, including 1,2,4,5-tetrazine, pyrrolidine, piperidine, piperazine, morpholine, azetidine, tetrahydropyran, tetrahydrofuran, dioxane, and the like. The term heterocyclyl group can also be a C2 heterocyclyl, C2-C3 heterocyclyl, C2- C4 heterocyclyl, C2-C5 heterocyclyl, C2-C6 heterocyclyl, C2-C7 heterocyclyl, C2-C8 heterocyclyl, C2-C9 heterocyclyl, C2-C10 heterocyclyl, C2-C11 heterocyclyl, and the like up to and including a C2-C18 heterocyclyl. For example, a C2 heterocyclyl comprises a group which has two carbon atoms and at least one heteroatom, including, but not limited to, aziridinyl, diazetidinyl, dihydrodiazetyl, oxiranyl, thiiranyl, and the like. Alternatively, for example, a C5 heterocyclyl comprises a group which has five carbon atoms and at least one heteroatom, including, but not limited to, piperidinyl, tetrahydropyranyl, tetrahydrothiopyranyl, diazepanyl, pyridinyl, and the like. It is understood that a heterocyclyl group may be bound either through a heteroatom in the ring, where chemically possible, or one of carbons comprising the heterocyclyl ring. [00109] The term “bicyclic heterocycle” or “bicyclic heterocyclyl” as used herein refers to a ring system in which at least one of the ring members is other than carbon. Bicyclic heterocyclyl encompasses ring systems wherein an aromatic ring is fused with another aromatic ring, or wherein an aromatic ring is fused with a non-aromatic ring. Bicyclic heterocyclyl encompasses ring systems wherein a benzene ring is fused to a 5- or a 6- membered ring containing 1, 2 or 3 ring heteroatoms or wherein a pyridine ring is fused to a 5- or a 6-membered ring containing 1, 2 or 3 ring heteroatoms. Bicyclic heterocyclic groups include, but are not limited to, indolyl, indazolyl, pyrazolo[1,5-a]pyridinyl, benzofuranyl, quinolinyl, quinoxalinyl, 1,3-benzodioxolyl, 2,3-dihydro-1,4-benzodioxinyl, 3,4-dihydro-2H- chromenyl, 1H-pyrazolo[4,3-c]pyridin-3-yl; 1H-pyrrolo[3,2-b]pyridin-3-yl; and 1H- pyrazolo[3,2-b]pyridin-3-yl. [00110] The term “heterocycloalkyl” as used herein refers to an aliphatic, partially unsaturated or fully saturated, 3- to 14-membered ring system, including single rings of 3 to 8 atoms and bi- and tricyclic ring systems. The heterocycloalkyl ring-systems include one to four heteroatoms independently selected from oxygen, nitrogen, and sulfur, wherein a nitrogen and sulfur heteroatom optionally can be oxidized and a nitrogen heteroatom optionally can be substituted. Representative heterocycloalkyl groups include, but are not limited to, pyrrolidinyl, pyrazolinyl, pyrazolidinyl, imidazolinyl, imidazolidinyl, piperidinyl, piperazinyl, oxazolidinyl, isoxazolidinyl, morpholinyl, thiazolidinyl, isothiazolidinyl, and tetrahydrofuryl. [00111] The term “hydroxyl” or “hydroxyl” as used herein is represented by the formula — OH. [00112] The term “ketone” as used herein is represented by the formula A¹C(O)A², where A¹ and A² can be, independently, an alkyl, cycloalkyl, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, or heteroaryl group as described herein. [00113] The term “azide” or “azido” as used herein is represented by the formula —N₃. [00114] The term “nitro” as used herein is represented by the formula —NO2. [00115] The term “nitrile” or “cyano” as used herein is represented by the formula —CN. [00116] The term “silyl” as used herein is represented by the formula —SiA¹A²A³, where A¹, A², and A³ can be, independently, hydrogen or an alkyl, cycloalkyl, alkoxy, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, or heteroaryl group as described herein. [00117] The term “sulfo-oxo” as used herein is represented by the formulas —S(O)A¹, — S(O)2A¹, —OS(O)2A¹, or —OS(O)2OA¹, where A¹ can be hydrogen or an alkyl, cycloalkyl, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, or heteroaryl group as described herein. Throughout this specification “S(O)” is a short hand notation for S=O. The term “sulfonyl” is used herein to refer to the sulfo-oxo group represented by the formula —S(O)₂A¹, where A¹ can be hydrogen or an alkyl, cycloalkyl, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, or heteroaryl group as described herein. The term “sulfone” as used herein is represented by the formula A¹S(O)2A², where A¹ and A² can be, independently, an alkyl, cycloalkyl, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, or heteroaryl group as described herein. The term “sulfoxide” as used herein is represented by the formula A¹S(O)A², where A¹ and A² can be, independently, an alkyl, cycloalkyl, alkenyl, cycloalkenyl, alkynyl, cycloalkynyl, aryl, or heteroaryl group as described herein. [00118] The term “thiol” as used herein is represented by the formula —SH. [00119] “R¹,” “R²,” “R³,” “Rⁿ,” where n is an integer, as used herein can, independently, possess one or more of the groups listed above. For example, if R¹ is a straight chain alkyl group, one of the hydrogen atoms of the alkyl group can optionally be substituted with a hydroxyl group, an alkoxy group, an alkyl group, a halide, and the like. Depending upon the groups that are selected, a first group can be incorporated within second group or, alternatively, the first group can be pendant (i.e., attached) to the second group. For example, with the phrase “an alkyl group comprising an amino group,” the amino group can be incorporated within the backbone of the alkyl group. Alternatively, the amino group can be attached to the backbone of the alkyl group. The nature of the group(s) that is (are) selected will determine if the first group is embedded or attached to the second group. [00120] As described herein, peptides of the invention may contain “optionally substituted” moieties. In general, the term “substituted,” whether preceded by the term “optionally” or not, means that one or more hydrogen of the designated moiety are replaced with a suitable substituent. Unless otherwise indicated, an “optionally substituted” group may have a suitable substituent at each substitutable position of the group, and when more than one position in any given structure may be substituted with more than one substituent selected from a specified group, the substituent may be either the same or different at every position. Combinations of substituents envisioned by this invention are preferably those that result in the formation of stable or chemically feasible peptides. In is also contemplated that, in certain aspects, unless expressly indicated to the contrary, individual substituents can be further optionally substituted (i.e., further substituted or unsubstituted). [00121] The term “stable,” as used herein, refers to peptides that are not substantially altered when subjected to conditions to allow for their production, detection, and, in certain aspects, their recovery, purification, and use for one or more of the purposes disclosed herein. [00122] Suitable monovalent substituents on a substitutable carbon atom of an “optionally substituted” group are independently halogen; –(CH2)0–4R ^; –(CH2)0–4OR ^; -O(CH2)0-4R^o, – O–(CH₂)_0–4C(O)OR°; –(CH₂)_0–4CH(OR ^)₂; –(CH₂)_0–4SR ^; –(CH₂)_0–4Ph, which may be substituted with R°; –(CH₂)_0–4O(CH₂)_0–1Ph which may be substituted with R°; –CH=CHPh, which may be substituted with R°; –(CH2)0–4O(CH2)0–1-pyridyl which may be substituted with R°; –NO₂; –CN; –N₃; -(CH₂)_0–4N(R ^)₂; –(CH₂)_0–4N(R ^)C(O)R ^; –N(R ^)C(S)R ^; – (CH2)0–4N(R ^)C(O)NR ^2; -N(R ^)C(S)NR ^2; –(CH2)0–4N(R ^)C(O)OR ^; –N(R ^)N(R ^)C(O)R ^; -N(R ^)N(R ^)C(O)NR ^2; -N(R ^)N(R ^)C(O)OR ^; –(CH2)0–4C(O)R ^; –C(S)R ^; –(CH2)0– ₄C(O)OR ^; –(CH₂)_0–4C(O)SR ^; -(CH₂)_0–4C(O)OSiR ^₃; –(CH₂)_0–4OC(O)R ^; –OC(O)(CH₂)_{0– 4}SR–, SC(S)SR°; –(CH₂)_0–4SC(O)R ^; –(CH₂)_0–4C(O)NR ^₂; –C(S)NR ^₂; –C(S)SR°; -(CH₂)_0– 4OC(O)NR ^2; -C(O)N(OR ^)R ^; –C(O)C(O)R ^; –C(O)CH2C(O)R ^; –C(NOR ^)R ^; -(CH2)0– 4SSR ^; –(CH2)0–4S(O)2R ^; –(CH2)0–4S(O)2OR ^; –(CH2)0–4OS(O)2R ^; –S(O)2NR ^2; -(CH2)0– ₄S(O)R ^; -N(R ^)S(O)₂NR ^₂; –N(R ^)S(O)₂R ^; –N(OR ^)R ^; –C(NH)NR ^₂; –P(O)₂R ^; -P(O)R ^₂; -OP(O)R ^₂; –OP(O)(OR ^)₂; SiR ^₃; –(C_1–4 straight or branched alkylene)O–N(R ^)₂; or –(C1–4 straight or branched alkylene)C(O)O–N(R ^)2, wherein each R ^ may be substituted as defined below and is independently hydrogen, C1–6 aliphatic, –CH2Ph, –O(CH2)0–1Ph, - CH₂-(5-6 membered heteroaryl ring), or a 5–6–membered saturated, partially unsaturated, or aryl ring having 0–4 heteroatoms independently selected from nitrogen, oxygen, or sulfur, or, notwithstanding the definition above, two independent occurrences of R ^, taken together with their intervening atom(s), form a 3–12–membered saturated, partially unsaturated, or aryl mono– or bicyclic ring having 0–4 heteroatoms independently selected from nitrogen, oxygen, or sulfur, which may be substituted as defined below. [00123] Suitable monovalent substituents on R ^ (or the ring formed by taking two independent occurrences of R ^ together with their intervening atoms), are independently halogen, –(CH2)0–2R ^{^}, –(haloR ^{^}), –(CH2)0–2OH, –(CH2)0–2OR ^{^}, –(CH2)0–2CH(OR ^{^})2; -O(haloR ^{^}), –CN, –N₃, –(CH₂)_0–2C(O)R ^{^}, –(CH₂)_0–2C(O)OH, –(CH₂)_0–2C(O)OR ^{^}, –(CH₂)_0– 2SR ^{^}, –(CH2)0–2SH, –(CH2)0–2NH2, –(CH2)0–2NHR ^{^}, –(CH2)0–2NR ^{^}2, –NO2, –SiR ^{^}3, –OSiR ^{^}3, -C(O)SR ^{^} _, –(C_1–4 straight or branched alkylene)C(O)OR ^{^}, or –SSR ^{^} wherein each R ^{^} is unsubstituted or where preceded by “halo” is substituted only with one or more halogens, and is independently selected from C_1–4 aliphatic, –CH₂Ph, –O(CH₂)_0–1Ph, or a 5–6–membered saturated, partially unsaturated, or aryl ring having 0–4 heteroatoms independently selected from nitrogen, oxygen, or sulfur. Suitable divalent substituents on a saturated carbon atom of R ^ include =O and =S. [00124] Suitable divalent substituents on a saturated carbon atom of an “optionally substituted” group include the following: =O, =S, =NNR^*2, =NNHC(O)R^*, =NNHC(O)OR^*, =NNHS(O)₂R^*, =NR^*, =NOR^*, –O(C(R^* ₂))_2–3O–, or –S(C(R^* ₂))_2–3S–, wherein each independent occurrence of R^* is selected from hydrogen, C1–6 aliphatic which may be substituted as defined below, or an unsubstituted 5–6–membered saturated, partially unsaturated, or aryl ring having 0–4 heteroatoms independently selected from nitrogen, oxygen, or sulfur. Suitable divalent substituents that are bound to vicinal substitutable carbons of an “optionally substituted” group include: –O(CR^*2)2–3O–, wherein each independent occurrence of R^* is selected from hydrogen, C_1–6 aliphatic which may be substituted as defined below, or an unsubstituted 5–6–membered saturated, partially unsaturated, or aryl ring having 0–4 heteroatoms independently selected from nitrogen, oxygen, or sulfur. [00125] Suitable substituents on the aliphatic group of R^* include halogen, –R ^{^}, -(haloR ^{^}), -OH, –OR ^{^}, –O(haloR ^{^}), –CN, –C(O)OH, –C(O)OR ^{^}, –NH2, –NHR ^{^}, –NR ^{^}2, or –NO2, wherein each R ^{^} is unsubstituted or where preceded by “halo” is substituted only with one or more halogens, and is independently C1–4 aliphatic, –CH2Ph, –O(CH2)0–1Ph, or a 5–6– membered saturated, partially unsaturated, or aryl ring having 0–4 heteroatoms independently selected from nitrogen, oxygen, or sulfur. [00126] Suitable substituents on a substitutable nitrogen of an “optionally substituted” group include –R^†, –NR^†2, –C(O)R^†, –C(O)OR^†, –C(O)C(O)R^†, –C(O)CH2C(O)R^†, –S(O)2R^†, -S(O)₂NR^† ₂, –C(S)NR^† ₂, –C(NH)NR^† ₂, or –N(R^†)S(O)₂R^†; wherein each R^† is independently hydrogen, C1–6 aliphatic which may be substituted as defined below, unsubstituted –OPh, or an unsubstituted 5–6–membered saturated, partially unsaturated, or aryl ring having 0–4 heteroatoms independently selected from nitrogen, oxygen, or sulfur, or, notwithstanding the definition above, two independent occurrences of R^†, taken together with their intervening atom(s) form an unsubstituted 3–12–membered saturated, partially unsaturated, or aryl mono– or bicyclic ring having 0–4 heteroatoms independently selected from nitrogen, oxygen, or sulfur. [00127] Suitable substituents on the aliphatic group of R^† are independently halogen, –R , ^● -(haloR ^●), –OH, –OR ^●, –O(haloR ), –CN, ^● –C(O)OH, –C(O)OR , –NH2, –NHR^●, –NR 2, or ^{● ●} –NO₂, wherein each R ^● is unsubstituted or where preceded by “halo” is substituted only with one or more halogens, and is independently C1–4 aliphatic, –CH2Ph, –O(CH2)0–1Ph, or a 5–6– membered saturated, partially unsaturated, or aryl ring having 0–4 heteroatoms independently selected from nitrogen, oxygen, or sulfur. [00128] The term “leaving group” refers to an atom (or a group of atoms) with electron withdrawing ability that can be displaced as a stable species, taking with it the bonding electrons. Examples of suitable leaving groups include halides and sulfonate esters, including, but not limited to, triflate, mesylate, tosylate, and brosylate. [00129] The terms “hydrolysable group” and “hydrolysable moiety” refer to a functional group capable of undergoing hydrolysis, e.g., under basic or acidic conditions. Examples of hydrolysable residues include, without limitation, acid halides, activated carboxylic acids, and various protecting groups known in the art (see, for example, “Protective Groups in Organic Synthesis,” T. W. Greene, P. G. M. Wuts, Wiley-Interscience, 1999). [00130] The phrase “residue of a peptide” as used with respect to the phrase “a surface covalently attached to a residue of a disclosed peptide,” means the portion of the peptide that remains after the peptide is covalently attached to, for example, the surface. Thus, for example, the residue of the peptide can refer to the peptide minus an atom or group of atoms at the N-terminus of the peptide such as, for example, a proton. [00131] The term “organic residue” defines a carbon-containing residue, i.e., a residue comprising at least one carbon atom, and includes but is not limited to the carbon-containing groups, residues, or radicals defined hereinabove. Organic residues can contain various heteroatoms, or be bonded to another molecule through a heteroatom, including oxygen, nitrogen, sulfur, phosphorus, or the like. Examples of organic residues include but are not limited alkyl or substituted alkyls, alkoxy or substituted alkoxy, mono or di-substituted amino, amide groups, etc. Organic residues can preferably comprise 1 to 18 carbon atoms, 1 to 15, carbon atoms, 1 to 12 carbon atoms, 1 to 8 carbon atoms, 1 to 6 carbon atoms, or 1 to 4 carbon atoms. In a further aspect, an organic residue can comprise 2 to 18 carbon atoms, 2 to 15, carbon atoms, 2 to 12 carbon atoms, 2 to 8 carbon atoms, 2 to 4 carbon atoms, or 2 to 4 carbon atoms. [00132] Peptides described herein can contain one or more double bonds and, thus, potentially give rise to cis/trans (E/Z) isomers, as well as other conformational isomers. Unless stated to the contrary, the invention includes all such possible isomers, as well as mixtures of such isomers. [00133] Unless stated to the contrary, a formula with chemical bonds shown only as solid lines and not as wedges or dashed lines contemplates each possible isomer, e.g., each enantiomer and diastereomer, and a mixture of isomers, such as a racemic or scalemic mixture. Peptides described herein can contain one or more asymmetric centers and, thus, potentially give rise to diastereomers and optical isomers. Unless stated to the contrary, the present invention includes all such possible diastereomers as well as their racemic mixtures, their substantially pure resolved enantiomers, all possible geometric isomers, and pharmaceutically acceptable salts thereof. Mixtures of stereoisomers, as well as isolated specific stereoisomers, are also included. During the course of the synthetic procedures used to prepare such compounds, or in using racemization or epimerization procedures known to those skilled in the art, the products of such procedures can be a mixture of stereoisomers. [00134] Many organic compounds (e.g., peptides) exist in optically active forms having the ability to rotate the plane of plane-polarized light. In describing an optically active compound, the prefixes D and L or R and S are used to denote the absolute configuration of the molecule about its chiral center(s). The prefixes d and l or (+) and (-) are employed to designate the sign of rotation of plane-polarized light by the compound, with (-) or meaning that the compound is levorotatory. A compound prefixed with (+) or d is dextrorotatory. For a given chemical structure, these compounds, called stereoisomers, are identical except that they are non-superimposable mirror images of one another. A specific stereoisomer can also be referred to as an enantiomer, and a mixture of such isomers is often called an enantiomeric mixture. A 50:50 mixture of enantiomers is referred to as a racemic mixture. Many of the compounds described herein can have one or more chiral centers and therefore can exist in different enantiomeric forms. If desired, a chiral carbon can be designated with an asterisk (*). When bonds to the chiral carbon are depicted as straight lines in the disclosed formulas, it is understood that both the (R) and (S) configurations of the chiral carbon, and hence both enantiomers and mixtures thereof, are embraced within the formula. As is used in the art, when it is desired to specify the absolute configuration about a chiral carbon, one of the bonds to the chiral carbon can be depicted as a wedge (bonds to atoms above the plane) and the other can be depicted as a series or wedge of short parallel lines is (bonds to atoms below the plane). The Cahn-Ingold-Prelog system can be used to assign the (R) or (S) configuration to a chiral carbon. [00135] When the disclosed peptides contain one chiral center, the peptides exist in two enantiomeric forms. Unless specifically stated to the contrary, a disclosed peptide includes both enantiomers and mixtures of enantiomers, such as the specific 50:50 mixture referred to as a racemic mixture. The enantiomers can be resolved by methods known to those skilled in the art, such as formation of diastereoisomeric salts that may be separated, for example, by crystallization (see, CRC Handbook of Optical Resolutions via Diastereomeric Salt Formation by David Kozma (CRC Press, 2001)); formation of diastereoisomeric derivatives or complexes that may be separated, for example, by crystallization, gas-liquid or liquid chromatography; selective reaction of one enantiomer with an enantiomer-specific reagent, for example enzymatic esterification; or gas-liquid or liquid chromatography in a chiral environment, for example on a chiral support for example silica with a bound chiral ligand or in the presence of a chiral solvent. It will be appreciated that where the desired enantiomer is converted into another chemical entity by one of the separation procedures described above, a further step can liberate the desired enantiomeric form. Alternatively, specific enantiomers can be synthesized by asymmetric synthesis using optically active reagents, substrates, catalysts or solvents, or by converting one enantiomer into the other by asymmetric transformation. [00136] Designation of a specific absolute configuration at a chiral carbon in a disclosed peptide is understood to mean that the designated enantiomeric form of the peptides can be provided in enantiomeric excess (e.e.). Enantiomeric excess, as used herein, is the presence of a particular enantiomer at greater than 50%, for example, greater than 60%, greater than 70%, greater than 75%, greater than 80%, greater than 85%, greater than 90%, greater than 95%, greater than 98%, or greater than 99%. In one aspect, the designated enantiomer is substantially free from the other enantiomer. For example, the “R” forms of the peptides can be substantially free from the “S” forms of the peptides and are, thus, in enantiomeric excess of the “S” forms. Conversely, “S” forms of the peptides can be substantially free of “R” forms of the peptides and are, thus, in enantiomeric excess of the “R” forms. [00137] When a disclosed peptide or compound has two or more chiral carbons, it can have more than two optical isomers and can exist in diastereoisomeric forms. For example, when there are two chiral carbons, the peptide or compound can have up to four optical isomers and two pairs of enantiomers ((S,S)/(R,R) and (R,S)/(S,R)). The pairs of enantiomers (e.g., (S,S)/(R,R)) are mirror image stereoisomers of one another. The stereoisomers that are not mirror-images (e.g., (S,S) and (R,S)) are diastereomers. The diastereoisomeric pairs can be separated by methods known to those skilled in the art, for example chromatography or crystallization and the individual enantiomers within each pair may be separated as described above. Unless otherwise specifically excluded, a disclosed peptide or compound includes each diastereoisomer of such peptides or compounds and mixtures thereof. [00138] The peptides according to this disclosure may form prodrugs at hydroxyl or amino functionalities using alkoxy, amino acids, etc., groups as the prodrug forming moieties. For instance, the hydroxymethyl position may form mono-, di- or triphosphates and again these phosphates can form prodrugs. Preparations of such prodrug derivatives are discussed in various literature sources (examples are: Alexander et al., J. Med. Chem.1988, 31, 318; Aligas-Martin et al., PCT WO 2000/041531, p.30). The nitrogen function converted in preparing these derivatives is one (or more) of the nitrogen atoms of a compound of the disclosure. [00139] “Derivatives” of the peptides disclosed herein are pharmaceutically acceptable salts, prodrugs, deuterated forms, radio-actively labeled forms, isomers, solvates and combinations thereof. The “combinations” mentioned in this context are refer to derivatives falling within at least two of the groups: pharmaceutically acceptable salts, prodrugs, deuterated forms, radio-actively labeled forms, isomers, and solvates. Examples of radio-actively labeled forms include peptides labeled with tritium, phosphorous-32, iodine-129, carbon-11, fluorine-18, and the like. [00140] Peptides described herein comprise atoms in both their natural isotopic abundance and in non-natural abundance. The disclosed peptides can be isotopically-labeled or isotopically-substituted peptides identical to those described, but for the fact that one or more atoms are replaced by an atom having an atomic mass or mass number different from the atomic mass or mass number typically found in nature. Examples of isotopes that can be incorporated into peptides of the invention include isotopes of hydrogen, carbon, nitrogen, oxygen, phosphorous, fluorine and chlorine, such as ² H, ³ H, ¹³ C, ¹⁴ C, ¹⁵ N, ¹⁸ O, ¹⁷ O, ³⁵ S, ¹⁸ F and ³⁶ Cl, respectively. Isotopically labeled peptides of the present invention and prodrugs thereof can generally be prepared by carrying out the procedures below, by substituting a readily available isotopically labeled reagent for a non-isotopically labeled reagent. [00141] The peptides described in the invention can be present as a solvate. In some cases, the solvent used to prepare the solvate is an aqueous solution, and the solvate is then often referred to as a hydrate. The peptides can be present as a hydrate, which can be obtained, for example, by crystallization from a solvent or from aqueous solution. In this connection, one, two, three or any arbitrary number of solvent or water molecules can combine with the peptides according to the invention to form solvates and hydrates. Unless stated to the contrary, the invention includes all such possible solvates. [00142] The term “co-crystal” means a physical association of two or more molecules which owe their stability through non-covalent interaction. One or more components of this molecular complex provide a stable framework in the crystalline lattice. In certain instances, the guest molecules are incorporated in the crystalline lattice as anhydrates or solvates, see e.g. “Crystal Engineering of the Composition of Pharmaceutical Phases. Do Pharmaceutical Co-crystals Represent a New Path to Improved Medicines?” Almarasson, O., et. al., The Royal Society of Chemistry, 1889-1896, 2004. Examples of co-crystals include p- toluenesulfonic acid and benzenesulfonic acid. [00143] It is also appreciated that certain peptides described herein can be present as an equilibrium of tautomers. For example, ketones with an α-hydrogen can exist in an equilibrium of the keto form and the enol form.

[00144] Likewise, amides with an N-hydrogen can exist in an equilibrium of the amide form and the imidic acid form. As another example, pyrazoles can exist in two tautomeric forms, N¹-unsubstituted, 3-A³ and N¹-unsubstituted, 5-A³ as shown below.

Unless stated to the contrary, the invention includes all such possible tautomers. [00145] It is known that chemical substances form solids that are present in different states of order, which are termed polymorphic forms or modifications. The different modifications of a polymorphic substance can differ greatly in their physical properties. The compounds according to the invention can be present in different polymorphic forms, with it being possible for particular modifications to be metastable. Unless stated to the contrary, the invention includes all such possible polymorphic forms. [00146] In some aspects, a structure of a peptide can include a group represented by a formula:

, which is understood to be equivalent to a formula:

, wherein n is typically an integer. That is, Rⁿ is understood to represent five independent substituents, R^n(a), R^n(b), R^n(c), R^n(d), R^n(e). By “independent substituents,” it is meant that each R substituent can be independently defined. For example, if in one instance R^n(a) is halogen, then R^n(b) is not necessarily halogen in that instance. [00147] Certain materials, peptides, compositions, and components disclosed herein can be obtained commercially or readily synthesized using techniques generally known to those of skill in the art. For example, the starting materials and reagents used in preparing the disclosed peptides and compositions are either available from commercial suppliers such as Aldrich Chemical Co., (Milwaukee, Wis.), Acros Organics (Morris Plains, N.J.), Strem Chemicals (Newburyport, MA), Fisher Scientific (Pittsburgh, Pa.), or Sigma (St. Louis, Mo.) or are prepared by methods known to those skilled in the art following procedures set forth in references such as Fieser and Fieser’s Reagents for Organic Synthesis, Volumes 1-17 (John Wiley and Sons, 1991); Rodd’s Chemistry of Carbon Compounds, Volumes 1-5 and supplemental volumes (Elsevier Science Publishers, 1989); Organic Reactions, Volumes 1-40 (John Wiley and Sons, 1991); March’s Advanced Organic Chemistry, (John Wiley and Sons, 4th Edition); and Larock’s Comprehensive Organic Transformations (VCH Publishers Inc., 1989). [00148] Unless otherwise expressly stated, it is in no way intended that any method set forth herein be construed as requiring that its steps be performed in a specific order. Accordingly, where a method claim does not actually recite an order to be followed by its steps or it is not otherwise specifically stated in the claims or descriptions that the steps are to be limited to a specific order, it is no way intended that an order be inferred, in any respect. This holds for any possible non-express basis for interpretation, including: matters of logic with respect to arrangement of steps or operational flow; plain meaning derived from grammatical organization or punctuation; and the number or type of embodiments described in the specification. [00149] Disclosed are the components to be used to prepare the compositions of the invention as well as the compositions themselves to be used within the methods disclosed herein. These and other materials are disclosed herein, and it is understood that when combinations, subsets, interactions, groups, etc. of these materials are disclosed that while specific reference of each various individual and collective combinations and permutation of these compounds cannot be explicitly disclosed, each is specifically contemplated and described herein. For example, if a particular peptide is disclosed and discussed and a number of modifications that can be made to a number of molecules including the peptides are discussed, specifically contemplated is each and every combination and permutation of the peptide and the modifications that are possible unless specifically indicated to the contrary. Thus, if a class of molecules A, B, and C are disclosed as well as a class of molecules D, E, and F and an example of a combination molecule, A-D is disclosed, then even if each is not individually recited each is individually and collectively contemplated meaning combinations, A-E, A-F, B-D, B-E, B-F, C-D, C-E, and C-F are considered disclosed. Likewise, any subset or combination of these is also disclosed. Thus, for example, the sub-group of A-E, B-F, and C-E would be considered disclosed. This concept applies to all aspects of this application including, but not limited to, steps in methods of making and using the compositions of the invention. Thus, if there are a variety of additional steps that can be performed it is understood that each of these additional steps can be performed with any specific embodiment or combination of embodiments of the methods of the invention. [00150] It is understood that the compositions disclosed herein have certain functions. Disclosed herein are certain structural requirements for performing the disclosed functions, and it is understood that there are a variety of structures that can perform the same function that are related to the disclosed structures, and that these structures will typically achieve the same result. B. PEPTIDES [00151] In one aspect, disclosed are peptides comprising alanine residues and glycosylated residues (e.g., glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues) in a particular ratio (e.g., from about 3:2 to about 4:1), wherein the peptide has a minumum chain length, such as, for example a chain length of at least 30 amino acids. As detailed elsewhere herein, the disclosed peptides beneficially inhibit ice crystal formation, and, therefore, offer utility in a wide range of applications, including, but not limited to biomedical cryopreservation, food technology, agriculture, cosmetics, and building materials. [00152] In one aspect, the disclosed peptides exhibit inhibition of ice crystal formation in a sample, as further described herein. As would be understood by one of ordinary skill in the art, inhibition of ice crystal formation can be measured by, for example, ice recrystallization inhibition (IRI) and reduction in crystal mean grain size (MGS). Thus, in various aspects, the disclosed peptides reduce crystal MGS by at least about 10%, about 20%, about 25%, about 30%, about 40%, about 50%, about 60%, about 65%, about 70%, about 75%, or more than about 75%. In various further aspects, the disclosed peptides alter the shape of ice crystals that are formed in the sample such that the majority of the ice crystals present in the sample are hexagonal, square, and/or amorphous crystals (as opposed to spicular crystals). In various further aspects, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, or more than 90% of the ice crystals present in the sample are hexagonal, square, and/or amorphous crystals. [00153] In one aspect, the disclosed peptides are useful in delaying, preventing, or otherwise decreasing ice crystal formation in a sample, as further described herein. [00154] It is contemplated that each disclosed derivative can be optionally further substituted. It is also contemplated that any one or more derivative can be optionally omitted from the invention. It is understood that a disclosed peptide can be provided by the disclosed methods. It is also understood that the disclosed peptides can be employed in the disclosed methods of using. 1. S^TRUCTURE [00155] In one aspect, disclosed are peptides comprising a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, and wherein the peptide has a chain length of at least 30 amino acid residues. [00156] In various aspects, the peptide consists essentially of the plurality of alanine residues and the plurality of glycosylated residues. [00157] In various aspects, the plurality of alanine residues is present in the peptide in an amount of about 70 wt% or less. In a further aspect, the plurality of alanine residues is present in the peptide in an amount of about 69 wt% or less. In a still further aspect, the plurality of alanine residues is present in the peptide in an amount of about 68 wt% or less. In yet a further aspect, the plurality of alanine residues is present in the peptide in an amount of about 67 wt% or less. In an even further aspect, the plurality of alanine residues is present in the peptide in an amount of about 66 wt% or less. In a still further aspect, the plurality of alanine residues is present in the peptide in an amount of about 65 wt% or less. In yet a further aspect, the plurality of alanine residues is present in the peptide in an amount of about 64 wt% or less. In an even further aspect, the plurality of alanine residues is present in the peptide in an amount of about 63 wt% or less. In a still further aspect, the plurality of alanine residues is present in the peptide in an amount of about 62 wt% or less. In yet a further aspect, the plurality of alanine residues is present in the peptide in an amount of about 61 wt% or less. In an even further aspect, the plurality of alanine residues is present in the peptide in an amount of about 60 wt% or less [00158] In various aspects, the plurality of alanine residues is present in the peptide in an amount of from about 60 wt% to about 70 wt%. In a further aspect, the plurality of alanine residues is present in the peptide in an amount of from about 60 wt% to about 68 wt%. In a still further aspect, the plurality of alanine residues is present in the peptide in an amount of from about 60 wt% to about 66 wt%. In yet a further aspect, the plurality of alanine residues is present in the peptide in an amount of from about 60 wt% to about 64 wt%. In an even further aspect, the plurality of alanine residues is present in the peptide in an amount of from about 60 wt% to about 62 wt%. In a still further aspect, the plurality of alanine residues is present in the peptide in an amount of from about 62 wt% to about 70 wt%. In yet a further aspect, the plurality of alanine residues is present in the peptide in an amount of from about 64 wt% to about 70 wt%. In an even further aspect, the plurality of alanine residues is present in the peptide in an amount of from about 66 wt% to about 70 wt%. In a still further aspect, the plurality of alanine residues is present in the peptide in an amount of from about 68 wt% to about 70 wt%. In yet a further aspect, the plurality of alanine residues is present in the peptide in an amount of from about 62 wt% to about 68 wt%. In a still further aspect, the plurality of alanine residues is present in the peptide in an amount of from about 64 wt% to about 66 wt%. In yet a further aspect, the plurality of alanine residues is present in the peptide in an amount of from about 65 wt% to about 67 wt%. [00159] In various aspects, the plurality of alanine residues is present in the peptide in an amount of about 60 wt%. In a still further aspect, the plurality of alanine residues is present in the peptide in an amount of about 61 wt%. In yet a further aspect, the plurality of alanine residues is present in the peptide in an amount of about 62 wt%. In an even further aspect, the plurality of alanine residues is present in the peptide in an amount of about 63 wt%. In a still further aspect, the plurality of alanine residues is present in the peptide in an amount of about 64 wt%. In yet a further aspect, the plurality of alanine residues is present in the peptide in an amount of about 65 wt%. In even further aspect, the plurality of alanine residues is present in the peptide in an amount of about 66 wt%. In an even still further aspect, the plurality of alanine residues is present in the peptide in an amount of about 67 wt%. In an even yet further aspect, the plurality of alanine residues is present in the peptide in an amount of about 68 wt%. In a further aspect, the plurality of alanine residues is present in the peptide in an amount of about 69 wt%. In a still further aspect, the plurality of alanine residues is present in the peptide in an amount of about 70 wt%. [00160] In various aspects, the peptide comprising a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, wherein the peptide has a chain length of at least 30 amino acid residues; and contains less than 36 sequential Ala-Ala-Thr repeating units. [00161] In various aspects, the peptide comprising a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, wherein the peptide has a chain length of at least 30 amino acid residues; and contains less than 36 sequential Ala-Ala-Ser repeating units. [00162] In various aspects, the peptide comprising a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, wherein the peptide has a chain length of at least 30 amino acid residues; and the plurality of glycosylated residues are glycosylated threonine residues. [00163] In various aspects, the peptide comprising a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, wherein the peptide has a chain length of at least 30 amino acid residues; and the plurality of glycosylated residues are glycosylated serine residues. [00164] In various aspects, the peptide comprising a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, wherein the peptide has a chain length of at least 30 amino acid residues; the peptide contains less than 36 sequential Ala-Ala-Thr repeating units; and the plurality of glycosylated residues are glycosylated threonine residues. [00165] In various aspects, the peptide comprising a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, wherein the peptide has a chain length of at least 30 amino acid residues; the peptide contains less than 36 sequential Ala-Ala-Ser repeating units; and the plurality of glycosylated residues are glycosylated serine residues. [00166] In various aspects, the peptide comprising a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, wherein the peptide has a chain length of at least 30 amino acid residues; the peptide contains less than 36 sequential Ala-Ala-Thr repeating units; and the plurality of glycosylated residues are a mixture of glycosylated threonine residues and glycosylated serine residues. [00167] In various aspects, the peptide contains less than 36 sequential Ala-Ala-Thr repeating units. In a further aspect, the peptide contains less than 35 sequential Ala-Ala-Thr repeating units. In a still further aspect, the peptide contains less than 34 sequential Ala-Ala- Thr repeating units. In yet a further aspect, the peptide contains less than 33 sequential Ala- Ala-Thr repeating units. In an even further aspect, the peptide contains less than 32 sequential Ala-Ala-Thr repeating units. In a still even further aspect, the peptide contains less than 31 sequential Ala-Ala-Thr repeating units. In yet an even further aspect, the peptide contains less than 30 sequential Ala-Ala-Thr repeating units. In a further aspect, the peptide contains less than 29 sequential Ala-Ala-Thr repeating units.In a still further aspect, the peptide contains less than 28 sequential Ala-Ala-Thr repeating units. In yet a further aspect, the peptide contains less than 27 sequential Ala-Ala-Thr repeating units. In an even further aspect, the peptide contains less than 26 sequential Ala-Ala-Thr repeating units. In a still even further aspect, the peptide contains less than 25 sequential Ala-Ala-Thr repeating units. In yet an even further aspect, the peptide contains less than 24 sequential Ala-Ala-Thr repeating units. In a further aspect, the peptide contains less than 23 sequential Ala-Ala-Thr repeating units. In a still further aspect, the peptide contains less than 22 sequential Ala-Ala-Thr repeating units. In yet a further aspect, the peptide contains less than 21 sequential Ala-Ala- Thr repeating units. In an even further aspect, the peptide contains less than 20 sequential Ala-Ala-Thr repeating units. In a still even further aspect, the peptide contains less than 19 sequential Ala-Ala-Thr repeating units. In yet an even further aspect, the peptide contains less than 18 sequential Ala-Ala-Thr repeating units. In a further aspect, the peptide contains less than 17 sequential Ala-Ala-Thr repeating units. In a still further aspect, the peptide contains less than 16 sequential Ala-Ala-Thr repeating units. In yet a further aspect, the peptide contains less than 15 sequential Ala-Ala-Thr repeating units. In an even further aspect, the peptide contains less than 14 sequential Ala-Ala-Thr repeating units. In a still even further aspect, the peptide contains less than 13 sequential Ala-Ala-Thr repeating units. In yet an even further aspect, the peptide contains less than 12 sequential Ala-Ala-Thr repeating units. In a further aspect, the peptide contains less than 11 sequential Ala-Ala-Thr repeating units. In a still further aspect, the peptide contains less than 10 sequential Ala-Ala-Thr repeating units. [00168] In various aspects, the peptide contains less than 36 sequential Ala-Ala-Ser repeating units. In a further aspect, the peptide contains less than 35 sequential Ala-Ala-Ser repeating units. In a still further aspect, the peptide contains less than 34 sequential Ala-Ala- Ser repeating units. In yet a further aspect, the peptide contains less than 33 sequential Ala- Ala-Ser repeating units. In an even further aspect, the peptide contains less than 32 sequential Ala-Ala-Ser repeating units. In a still even further aspect, the peptide contains less than 31 sequential Ala-Ala-Ser repeating units. In yet an even further aspect, the peptide contains less than 30 sequential Ala-Ala-Ser repeating units. In a further aspect, the peptide contains less than 29 sequential Ala-Ala-Ser repeating units.In a still further aspect, the peptide contains less than 28 sequential Ala-Ala-Ser repeating units. In yet a further aspect, the peptide contains less than 27 sequential Ala-Ala-Ser repeating units. In an even further aspect, the peptide contains less than 26 sequential Ala-Ala-Ser repeating units. In a still even further aspect, the peptide contains less than 25 sequential Ala-Ala-Ser repeating units. In yet an even further aspect, the peptide contains less than 24 sequential Ala-Ala-Ser repeating units. In a further aspect, the peptide contains less than 23 sequential Ala-Ala-Ser repeating units. In a still further aspect, the peptide contains less than 22 sequential Ala-Ala-Ser repeating units. In yet a further aspect, the peptide contains less than 21 sequential Ala-Ala- Ser repeating units. In an even further aspect, the peptide contains less than 20 sequential Ala-Ala-Ser repeating units. In a still even further aspect, the peptide contains less than 19 sequential Ala-Ala-Ser repeating units. In yet an even further aspect, the peptide contains less than 18 sequential Ala-Ala-Ser repeating units. In a further aspect, the peptide contains less than 17 sequential Ala-Ala-Ser repeating units. In a still further aspect, the peptide contains less than 16 sequential Ala-Ala-Ser repeating units. In yet a further aspect, the peptide contains less than 15 sequential Ala-Ala-Ser repeating units. In an even further aspect, the peptide contains less than 14 sequential Ala-Ala-Ser repeating units. In a still even further aspect, the peptide contains less than 13 sequential Ala-Ala-Ser repeating units. In yet an even further aspect, the peptide contains less than 12 sequential Ala-Ala-Ser repeating units. In a further aspect, the peptide contains less than 11 sequential Ala-Ala-Ser repeating units. In a still further aspect, the peptide contains less than 10 sequential Ala-Ala-Ser repeating units. [00169] In various aspects, the plurality of glycosylated residues are glycosylated threonine residues. [00170] In various aspects, the plurality of glycosylated residues are glycosylated serine residues. [00171] In various aspects, the plurality of glycosylated residues are a mixture of glycosylated threonine residues and glycosylated serine residues. [00172] In various aspects, the plurality of glycosylated residues are glycosylated with one or more of αGal, βGal, αGalNAc, βGalNAc, βGal(1→3)αGalNAc, αLac, and βLac. In a further aspect, the plurality of glycosylated residues are glycosylated with one or more of αGal, βGal, αGalNAc, βGalNAc, andr βGal(1→3)αGalNAc. In a further aspect, the plurality of glycosylated residues are glycosylated with one or more of αGal, βGal, αGalNAc, βGalNAc, αLac, and βLac. In a still further aspect, the plurality of glycosylated residues are glycosylated with one or more of αGal, βGal, βGal(1→3)αGalNAc, αLac, or βLac. In yet a further aspect, the plurality of glycosylated residues are glycosylated with one or more of αGal, βGal, and βGal(1→3)αGalNAc. In an even further aspect, the plurality of glycosylated residues are glycosylated with one or more of αGalNAc, βGalNAc, and βGal(1→3)αGalNAc. In a still further aspect, the plurality of glycosylated residues are glycosylated with one or more of βGal(1→3)αGalNAc, αLac, and βLac. In yet a further aspect, the plurality of glycosylated residues are glycosylated with one or more of αGal, βGal, αGalNAc, and βGalNAc. In an even further aspect, the plurality of glycosylated residues are glycosylated with one or more of αGal, βGal, αLac, and βLac. In a still further aspect, the plurality of glycosylated residues are glycosylated with one or more of αGalNAc, βGalNAc, αLac, and βLac. In yet a further aspect, the plurality of glycosylated residues are glycosylated with one or more of αGal and βGal. In an even further aspect, the plurality of glycosylated residues are glycosylated with one or more of αGalNAc and βGalNAc. In an even still further aspect, the plurality of glycosylated residues are glycosylated with βGal(1→3)αGalNAc. In a yet even further aspect, the plurality of glycosylated residues are glycosylated with one or more of αLac and βLac. [00173] In various aspects, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1. In a further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 19:11 to about 4:1. In a still further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 2:1 to about 4:1. In a yet further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 21:9 to about 4:1. In an even further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 11:4 to about 4:1. In an even still further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 23:7 to about 4:1. In an even yet further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 23:7 to about 4:1. In a further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 23:7. In a still further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 11:4. In a yet further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 21:9. In an even further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 2:1. In an even still further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 19:11. In an even yet further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 19:11 to about 23:7. In a further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 2:1 to about 11:4. In a still further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 21:9 to about 11:4. [00174] In various aspects, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is about 3:2. In a further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is about 19:11. In a still further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is about 2:1. In a yet further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is about 21:9. In an even further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is about 11:4. In an even still further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is about 23:7. In an even yet further aspect, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is about 4:1. [00175] In various aspects, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is not about 2:1. [00176] In various aspects, the ratio of the plurality of alanine residues to the plurality of glycosylated residues is about 1:1 or about 1:2. [00177] In various aspects, the peptide has a chain length of at least 30 amino acid residues. In a further aspect, the peptide has a chain length of at least 40 amino acid residues. In a still further aspect, the peptide has a chain length of at least 50 amino acid residues. In a yet further aspect, the peptide has a chain length of at least 60 amino acid residues. In an even further aspect, the peptide has a chain length of at least 70 amino acid residues. In an even still further aspect, the peptide has a chain length of at least 80 amino acid residues. In an even yet further aspect, the peptide has a chain length of at least 90 amino acid residues. In a further aspect, the peptide has a chain length of at least 100 amino acid residues. In a still further aspect, the peptide has a chain length of at least 110 amino acid residues. In a yet further aspect, the peptide has a chain length of at least 120 amino acid residues. In an even further aspect, the peptide has a chain length of at least 130 amino acid residues. In an even still further aspect, the peptide has a chain length of at least 140 amino acid residues. In even yet further aspect, the peptide has a chain length of at least 150 amino acid residues. In a further aspect, the peptide has a chain length of at least 160 amino acid residues. In a still further aspect, the peptide has a chain length of at least 170 amino acid residues. In a yet further aspect, the peptide has a chain length of at least 180 amino acid residues. In an even further aspect, the peptide has a chain length of at least 190 amino acid residues. In an even still further aspect, the peptide has a chain length of at least 200 amino acid residues. In an even yet further aspect, the peptide has a chain length of at least 210 amino acid residues. In a further aspect, the peptide has a chain length of at least 220 amino acid residues. In a still further aspect, the peptide has a chain length of at least 230 amino acid residues. In a yet further aspect, the peptide has a chain length of at least 240 amino acid residues. In an even further aspect, the peptide has a chain length of at least 250 amino acid residues. In an even still further aspect, the peptide has a chain length of at least 260 amino acid residues. In even yet further aspect, the peptide has a chain length of at least 270 amino acid residues. In a further aspect, the peptide has a chain length of at least 280 amino acid residues. In a still further aspect, the peptide has a chain length of at least 290 amino acid residues. In a yet further aspect, the peptide has a chain length of at least 300 amino acid residues. In an even further aspect, the peptide has a chain length of at least 310 amino acid residues. In an even still further aspect, the peptide has a chain length of at least 320 amino acid residues. In an even yet further aspect, the peptide has a chain length of at least 330 amino acid residues. In a further aspect, the peptide has a chain length of at least 330 amino acid residues. In a still further aspect, the peptide has a chain length of at least 340 amino acid residues. In a yet further aspect, the peptide has a chain length of at least 350 amino acid residues. In an even further aspect, the peptide has a chain length of at least 360 amino acid residues. In an even still further aspect, the peptide has a chain length of at least 370 amino acid residues. In even yet further aspect, the peptide has a chain length of at least 380 amino acid residues. In a further aspect, the peptide has a chain length of at least 390 amino acid residues. In a still further aspect, the peptide has a chain length of at least 400 amino acid residues. In a yet further aspect, the peptide has a chain length of at least 410 amino acid residues. In an even further aspect, the peptide has a chain length of at least 420 amino acid residues. In an even still further aspect, the peptide has a chain length of at least 430 amino acid residues. In an even yet further aspect, the peptide has a chain length of at least 440 amino acid residues. In a further aspect, the peptide has a chain length of at least 450 amino acid residues. In a still further aspect, the peptide has a chain length of at least 460 amino acid residues. In a yet further aspect, the peptide has a chain length of at least 470 amino acid residues. In an even further aspect, the peptide has a chain length of at least 480 amino acid residues. In an even still further aspect, the peptide has a chain length of at least 490 amino acid residues. In even yet further aspect, the peptide has a chain length of at least 500 amino acid residues. [00178] In various aspects, the peptide has a chain length of from about 30 amino acid residues to about 500 amino acid residues. In a further aspect, the peptide has a chain length of from about 50 amino acid residues to about 500 amino acid residues. In a still further aspect, the peptide has a chain length of from about 100 amino acid residues to about 500 amino acid residues. In a yet further aspect, the peptide has a chain length of from about 200 amino acid residues to about 500 amino acid residues. In an even further aspect, the peptide has a chain length of from about 300 amino acid residues to about 500 amino acid residues. In an even still further aspect, the peptide has a chain length of from about 40 amino acid residues to about 500 amino acid residues. In an even yet further aspect, the peptide has a chain length of from about 30 amino acid residues to about 400 amino acid residues. In a further aspect, the peptide has a chain length of from about 30 amino acid residues to about 300 amino acid residues. In a still further aspect, the peptide has a chain length of from about 30 amino acid residues to about 200 amino acid residues. In a yet further aspect, the peptide has a chain length of from about 30 amino acid residues to about 100 amino acid residues. In an even further aspect, the peptide has a chain length of from about 30 amino acid residues to about 50 amino acid residues. In an even still further aspect, the peptide has a chain length of from about 50 amino acid residues to about 400 amino acid residues. In even yet further aspect, the peptide has a chain length of from about 100 amino acid residues to about 300 amino acid residues. In a further aspect, the peptide has a chain length of from about about 50 residues to about 100 residues. In a still further aspect, the peptide has a chain length of from about 100 amino acid residues to about 150 amino acid residues. In a yet further aspect, the peptide has a chain length of from about 150 amino acid residues to about 200 amino acid residues. In an even further aspect, the peptide has a chain length of from about 200 amino acid residues to about 250 amino acid residues. In an even still further aspect, the peptide has a chain length of from about 250 amino acid residues to about 300 amino acid residues. In even yet further aspect, the peptide has a chain length of from about 300 amino acid residues to about 350 amino acid residues. In a further aspect, the peptide has a chain length of from about 350 amino acid residues to about 400 amino acid residues. In a still further aspect, the peptide has a chain length of from about 400 amino acid residues to about 450 amino acid residues. In a yet further aspect, the peptide has a chain length of from about 450 amino acid residues to about 500 amino acid residues. In an even further aspect, the peptide has a chain length of from about 125 amino acid residues to about 275 amino acid residues. In an even still further aspect, the peptide has a chain length of from about 150 amino acid residues to about 250 amino acid residues. In even yet further aspect, the peptide has a chain length of from about 175 amino acid residues to about 225 amino acid residues. [00179] In various aspects, the peptide has a number average molecular weight (M_n) of at least about 3,000. In a further aspect, the peptide has a number average molecular weight (M_n) of at least about 4,000. In a still further aspect, the peptide has a number average molecular weight (Mn) of at least about 5,000. In a yet further aspect, the peptide has a number average molecular weight (M_n) of at least about 6,000. In an even further aspect, the peptide has a number average molecular weight (Mn) of at least about 7,000. In an even still further aspect, the peptide has a number average molecular weight (M_n) of at least about 8,000. In an even yet further aspect, the peptide has a number average molecular weight (M_n) of at least about 9,000. In a further aspect, the peptide has a number average molecular weight (M_n) of at least about 10,000. In a still further aspect, the peptide has a number average molecular weight (M_n) of at least about 11,000. In a yet further aspect, the peptide has a number average molecular weight (M_n) of at least about 12,000. In an even further aspect, the peptide has a number average molecular weight (M_n) of at least about 13,000. In an even still further aspect, the peptide has a number average molecular weight (M_n) of at least about 14,000. In an even yet further aspect, the peptide has a number average molecular weight (M_n) of at least about 15,000. In a further aspect, the peptide has a number average molecular weight (Mn) of at least about 20,000. In a still further aspect, the peptide has a number average molecular weight (M_n) of at least about 25,000. In a yet further aspect, the peptide has a number average molecular weight (Mn) of at least about 30,000. In an even further aspect, the peptide has a number average molecular weight (M_n) of at least about 35,000. In an even still further aspect, the peptide has a number average molecular weight (M_n) of at least about 40,000. In an even yet further aspect, the peptide has a number average molecular weight (Mn) of at least about 45,000. In a further aspect, the peptide has a number average molecular weight (M_n) of at least about 50,000. [00180] In various aspects, the peptide has a number average molecular weight (Mn) of from about 3,000 to about 50,000. In a further aspect, the peptide has a number average molecular weight (Mn) of from about 5,000 to about 45,000. In a still further aspect, the peptide has a number average molecular weight (M_n) of from about 10,000 to about 40,000. In a yet further aspect, the peptide has a number average molecular weight (Mn) of from about 15,000 to about 35,000. In an even further aspect, the peptide has a number average molecular weight (Mn) of from about 20,000 to about 30,000. In an even still further aspect, the peptide has a number average molecular weight (M_n) of from about 3,000 to about 5,000. In an even yet further aspect, the peptide has a number average molecular weight (Mn) of from about 3,000 to about 10,000. In a further aspect, the peptide has a number average molecular weight (Mn) of from about 3,000 to about 15,000. In a still further aspect, the peptide has a number average molecular weight (M_n) of from about 3,000 to about 20,000. In a yet further aspect, the peptide has a number average molecular weight (Mn) of from about 3,000 to about 25,000. In an even further aspect, the peptide has a number average molecular weight (M_n) of from about 3,000 to about 30,000. In an even still further aspect, the peptide has a number average molecular weight (M_n) of from about 3,000 to about 35,000. In an even yet further aspect, the peptide has a number average molecular weight (M_n) of from about 30,000 to about 40,000. In a further aspect, the peptide has a number average molecular weight (M_n) of from about 3,000 to about 45,000. In a still further aspect, the peptide has a number average molecular weight (M_n) of from about 45,000 to about 50,000. In a yet further aspect, the peptide has a number average molecular weight (M_n) of from about 40,000 to about 50,000. In an even further aspect, the peptide has a number average molecular weight (M_n) of from about 35,000 to about 50,000. In an even still further aspect, the peptide has a number average molecular weight (M_n) of from about 30,000 to about 50,000. In an even yet further aspect, the peptide has a number average molecular weight (M_n) of from about 25,000 to about 50,000. In a further aspect, the peptide has a number average molecular weight (Mn) of from about 20,000 to about 50,000. In a still further aspect, the peptide has a number average molecular weight (Mn) of from about 15,000 to about 50,000. In a yet further aspect, the peptide has a number average molecular weight (M_n) of from about 10,000 to about 50,000. In an even further aspect, the peptide has a number average molecular weight (Mn) of from about 5,000 to about 50,000. In an even still further aspect, the peptide has a number average molecular weight (Mn) of from about 10,000 to about 30,000. In an even yet further aspect, the peptide has a number average molecular weight (M_n) of from about 12,000 to about 28,000. In a further aspect, the peptide has a number average molecular weight (Mn) of from about 14,000 to about 25,000. In a still further aspect, the peptide has a number average molecular weight (Mn) of from about 15,000 to about 23,000. In a yet further aspect, the peptide has a number average molecular weight (M_n) of from about 18,000 to about 22,000. In an even further aspect, the peptide has a number average molecular weight (Mn) of from about 19,000 to about 21,000. [00181] In various aspects, the peptide has a degree of polymerization (DP) of at least about 25. In a further aspect, the peptide has a degree of polymerization (DP) of at least about 30. In a still further aspect, the peptide has a degree of polymerization (DP) of at least about 40. In a yet further aspect, the peptide has a degree of polymerization (DP) of at least about 50. In an even further aspect, the peptide has a degree of polymerization (DP) of at least about 60. In an even still further aspect, the peptide has a degree of polymerization (DP) of at least about 70. In an even yet further aspect, the peptide has a degree of polymerization (DP) of at least about 80. In a further aspect, the peptide has a degree of polymerization (DP) of at least about 90. In a still further aspect, the peptide has a degree of polymerization (DP) of at least about 100. In a yet further aspect, the peptide has a degree of polymerization (DP) of at least about 110. In an even further aspect, the peptide has a degree of polymerization (DP) of at least about 112. In an even still further aspect, the peptide has a degree of polymerization (DP) of at least about 120. In even yet further aspect, the peptide has a degree of polymerization (DP) of at least about 130. In a further aspect, the peptide has a degree of polymerization (DP) of at least about 140. In a still further aspect, the peptide has a degree of polymerization (DP) of at least about 150. In a yet further aspect, the peptide has a degree of polymerization (DP) of at least about 160. In an even further aspect, the peptide has a degree of polymerization (DP) of at least about 170. In an even still further aspect, the peptide has a degree of polymerization (DP) of at least about 180. In an even yet further aspect, the peptide has a degree of polymerization (DP) of at least about 190. In a further aspect, the peptide has a degree of polymerization (DP) of at least about 200. In a still further aspect, the peptide has a chain length of at least 210 amino acid residues. In a yet further aspect, the peptide has a chain length of at least 220 amino acid residues. In an even further aspect, the peptide has a degree of polymerization (DP) of at least about 230. In an even still further aspect, the peptide has a degree of polymerization (DP) of at least about 240. In an even yet further aspect, the peptide has a degree of polymerization (DP) of at least about 250. In a further aspect, the peptide has a degree of polymerization (DP) of at least about 260. In a still further aspect, the peptide has a chain length of at least 270 amino acid residues. In a yet further aspect, the peptide has a chain length of at least 280 amino acid residues. In an even further aspect, the peptide has a chain length of at least 290 amino acid residues. In an even still further aspect, the peptide has a chain length of at least 300 amino acid residues. [00182] In various aspects, the peptide has a degree of polymerization (DP) from about 30 to about 500. In a further aspect, the peptide has a degree of polymerization (DP) from about 30 to about 450. In a still further aspect, the peptide has a degree of polymerization (DP) from about 30 to about 400. In a yet further aspect, the peptide has a degree of polymerization (DP) from about 30 to about 350. In an even further aspect, the peptide has a degree of polymerization (DP) from about 30 to about 300. In an even still further aspect, the peptide has a degree of polymerization (DP) from about 30 to about 250. In an even yet further aspect, the peptide has a degree of polymerization (DP) from about 30 to about 200. In a further aspect, the peptide has a degree of polymerization (DP) from about 30 to about 150. In a still further aspect, the peptide has a degree of polymerization (DP) from about 30 to about 100. In a yet further aspect, the peptide has a degree of polymerization (DP) from about 30 to about 50. In an even further aspect, the peptide has a degree of polymerization (DP) from about 50 to about 500. In an even still further aspect, the peptide has a degree of polymerization (DP) from about 100 to about 500. In an even yet further aspect, the peptide has a degree of polymerization (DP) from about 150 to about 500. In a further aspect, the peptide has a degree of polymerization (DP) from about 200 to about 500. In a still further aspect, the peptide has a degree of polymerization (DP) from about 250 to about 500. In a yet further aspect, the peptide has a degree of polymerization (DP) from about 300 to about 500. In an even further aspect, the peptide has a degree of polymerization (DP) from about 350 to about 500. In an even still further aspect, the peptide has a degree of polymerization (DP) from about 400 to about 500. In an even yet further aspect, the peptide has a degree of polymerization (DP) from about 450 to about 500. In a further aspect, the peptide has a degree of polymerization (DP) from about 50 to about 450. In a still further aspect, the peptide has a degree of polymerization (DP) from about 100 to about 400. In a yet further aspect, the peptide has a degree of polymerization (DP) from about 150 to about 350. In an even further aspect, the peptide has a degree of polymerization (DP) from about 200 to about 300. In an even still further aspect, the peptide has a degree of polymerization (DP) from about 50 to about 100. In an even yet further aspect, the peptide has a degree of polymerization (DP) from about 100 to about 150. In a further aspect, the peptide has a degree of polymerization (DP) from about 150 to about 200. In a still further aspect, the peptide has a degree of polymerization (DP) from about 200 to about 250. In a yet further aspect, the peptide has a degree of polymerization (DP) from about 250 to about 300. In an even further aspect, the peptide has a degree of polymerization (DP) from about 300 to about 350. In an even still further aspect, the peptide has a degree of polymerization (DP) from about 350 to about 400. In an even yet further aspect, the peptide has a degree of polymerization (DP) from about 400 to about 450. In a further aspect, the peptide has a degree of polymerization (DP) from about 100 to about 330. [00183] In various aspects, the peptide has a structure represented by a formula:

, wherein n is an integer selected from 15 to about 300; wherein R¹ is independently a monosaccharide moiety or a disaccharide moiety; wherein each occurrence of R² is independently selected from hydrogen and methyl, of x to y is of from about 3:2 to about 4:1; and wherein the sum of x and y is at least 30, or a pharmaceutically acceptable salt thereof. [00184] In various aspects, x is 18 or greater and y is 6 or greater. In a further aspect, x is 30 or greater and y is 10 or greater. In a still further aspect, x is 60 or greater and y is 20 or greater. In a yet further aspect, x is 90 or greater and y is 30 or greater. In an even further aspect, x is 120 or greater and y is 40 or greater. In an even still further aspect, x is 150 or greater and y is 50 or greater. In an even yet further aspect, x is 180 or greater and y is 60 or greater. In a further aspect, x is 210 or greater and y is 70 or greater. In a still further aspect, x is 240 or greater and y is 80 or greater. In a yet further aspect, x is 270 or greater and y is 90 or greater. In an even further aspect, x is 300 or greater and y is 100 or greater. In an even still further aspect, x is 330 or greater and y is 110 or greater. In an even yet further aspect, x is 360 or greater and y is 120 or greater. [00185] In various aspects, x is from 18 to 360 and y is from 6 to 120. In a further aspect, x is from 30 to 360 and y is from 10 to 120. In a still further aspect, x is from 60 to 360 and y is from 20 to 120. In a yet further aspect, x is from 90 to 360 and y is from 30 to 120. In an even further aspect, x is from 120 to 360 and y is from 40 to 120. In an even still further aspect, x is from 150 to 360 and y is from 50 to 120. In an even yet further aspect, x is from 180 to 360 and y is from 60 to 120. In a further aspect, x is from 210 to 360 and y is from 70 to 120. In a still further aspect, x is from 240 to 360 and y is from 80 to 120. In a yet further aspect, x is from 270 to 360 and y is from 90 to 120. In an even further aspect, x is from 330 to 360 and y is from 110 to 120. In an even still further aspect, x is from 18 to 330 and y is from 6 to 110. In an even yet further aspect, x is from 18 to 300 and y is from 6 to 100. In a further aspect, x is from 18 to 270 and y is from 6 to 90. In a still further aspect, x is from 18 to 240 and y is from 6 to 80. In a yet further aspect, x is from 18 to 210 and y is from 6 to 70. In an even further aspect, x is from 18 to 180 and y is from 6 to 60. In an even still further aspect, x is from 18 to 150 and y is from 6 to 50. In an even yet further aspect, x is from 18 to 120 and y is from 6 to 40. In a further aspect, x is from 18 to 90 and y is from 6 to 30. In a still further aspect, x is from 18 to 60 and y is from 6 to 20. In a yet further aspect, x is from 18 to 30 and y is from 6 to 10. In an even further aspect, x is from 18 to 180 and y is from 6 to 60. In an even still further aspect, x is from 18 to 150 and y is from 6 to 50. In an even yet further aspect, x is from 18 to 120 and y is from 6 to 40. In a further aspect, x is from 60 to 180 and y is from 20 to 120. [00186] In various aspects, the ratio of x to y is about 3:2 to about 4:1. In a further aspect, the ratio of x to y is about 19:11 to about 4:1. In a still further aspect, the ratio of x to y is about 2:1 to about 4:1. In a yet further aspect, the ratio of x to y is about 21:9 to about 4:1. In an even further aspect, the ratio of x to y is about 11:4 to about 4:1. In an even still further aspect, the ratio of x to y is about 23:7 to about 4:1. In an even yet further aspect, the ratio of x to y is about 23:7 to about 4:1. In a further aspect, the ratio of x to y is about 3:2 to about 23:7. In a still further aspect, the ratio of x to y is about 3:2 to about 11:4. In a yet further aspect, the ratio of x to y is about 3:2 to about 21:9. In an even further aspect, the ratio of x to y is about 3:2 to about 2:1. In an even still further aspectthe ratio of x to y is about 3:2 to about 19:11. In an even yet further aspect, the ratio of x to y is about 19:11 to about 23:7. In a further aspect, the ratio of x to y is about 2:1 to about 11:4. In a still further aspect, the ratio of x to y is about 21:9 to about 11:4. [00187] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00188] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00189] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00190] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00191] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00192] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00193] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00194] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00195] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00196] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00197] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00198] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00199] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00200] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00201] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00202] In various aspects, the peptide has a structure represented by a formula:

, wherein R²⁰ is selected from ‒OR³¹, ‒NHR³², ‒N3, a protein tag, a sortase recognition sequence, a sugar residue, and a structure:

; wherein R³¹ and R³² is selected from hydrogen, ‒CH2Ph, C1-C8 alkyl, C2-C8 alkyne, C1-C8 azide, tetrazinyl, cyclooctynyl, norbornenyl, and –(CH₂CH₂O)_mCH₃, and wherein m is an integer selected from 1 to 100. [00203] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00204] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00205] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00206] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00207] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00208] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00209] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00210] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00211] In various aspects, the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof. [00212] In one aspect, n is an integer selected from 15 to 300. In a further aspect, n is an integer selected from 15 to 250. In a still further aspect, n is an integer selected from 15 to 200. In a yet further aspect, n is an integer selected from 15 to 150. In an even further aspect, n is an integer selected from 15 to 100. In an even still further aspect, n is an integer selected from 15 to 50. In an even yet further aspect, n is an integer selected from 50 to 300. In a further aspect, n is an integer selected from 100 to 300. In a still further aspect, n is an integer selected from 150 to 300. In a yet further aspect, n is an integer selected from 200 to 300. In an even further aspect, n is an integer selected from 250 to 300. In an even still further aspect, n is an integer selected from 50 to 100. In an even yet further aspect, n is an integer selected from 100 to 150. In a further aspect, n is an integer selected from 150 to 200. In a still further aspect, n is an integer selected from 200 to 250. In a yet further aspect, n is an integer selected from 250 to 300. [00213] In one aspect, m is an integer selected from 1 to 100. In a further aspect, m is an integer selected from 2 to 100. In a still further aspect, m is an integer selected from 5 to 100. In a yet further aspect, m is an integer selected from 10 to 100. In an even further aspect, m is an integer selected from 20 to 100. In an even still further aspect, m is an integer selected from 30 to 100. In an even yet further aspect, m is an integer selected from 40 to 100. In a further aspect, m is an integer selected from 50 to 100. In a still further aspect, m is an integer selected from 60 to 100. In a yet further aspect, m is an integer selected from 70 to 100. In an even further aspect, m is an integer selected from 80 to 100. In an even still further aspect, m is an integer selected from 90 to 100. In an even yet further aspect, m is an integer selected from 1 to 90. In a further aspect, m is an integer selected from 1 to 80. In a still further aspect, m is an integer selected from 1 to 70. In a yet further aspect, m is an integer selected from 1 to 60. In an even further aspect, m is an integer selected from 1 to 50. In an even still further aspect, m is an integer selected from 1 to 40. In an even yet further aspect, m is an integer selected from 1 to 30. In a further aspect, m is an integer selected from 1 to 20. In a still further aspect, m is an integer selected from 1 to 10. In a yet further aspect, m is an integer selected from 1 to 5. In an even further aspect, m is an integer selected from 5 to 20. In an even still further aspect, m is an integer selected from 20 to 30. In an even yet further aspect, m is an integer selected from 30 to 40. In a further aspect, m is an integer selected from 40 to 50. In a still further aspect, m is an integer selected from 50 to 60. In a yet further aspect, m is an integer selected from 60 to 70. In an even further aspect, m is an integer selected from 70 to 80. In an even still further aspect, m is an integer selected from 80 to 90. [00214] In various aspects, m is an integer selected from 1, 2, 3, 4, 5, 6, 7, 8, 9, and 10. In a further aspect, m is an integer selected from 1, 2, 3, 4, 5, 6, 7, 8, and 9. In a still further aspect, m is an integer selected from 1, 2, 3, 4, 5, 6, 7, and 8. In a yet further aspect, m is an integer selected from 1, 2, 3, 4, 5, 6, and 7. In an even further aspect, m is an integer selected from 1, 2, 3, 4, 5, and 6. In an even still further aspect, m is an integer selected from 1, 2, 3, 4, and 5. In an even yet further aspect, m is an integer selected from 1, 2, 3, and 4. In a further aspect, m is an integer selected from 1, 2, and 3. In a still further aspect, m is an integer selected from 1 and 2. a. R¹ GROUPS [00215] In various aspects, each occurrence of R¹ is independently selected from a glucose moiety, an N-acetylglmannosamine moiety, a mannose moiety, an N-acetylglmannosamine moiety, a fucose moiety, a sialic acid moiety, a fructose moiety, a lactose moiety, a sucrose moiety, a glucuronic acid moiety, a manuronic acid moiety, a gulose moiety, a guloronic acid moiety, a xylose moiety, a ribose moiety, an allose moiety, an altrose moiety, an idose moiety, and a talose moiety. [00216] In various aspects, each occurrence of R¹ is independently a monosaccharide moiety or a disaccharide moiety having a structure represented by a formula:

^. [00217] In a further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

[00218] In a still further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

[00219] In a yet further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

^. [00220] In an even further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

. [00221] In an even still further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

[00222] In an even yet further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

[00223] In a further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

[00224] In a still further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

. [00225] In a yet further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

_, [00226] In an even further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

[00227] In an even still further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

[00228] In an even yet further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

[00229] In a further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

. [00230] In a still further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from: .

[00231] In a yet further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

[00232] In an even further aspect, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

. [00233] In various aspects, R¹ is a glycosyl moiety having a structure represented by a formula selected from:

b. R¹⁰ AND R¹¹ GROUPS [00234] In one aspect, each occurrence of R¹⁰ and R¹¹ is independently selected from ‒OH and ‒NHAc. In a further aspect, each occurrence of R¹⁰ and R¹¹ is ‒OH. In a still further aspect, each occurrence of R¹⁰ and R¹¹ is ‒NHAc. [00235] In various aspects, each occurrence of R¹⁰ is selected from ‒OH and ‒NHAc. In a further aspect, each occurrence of R¹⁰ is ‒OH. In a still further aspect, each occurrence of R¹⁰ is ‒NHAc. [00236] In various aspects, each occurrence of R¹¹ is selected from ‒OH and ‒NHAc. In a further aspect, each occurrence of R¹¹ is ‒OH. In a still further aspect, each occurrence of R¹¹ is ‒NHAc. c. R²⁰ GROUPS [00237] In one aspect, R²⁰ is selected from ‒OR³¹, ‒NHR³², ‒N3, a protein tag, a sortase recognition sequence, a sugar residue, and a structure:

. [00238] In various aspects, R²⁰ is selected from ‒OR³¹, ‒NHR³², ‒N₃, and a structure:

. [00239] In a further aspect, R²⁰ is selected from ‒OR³¹ and ‒NHR³². In a still further aspect, R²⁰ is ‒OR³¹. In a yet further aspect, R²⁰ is ‒NHR³². [00240] In various aspects, R²⁰ is ‒N3. [00241] In various aspects, R²⁰ is the protein tag. As would used herein, the term “protein tag” refers to a peptide sequence located at the N-terminus of the peptide (e.g., a peptide as disclosed herein) for a specific purpose. For example, a fluorescence tag can be used to give visueal readout on the peptide. Exemplary fluorescence tags include, but are not limited to, green fluorescent protein (GFP) and red fluorescent protein. Alternatively, a protein tag can be used to allow for specific enzymatic modification (such as biotinylation by a biotin ligase) or chemical modification (such as coupling to other protein). In various further aspects, the protein tag is selected from a polyglutamate tag, a polyarginine tag, a calmodulin-tag, CBP, FLAG, GST, HA, HBH, MBP, Myc, poly His, S-tag, SUMO, TAP, TRX, and V5. [00242] In various aspects, R²⁰ is the sortase recognition sequence. As used herein, the term “sortase recognition sequence” refers to a sequence located at the N-terminus of the peptide (e.g., a peptide as disclosed herein) that is recognized by a sortase (a bacterial transpeptidase) and is subsequently cleaved. A sortase recognition sequence can be used, for example, to allow for sortase-mediated ligation to generate site-specifically modified proteins utilizing sortase transpeptides. In various further aspects, the sortase recognition sequence is selected from LPXTG (SEQ ID NO: 1), LPXTGG (SEQ ID NO: 2), LPXTGGG (SEQ ID NO: 3), and LPXTGGGG (SEQ ID NO: 4), wherein X is a natural or unnatural amino acid. Examples of natural amino acids include, but are not limited to, serine, threonine, asparagine, glutamine, cysteine, selenocysteine, glycine, proline, alanine, valine, isoleucine, leucine, methionine, phenylalanine, tyrosine, and tryptophan. Examples of unnatural amino acids include, but are not limited to, hydroxyproline, beta-alanine, citrulline, ornithine, norleucine, 3-nitrotyrosine, nitroarginine, and pyroglutamic acid. In various further aspects, the sortase recognition sequence is selected from LPETG (SEQ ID NO: 5), LPETGG (SEQ ID NO: 6), LPETGGG (SEQ ID NO: 7), and LPETGGGG (SEQ ID NO: 8). [00243] In various aspects, R²⁰ is the sugar residue. As used herein, the term “sugar residue” refers to the portion of a monosaccharide or a polysaccharide that remains after the monosaccharide or the polysaccharide is covalently attached to, for example, the N-terminus of the peptide (e.g., a peptide as disclosed herein). Thus, in various aspects, the sugar residue can refer to the sugar minus an atom such as, for example, a proton. In various aspects, the sugar residue is a residue of a sugar selected from fructose, glucose, and lactose. In a further aspect, the sugar residue is a residue of a sugar selected from fructose and glucose. In a still further aspect, the sugar residue is a residue of a sugar selected from fructose and lactose. In a yet further aspect, the sugar residue is a residue of a sugar selected from glucose and lactose. In an even further aspect, the sugar residue is a fructose residue. In an even still further aspect, the sugar residue is a glucose residue. In an even yet further aspect, the sugar residue is a lactose residue. [00244] In various aspects, R²⁰ is a structure:

. d. R³¹ AND R³² GROUPS [00245] In various aspects, R³¹ and R³² are selected from hydrogen, ‒CH2Ph, C1-C8 alkyl, C2-C8 alkyne, C1-C8 azide, tetrazinyl, cyclooctynyl, norbornenyl, and –(CH2CH2O)mCH3. In a further aspect, R³¹ and R³² is selected from hydrogen, ‒CH2Ph, C1-C4 alkyl, C2-C4 alkyne, C1-C4 azide, tetrazinyl, cyclooctynyl, norbornenyl, and –(CH2CH2O)mCH3. In a still further aspect, R³¹ and R³² is selected from hydrogen, ‒CH2Ph, methyl, ethyl, propyl, isopropyl, ‒CH≡CH, ‒CH2CH≡CH, ‒CH2N3, ‒CH2CH2N3, ‒CH2CH2CH2N3, tetrazinyl, cyclooctynyl, norbornenyl, and –(CH2CH2O)mCH3. In a yet further aspect, R³¹ and R³² is selected from hydrogen, ‒CH2Ph, methyl, ethyl, ‒CH≡CH, ‒CH2N3, ‒CH2CH2N3, tetrazinyl, cyclooctynyl, norbornenyl, and –(CH₂CH₂O)_mCH₃. In an even further aspect, R³¹ and R³² is selected from hydrogen, ‒CH₂Ph, methyl, ‒CH₂N₃, tetrazinyl, cyclooctynyl, norbornenyl, and –(CH2CH2O)mCH3. [00246] In various aspects, R³¹ and R³² is selected from hydrogen, ‒CH₂Ph, C1-C8 alkyl, and C2-C8 alkyne. In a further aspect, R³¹ and R³² is selected from hydrogen, ‒CH2Ph, C1-C4 alkyl, and C2-C4 alkyne. In a still further aspect, R³¹ and R³² is selected from hydrogen, ‒CH2Ph, methyl, ethyl, propyl, isopropyl, ‒CH≡CH, and ‒CH2CH≡CH. In a yet further aspect, R³¹ and R³² is selected from hydrogen, ‒CH₂Ph, and methyl. In an even further aspect, R³¹ and R³² is selected from hydrogen and methyl. [00247] In various aspects, R³¹ and R³² is selected from hydrogen and C1-C8 azide. In a further aspect, R³¹ and R³² is selected from hydrogen and C1-C4 azide. In a still further aspect, R³¹ and R³² is selected from hydrogen, ‒CH₂N₃, ‒CH₂CH₂N₃, ‒CH₂CH₂CH₂N₃. In a yet further aspect, R³¹ and R³² is selected from hydrogen, ‒CH2N3, ‒CH2CH2N3. In an even further aspect, R³¹ and R³² is selected from hydrogen and ‒CH₂N₃. [00248] In various aspects, R³¹ and R³² is selected from hydrogen, tetrazinyl, cyclooctynyl, and norbornenyl. In a further aspect, R³¹ and R³² is selected from hydrogen and tetrazinyl. In a still further aspect, R³¹ and R³² is selected from hydrogen and cyclooctynyl. In a yet further aspect, R³¹ and R³² is selected from hydrogen and norbornenyl. [00249] In various aspects, R³¹ and R³² is selected from hydrogen and –(CH2CH2O)mCH3. [00250] In various aspect, v is selected from hydrogen and C1-C8 alkyl. In a further aspect, R³¹ and R³² is selected from hydrogen and C1-C4 alkyl. In a still further aspect, R³¹ and R³² is selected from hydrogen, methyl, ethyl, propyl and isopropyl. In a yet further aspect, R³¹ and R³² is selected from hydrogen, methyl, and ethyl. In an even further aspect, R³¹ and R³² is selected from hydrogen and methyl. [00251] In various aspects, R³¹ and R³² is hydrogen. 2. E^XAMPLE P^EPTIDES [00252] In one aspect, a peptide can be present as one or more of the following structures:

, ,

,

, ,

,

o

, or a pharmaceutically acceptable salt thereof. [00253] In one aspect, a peptide can be present as one or more of the following structures:

, ,

,

, ,

,

or a pharmaceutically acceptable salt thereof. [00254] It is contemplated that one or more peptides can optionally be omitted from the disclosed invention. [00255] It is understood that the disclosed peptides can be used in connection with the disclosed methods, compositions, food products, solid or semi-solid supports, kits, and uses. [00256] It is understood that pharmaceutically acceptable derivatives of the disclosed peptides can be used also in connection with the disclosed methods, compositions, food products, solid or semi-solid supports, kits, and uses. The pharmaceutically acceptable derivatives of the peptides can include any suitable derivative, such as pharmaceutically acceptable salts as discussed below, isomers, radiolabeled analogs, tautomers, and the like. C. M^{ETHODS OF} M^{AKING A} P^EPTIDE [00257] The peptides of the invention can be prepared by employing reactions as shown in the following schemes, in addition to other standard manipulations that are known in the literature, exemplified in the experimental sections or clear to one skilled in the art. For clarity, examples having a single substituent are shown where multiple substituents are allowed under the definitions disclosed herein. [00258] Reactions used to generate the peptides of the invention are prepared by employing reactions as shown in the following Reaction Schemes, as described and exemplified below. In certain specific examples, the disclosed peptides can be prepared by Routes I-II, as described and exemplified below. The following examples are provided so that the invention might be more fully understood, are illustrative only, and should not be construed as limiting. 1. ROUTE I [00259] In one aspect, substituted glycosylated threonine or glycosylated serine analogs can be prepared as shown below. SCHEME 1A.

[00260] Peptides are represented in generic form, wherein PG¹ is a carboxylic acid protecting group such as, for example, benzyl, PG² is an amine protecting group such as, for example, benzyl or carbobenzyloxy, and R’ is an alkyl group such as, for example, methyl, ethyl, propyl, isopropyl, butyl, isobutyl, or tert-butyl, and with other substituents as noted in compound and peptide descriptions elsewhere herein. A more specific non-limiting example of the synthesis shown in Scheme 1A is set forth below. S^CHEME 1B.

[00261] In one aspect, compounds of type 1.14, and similar compounds, can be prepared according to reaction Scheme 1B above. Thus, compounds of type 1.10 can be prepared by glycosyl coupling of an appropriate hydroxyl protected substituted aminoacid, e.g., 1.8 as shown above, using an appropriate protected glycosyl residue, e.g., 1.9 as shown above. Appropriate protected hydroxyl substituted amino acids and appropriate protected glycosyl residues are commercially available or prepared by methods known to one skilled in the art. The coupling is carried out in the presence of an appropriate Lewis acid, e.g., boron trifluoride diethyl etherate, in an appropriate solvent, e.g., dichloromethane, at an appropriate temperature, e.g., 0 °C to room temperature, for an appropriate amount of time, e.g., overnight. Compounds of type 1.11 can be prepared by deprotection of an appropriate protected amino acid, e.g., 1.10 as shown above. The deprotection reaction is carried out in the presence of an appropriate deprotecting reagent, e.g., hydrogen gas, in the presence of an appropriate catalyst, e.g., 10 % palladium on carbon, in an appropriate solvent, e.g., methanol. Compounds of type 1.13 can be prepared by reaction of an appropriate dialkyl dicarbonate, e.g., 1.12 as shown above, with an appropriate amino acid, e.g., 1.11 as shown above. Appropirate dialkyl dicarbonates are commercially available or prepared by methods known to one skilled in the art. The reaction is carried out in the presence of an appropriate base, e.g., sodium bicarbonate, in an appropriate solvent system, e.g., tetrahydrofuan and water, at an appropriate temperature, e.g., 0 °C. Compounds of type 1.14 can be prepared by cyclization of an appropriate carbamate protected amino acid, e.g., 1.13 as shown above. The reaction is carried out in the presence of an appropriate carboxyl activating agent, e.g., triphosgene, and an appropriate base, e.g., triethylamine, in the presence of an appropriate chloride scavenger, e.g., epichlorohydrin, in an appropriate solvent, e.g., tetrahydrofuan, at an appropriate temperature, e.g., room temperature. As can be appreciated by one skilled in the art, the above reaction provides an example of a generalized approach wherein compounds similar in structure to the specific reactants above (compounds similar to compounds of type 1.1, 1.2, 1.3, 1.4, 1.5, and 1.6), can be substituted in the reaction to provide glycosylated threonine analogs similar to Formula 1.7. 2. ROUTE II [00262] In one aspect, peptide analogs can be prepared as shown below. S^CHEME 2A.

[00263] Peptides are represented in generic form, with substituents as noted in compound and peptide descriptions elsewhere herein. A more specific non-limiting example of the synthesis shown in Scheme 2A is set forth below.

[00264] In one aspect, compounds of type 2.7, and similar compounds, can be prepared according to reaction Scheme 2B above. Thus, compounds of type 2.7 can be prepared by NCA copolymerization of an appropriate glycosylated threonine or glycosylated serine analogs, e.g., 2.5 as shown above, and an alanine-N-carboxy anhydride, e.g., 2.4 as shown above. Alanine-N-carboxy anhydride is commercially available or prepared by methods known to one skilled in the art. Degrees of polymerization can be readily tuned by altering the monomer to initiator ratios, and amino acid compositions can be tuned via the amino acid N-carboxy anhydride feed ratios, as further detailed herein. The polymerization is carried out in the presence of an catalyst, e.g., tetrakis(trimethylphosphine)cobalt, in an appropriate solvent, e.g., tetrahydrofuran, at an appropriate temperature, e.g., 0 °C. Subsequent acetyl group deprotection was carried out in the presence of an appropriate base, e.g., potassium carbonate, in an appropriate solvent system, e.g., methanol and water. As can be appreciated by one skilled in the art, the above reaction provides an example of a generalized approach wherein compounds similar in structure to the specific reactants above (compounds similar to compounds of type 2.1, 2.2, and 2.3), can be substituted in the reaction to provide peptide analogs similar to Formula 2.4. D. COMPOSITIONS [00265] As detailed herein, the disclosed peptides are useful in a wide range of applications, including, but not limited to biomedical cryopreservation, agriculture, and cosmetics. Thus, in various aspects, the disclosed peptides can be formulated into a composition (e.g., a cryoprotectant composition, an agricultural composition, a cosmetic composition) to facilitate use in these areas. [00266] In various aspects, the disclosed composition reduces or inhibits ice crystal formation at a temperature of from about 0 °C to about -20 °C (e.g., at about 0, -1, -2, -3, -4, - 5, -6, -7, -8, -9, -10, -11, -12, -13, -14, -15, -16, -17, -18, -19, or -20 °C). In a further aspect, the disclosed composition reduces or inhibits ice crystal formation at a temperature of from about -20 °C to about -40 °C (e.g., at about -20, -21, -22, -23, -24, -25, -26, -27, -28, -29, -30, -31, -32, -33, -34, -35, -36, -37, -38, -39, or -40 °C). In a still further aspect, the disclosed composition reduces or inhibits ice crystal formation at about -20 °C. In yet a further aspect, the disclosed composition reduces or inhibits ice crystal formation at a temperature of from about -40 °C to about -200 °C (e.g., at about -40, -45, -50, -55, -60, -65, -70, -75, -80, -85, - 90, -95, -100, -105, -110, -115, -120, -125, -130, -135, -140, -145, -150, -155, -160, -165, - 170, -175, -180, -185, -190, -195, or -200 °C). In an even further aspect, the disclosed composition reduces or inhibits ice crystal formation at about -196 °C. [00267] In various aspects, the disclosed composition reduces or inhibits ice crystal formation at a temperature from about 0 °C to about -200 °C, from about -10 °C to about - 190 °C, from about -20 °C to about -180 °C, from about -30 °C to about -170 °C, from about -40 °C to about -160 °C, from about -50 °C to about -150 °C, from about -60 °C to about - 140 °C, from about -70 °C to about -140 °C, from about -80 °C to about -130 °C, from about -90 °C to about -120 °C, or from about -100 °C to about -110 °C. [00268] In various aspects, the disclosed composition comprises the peptide in a concentration of from about 100 nM to about 1,000 mM. In a further aspect, the disclosed composition comprises the peptide in a concentration of from about 100 nM to about 250 nM, from about 250 nM to about 500 nM, from about 500 nM to about 750 nM, from about 750 nM to about 1 μM, from about 1 μM to about 5 μM, from about 5 μM to about 25 μM, from about 25 μM to about 50 μM, from about 50 μM to about 100 μM, from about 100 μM to about 250 μM, from about 250 μM to about 500 μM, from about 500 μM to about 750 μM, from about 750 μM to about 1 mM, from about 1 mM to about 10 mM, from about 10 mM to about 50 mM, from about 50 mM to about 100 mM, from about 100 mM to about 250 mM, from about 250 mM to about 500 mM, from about 500 mM to about 750 mM, or from about 750 mM to about 1,000 mM. In a still further aspect, the disclosed composition comprises the peptide in a concentration of about 100 nM, about 1 μM, about 10 μM, about 100 μM, about 1 mM, about 10 mM, about 100 mM, or about 1,000 mM. In yet a further aspect, the disclosed composition comprises the peptide in a concentration of about 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 20, 30, 40, 50, 60, 70, 80, 90, or 100 mM. [00269] It is understood that the disclosed compositions can be prepared from the disclosed peptide. It is also understood that the disclosed compositions can be employed in the disclosed methods of using. 1. C^{RYOPROTECTANT} C^OMPOSITIONS [00270] In one aspect, disclosed are cryoprotectant compositions comprising an effective amount of a disclosed peptide and one or more selected from: (a) a non-antifreeze protein; (b) a microbe; (c) a cell component; and (d) a cell. In a further aspect, the peptide comprises a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, and wherein the peptide has a chain length of at least 30 amino acid residues, and one or more selected from: (a) a non-antifreeze protein; (b) a microbe; (c) a cell component; and (d) a cell. [00271] As detailed herein, the disclosed peptides are useful in preventing or reducing damage caused by ice creation and ice recrystallization in a composition requiring cryoprotection. Thus, in various aspects, the disclosed peptides can be formulated into a cryoprotectant composition. As used herein, the term “cryoprotectant” refers to the ability of a composition (e.g., a cryoprotectant composition as disclosed herein) to protect a sample such as, for example, a biological sample (e.g., a non-antifreeze protein, a microbe, a cell component, or a cell) from freezing and/or from damage that occurs during freezing (e.g., due to ice formation). [00272] Cryopreservation is a process whereby a sample (e.g., a biological sample) is preserved by cooling to sub-zero temperatures. At these low temperatures, any biological activity, including the biochemical reactions is slowed or stopped. For cryopreservation to be useful, the preserved sample should retain the integrity and viability to a reasonable level at the time of harvest. Thus, the process of preserving cells or tissue should preferably not, in itself, severely damage or destroy for example the cells or tissue architecture. However, it is known that upon freezing cells or tissue that ice crystals may form. [00273] In conventional cryopreservation techniques, the cells or tissue are placed in a storage solution, and then preserved by freezing. When the sample is to be used, it is thawed, and then placed in a cell culture medium. Cryopreservation protocols subject the cells to a multitude of stresses and insults throughout the process of cell harvesting, freezing, and thawing. These stresses and insults can cause irreversible damage to the cell. Therefore, in order for the cells or tissues to be preserved, cryoprotectant compositions are typically used to prevent damage due to freezing during the cooling or thawing process. [00274] To effect the desired cryoprotectant properties, the disclosed cryoprotectant composition can be applied directly to the sample as a pre-treatment (e.g., before storing), applied at an additional timepoint during freezing, and/or prior to thawing. In various further aspects, the cryoprotectant composition can be applied to the sample before freezing. In various further aspects, the cryoprotectant composition can be applied to the sample during freezing. In various further aspects, the cryoprotectant composition can be applied to the sample after freezing but prior to thawing. In various further aspects, the cryoprotectant composition can be applied to the sample at multiple timepoints (e.g., before, during, and/or after freezing). [00275] The disclosed cryoprotectant composition can be formulated as a non-freezing liquid (e.g., an aqueous solution or a non-aqueous solution), a non-freezing gel, a non-freezing hydrogel, or a non-freezing paste. The cryoprotectant composition can be hygroscopic, thermally conductive, and/or biocompatible. In various aspects, the cryoprotectant composition can be formulated to be acoustically transparent such as, for example, to allow ultrasound to pass through the cryoprotectant compositions such as, for example, a water- based gel as described in US 4,002,221 and US 4,459,854. [00276] In various aspects, the cryoprotectant composition comprises a non-antifreeze protein. As used herein, the term “non-antifreeze protein” refers to proteins that are not recognized to have properties of ice recrystallization inhibition or ice crystal shaping. Thus in various aspects, the non-antifreeze protein is selected from an enzyme, a hormone, an antibody, a growth factor, a vaccination protein, a therapeutic protein, or a nutrient protein. Additional examples of a non-antifreeze protein include, but are not limited to, egg albumin, bovine serum albumin, human serum albumin, and gelatin. [00277] In various aspects, the cryoprotectant composition comprises a microbe. As used herein, the term “microbe” means a microorganism that can exist in a single-celled form or as a colony of cells. Examples of microbes include, but are not limited to viruses, bacteria, archaea, fungi, protists, protozoa, algae, amoebas, and slime molds. [00278] In various aspects, the cryoprotectant composition comprises a cell component. As used herein, the term “cell component” refers to the biomolecules and structures of which cells are composed. Examples of cell components include, but are not limited to, a nucleolus, a nucleus, a ribosome, a vesicle, a rough endoplasmic reticulum, a Golgi apparatus, a cytoskeleton, a smooth endoplasmic reticulum, a mitochondria, a vacuole, a cytosol, a lysosome, and a centriole. [00279] In various aspects, the cryoprotectant composition comprises a cell. As used herein, the term “cell” means the smallest, most basic basic membrane-bound unit that contains the fundamental molecules of life. Examples of cells include, but are not limited to, stem cells, bone cells, blood cells, muscle cells, sperm cells, female egg cells, fat cells, and nerve cell. Additional examples of cells include, but are not limited to, liver tissue or hepatocytes, kidney, intestine, heart, pancreas, genitourinary cells (e.g., sperm cells, oocytes), corpus cavernosum cells (e.g., smooth muscle corpus cavernosum cells, epithelial corpus cavernosum cells), urinary bladder cells, urethral cells, ureter cells, kidney cells, testicular cells), bone marrow, primary cells, organoids, and other biological cells and tissues for cryopreservation. [00280] The disclosed cyroprotectant composition can also contain various additives including, but not limited to, a freezing point depressant, a thickening agent, a pH buffer, a humectant, a surfactant, and/or other additives configured to provide the desired cryoprotectant properties to the composition. [00281] In various aspects, the cryoprotectant composition further comprises a freezing point depressant. Examples of freezing point depressants include, but are not limited to, propylene glycol (PG), polyethylene glycol (PEG), polypropylene glycol (PPG), ethylene glycol, dimethyl sulfoxide (DMSO), combinations thereof, and other glycols. The freezing point depressant can also include ethanol, propanol, iso-propanol, butanol, and/or other suitable alcohol compounds. Certain freezing point depressants (e.g., PG, PPG, PEG, etc.) can also be used to improve spreadability of the cryoprotectant and to provide lubrication. As would be understood by one of ordinary skill in the art, the freezing point depressant can lower the freezing point of a sample (e.g., a biological sample) to from about 0 °C to about -40 °C. In various aspects, the freezing point of a solution can be lowered to from about -10 °C to about -20 °C, to from about -10 °C to about -18 °C, or to from about -10 °C to about -15 °C. In various aspects, the freezing point of a sample can be lowered to a temperature less than about 0 °C, less than about -5 °C, less than about -10 °C, less than about -12 °C, less than about -15 °C, less than about -16 °C, less than about -17 °C, less than about -18 °C, less than about -19 °C, or less than about -20 °C. For example, the freezing point depressant can lower the freezing point of a sample (e.g., a biological sample) to a temperature of less than about - 20 °C to about -25 °C, less than about -20 °C to about -30 °C, less than about -25 °C to about -35 ° C, or less than about -30 °C to about -40 °C. [00282] In various aspects, the cryoprotectant composition further comprises a thickening agent. Examples of thickening agents include, but are not limited to, carboxyl polyethylene polymer, hydroxyethyl xylose polymer, carboxyl methylcellulose, hydroxyethyl cellulose (HEC), and/or other viscosity modifiers, and can be used to provide a viscosity in the range of about 1 cP to about 10,000 cP. In various aspects, the thickening agent can provide a viscosity in the range of about 4,000 cP to about 8,000 cP. In a further aspect, the thickening agent can provide a viscosity in the range of about 5,000 cP to about 7,000 cP. Other viscosities can be achieved, if needed or desired. In various embodiments, a cryoprotectant composition having a viscosity in one or more of these ranges can readily adhere to a treatment device, the surface of the sample, the skin of a subject, and/or the interface between the treatment device and the skin of the subject during treatment. [00283] In various aspects, the cryoprotectant composition further comprises a pH buffer. Examples of pH buffers include, but are not limited to, cholamine chloride, cetamide, glycine, tricine, glycinamide, bicine, and/or other suitable pH buffers. In various aspects, the pH buffer can help the cryoprotectant composition to have a consistent pH of from about 3.5 to about 11.5. In a further aspect, the pH is of from about 5 to about 9.5. In a still further aspect, the pH is of from about 6 to about 7.5. In yet a further aspect, the pH of the cryoprotectant composition is within ±2 or ±1 of the pH of the sample. [00284] In various aspects, the cryoprotectant composition further comprises a humectant. Examples of humectants include, but are not limited to, glycerin, alkylene glycol, polyalkylene glycol, propylene glycol, glyceryl triacetate, polyols (e.g., sorbitol and/or maltitol), polymeric polyols (e.g., polydextrose), quillaia, lactic acid, and/or urea. In various aspects, the humectant can promote the retention of water to prevent the cryoprotectant composition from drying out. [00285] In various aspects, the cryoprotectant composition further comprises a surfactant. Examples of surfactants include, but are not limited to, sodium dodecyl sulfate, ammonium lauryl sulfate, sodium lauryl sulfate, alkyl benzene sulfonate, sodium lauryl ether sulfate, and other suitable surfactants. In various aspects, the surfactant can promote easy spreading of the cryoprotectant composition when an operator applies the cryoprotectant to a sample (e.g., a biological sample). [00286] The cryoprotectant may also include other additives in addition to or in lieu of the composition components described above. For example, some of the embodiments of cryoprotectant compositions may also include a coloring agent, fragrance or perfume, emulsifier, stabilizer, an anesthetic agent, and/or other ingredient. 2. A^GRICULTURAL C^OMPOSITIONS [00287] In one aspect, disclosed are agricultural compositions comprising a disclosed peptide. In a further aspect, the peptide comprises a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, and wherein the peptide has a chain length of at least 30 amino acid residues. In various aspects, the agricultural composition is a cryoprotectant agricultural composition. [00288] As used herein, the term “agricultural compositions” refers to compositions used treat agriculture products to increase food production and decrease the amount damage caused by environmental stress due to low temperatures near freezing. Non-limiting examples of agriculture products include grains, feeds, soybeans, tree nuts, fruits, and vegetables. [00289] Frost is a major environmental stress caused by low temperature combined with dewpoints below freezing points (≤ 0°C), posing substantial economic threat on plants. At the organ level, the damage occurs when water within plant tissues freezes, forming extracellular ice crystals that result in cell dehydration. Freezing-induced cellular dehydration is the predominant cause of damage in which the cell membranes are disrupted when the dehydration exceeds cell dehydration-tolerance. Even a brief frost event persisting only for a few hours can cause substantial damage to various crops. Thus, agricultural compositions such as, for example, agricultural compositions having cryoprotective properties can beneficially reduce, minimize, and otherwise prevent damage to plants due to frost. [00290] Additionally, many tropical and subtropical species of plants are in danger of extinction due to climate change and abiotic stress. Cryopreservation is a promising long- term technique to preserve the germplasms of these species. However, tropical species are temperature delicate. Thus, cryoprotectant agricultural compositions that can increase the explant’s tolerance to low temperatures and/or enable the plant cells to withstand freezing are desirable. [00291] As detailed herein, the resistance of plants and plant tissue to frost and low temperatures, including subfreezing temperatures, can be increased via application of an agricultural composition (e.g., a disclosed agricultural composition). For example, the agricultural composition can be sprayed onto the plants to be treated using a plant spray apparatus suitable for spraying aqueous solutions. The plants to be treated are thoroughly sprayed so that all of the plant tissue surfaces are completely covered. Due to the size or shape of a plant, a single application may require two or more sprayings. Alternatively, the plant can be dipped directly into the composition. [00292] In various aspects, the agricultural composition further comprises a non-ionic surfactant, which can help to ensure that the entire surface of the plant is coated with the compositions. Examples of non-ionic surfactants that may be useful for this purpose include, but are not limited to polyoxyethylene sorbitan monolaurate (Tween 20) and polyoxyethylene sorbitan monooleate (Tween 80). In various aspects, the agricultural composition comprises from about 0.01 wt% to about 0.5 wt%, 0.05 wt% to about 0.5 wt%, 0.1 wt% to about 0.5 wt%, 0.01 wt% to about 0.1 wt%, 0.01 wt% to about 0.05 wt%, or 0.05 wt% to about 0.1 wt% of the non-ionic surfactant. [00293] Additional agents that can be used in the disclosed agricultural composition include, but are not limited to, organic/inorganic fertilizers, pesticides, plant hormones, growth regulators, other polymers, and various coating materials. In various aspects, the disclosed agricultural composition does not include a pesticide. [00294] Although the disclosed agricultural composition can be applied to the plants immediately prior to exposure to freezing conditions, it is also envisioned that the composition can be applied much earlier such as, for example, from about 4 hours to about 1 week prior to exposure to freezing conditions. In various aspects, the disclosed agricultural composition can be applied more than once before onset of the freezing temperatures, the first application being made from about several days to about one week prior to the onset of freezing temperatures and constituting a conditioning application. The second (or subsequent) application is then made a sufficient period prior to the onset of freezing temperatures to permit absorption of the composition, e.g., at least about 4 hours. [00295] In various aspects, the disclosed agricultural composition can be applied regularly such as, for example, on a yearly basis, on a monthly basis, on a weekly basis, or even on a daily basis, in order to minimize any damage that might be caused by a sudden occurrence of freezing temperatures. Alternatively, the disclosed agricultural composition can be applied immediately before the exposure to freezing temperatures if the plant can to tolerate a high concentration of the agent. 3. COSMETIC COMPOSITIONS [00296] In one aspect, disclosed are cosmetic compositions comprising a disclosed peptide. In a further aspect, the peptide comprises a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, and wherein the peptide has a chain length of at least 30 amino acid residues. [00297] When cosmetics containing an oil component and a fat component are frozen, water contained in the cosmetics can become crystallized. As a result, the oil component and the fat component are physically pressed and the structure thereof is destroyed, causing the quality of the cosmetics to become deteriorated. The degradation of quality and the like can be avoided by incorporation of a disclosed peptide (i.e., to form a disclosed cosmetic composition) since crystallization of water can be prevented and the structure of oil component and fat component can be maintained. [00298] In addition, the disclosed cosmetic compositions can also be formulated to penetrate skin, thereby reducing the risk of ice nucleation and protecting the tissue's cells if ice formation does occur. Such applications can increase the resistance of human skin to frostbite, for example, at temperatures near or below 0 °C, and can minimize the resulting damage if cellular freezing does occur. [00299] Methods of applying a cosmetic composition are well-known in the art and include, for example, application by hand, by spraying, or in conjunction with an occlusive backing such as in an adhesive patch. The formulation should be sufficiently viscous to remain on the skin for an extended period of time, to allow for maximum protection to be achieved. [00300] In various aspects, the cosmetic composition is a skin care product. Thus, in various further aspects, the cosmetic composition is a topical formulation. Examples of topical formulations include, but are not limited to, creams, serums, gels, solutions, aerosols, ointments, sprays, lotions, and patches. [00301] Topical cosmetic compositions can be co-formulated to include inhibitors of apoptosis or reperfusion injury, and additional cryoprotectants such as glycerol, dimethylsulfoxide (DMSO), and/or low molecular weight sugars. The formulation can also include a variety of optional additives including, but not limited to, wetting agents, fragrances, and/or preservatives. E. FOOD PRODUCTS [00302] In one aspect, disclosed are food products comprising a disclosed peptide. In a further aspect, the peptide comprises a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, and wherein the peptide has a chain length of at least 30 amino acid residues. [00303] Frozen compositions, such as ice cream, typically incorporate a hardening step that involves quickly freezing the composition to obtain a desired frozen composition mouthfeel. Mouthfeel is affected by the size of ice crystals within the frozen composition. Larger ice crystals impart a grainy mouthfeel. Consequently, rapid freezing results in smaller ice crystals and smoother frozen composition mouthfeel. Without the hardening step, liquid water in frozen composition compositions freezes at much slower rates and forms large ice crystals which impart unacceptably grainy mouthfeel to the frozen composition. In addition, during frozen storage, ice crystal size increases over time as disproportionation occurs and smaller crystals melt and recrystallize onto larger ice crystals in a dynamic process resulting in pronounced iciness, giving the product an undesirable characteristic. Controlling the ice crystal size, whether by formulation, processing, distribution temperature control, or product age management is an objective of all frozen composition manufacturers in order to ensure a high quality finished product. [00304] Frozen fruits and vegatables produced according to traditional freezing methods suffer from a breakdown in the vegetable or fruit cell wall structure and, as such, have a low textural crispness. Crispness generally relates to the amount of water found in the cells of the vegetable or fruit, and translates into plant textural firmness upon mastication. Crispness is also a function of the structural integrity of the cells. A crisp vegetable is typically imbibed with water, has an intact cell wall structure, and, as such, has a firm, crisp texture. Most importantly, crisp vegetables and fruits have a crunchy and firm texture. For example, turgid or crisp celery will be crisp and crunchy; non-turgid or low crispness celery will be limp. When the cell walls break, water exits and crispness decreases. This means that the product will have a poor or mushy texture and will not retain suitable amounts of water. Typically, with slower freezing techniques, upon thawing, water leaches out of a vegetable or fruit product that has been frozen, resulting in a low texture limp product. As such, a product having fresh-like characteristics is not produced. [00305] As detailed herein, the disclosed peptides can be incorporated into a food product, in order slow, reduce, or otherwise inhibit ice crystal growth processes that influence the size and shape characteristics of the resultant ice that is formed during regrowth, thereby minimizing potential freezing damage by preventing or inhibiting ice recrystallisation of the product upon freezing. Thus, in various aspects, the disclosed food product reduces or inhibits ice crystal formation at a temperature of from about 0 °C to about -20 °C (e.g., at about 0, -1, -2, -3, -4, -5, -6, -7, -8, -9, -10, -11, -12, -13, -14, -15, -16, -17, -18, -19, or -20 °C). In a further aspect, the disclosed food product reduces or inhibits ice crystal formation at a temperature of from about -20 °C to about -40 °C (e.g., at about -20, -21, -22, -23, -24, -25, -26, -27, -28, -29, -30, -31, -32, -33, -34, -35, -36, -37, -38, -39, or -40 °C). In a still further aspect, the disclosed food product reduces or inhibits ice crystal formation at about -20 °C. In yet a further aspect, the disclosed food product reduces or inhibits ice crystal formation at a temperature of from about -40 °C to about -200 °C (e.g., at about -40, -45, -50, -55, -60, -65, -70, -75, -80, -85, -90, -95, -100, -105, -110, -115, -120, -125, -130, -135, -140, -145, -150, - 155, -160, -165, -170, -175, -180, -185, -190, -195, or -200 °C). In an even further aspect, the disclosed food product reduces or inhibits ice crystal formation at about -196 °C. [00306] In various aspects, the disclosed food product reduces or inhibits ice crystal formation at a temperature from about 0 °C to about -200 °C, from about -10 °C to about - 190 °C, from about -20 °C to about -180 °C, from about -30 °C to about -170 °C, from about -40 °C to about -160 °C, from about -50 °C to about -150 °C, from about -60 °C to about - 140 °C, from about -70 °C to about -140 °C, from about -80 °C to about -130 °C, from about -90 °C to about -120 °C, or from about -100 °C to about -110 °C. [00307] In various aspects, the disclosed food product comprises the peptide in a concentration of from about 100 nM to about 1,000 mM. In a further aspect, the disclosed food product comprises the peptide in a concentration of from about 100 nM to about 250 nM, from about 250 nM to about 500 nM, from about 500 nM to about 750 nM, from about 750 nM to about 1 μM, from about 1 μM to about 5 μM, from about 5 μM to about 25 μM, from about 25 μM to about 50 μM, from about 50 μM to about 100 μM, from about 100 μM to about 250 μM, from about 250 μM to about 500 μM, from about 500 μM to about 750 μM, from about 750 μM to about 1 mM, from about 1 mM to about 10 mM, from about 10 mM to about 50 mM, from about 50 mM to about 100 mM, from about 100 mM to about 250 mM, from about 250 mM to about 500 mM, from about 500 mM to about 750 mM, or from about 750 mM to about 1,000 mM. In a still further aspect, the disclosed food product comprises the peptide in a concentration of about 100 nM, about 1 μM, about 10 μM, about 100 μM, about 1 mM, about 10 mM, about 100 mM, or about 1,000 mM. In yet a further aspect, the disclosed food product comprises the peptide in a concentration [00308] In various aspects, the food product is selected from ice cream, yogurt, seafood, fruit, and a meat product. In a further aspect, the food product is ice cream. In a still further aspect, the food product is yogurt. In a yet further aspect, the food product is ice cream. In an even further aspect, the food product is seafood. In an even still further aspect, the food product is a fruit. In an even yet further aspect, the food product is a meat product. F. SURFACES [00309] In one aspect, disclosed are surfaces attached to a disclosed peptide. In a further aspect, the disclosed peptide comprises a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, and wherein the peptide has a chain length of at least 30 amino acid residues. [00310] In one aspect, disclosed are solid or semi-solid supports comprising a surface attached (e.g., covalently attached or coated) to a residue of a disclosed peptide. In a further aspect, the disclosed peptide comprises a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, and wherein the peptide has a chain length of at least 30 amino acid residues. [00311] The development of anti-icing, anti-frosting surfaces is of importance in building materials because surfaces covered with ice layers and frost layers often cause serious issues, such as poor visibility through the windshields of aircraft, trains and automobiles; poor visibility of traffic lights and surveillance cameras; decreases in efficiency of the heat exchanger and power generation efficiency of solar panels; breaking of power transmission lines in winter; and deterioration of the aerodynamic performance of aircraft wings. [00312] As detailed herein, the disclosed peptides can be attached to a surface in order to prevent, inhibit, or otherwise delay the formation of ice on objects including, but not limited to, aircrafts or parts thereof, gas pipelines, windows, electrical equipment, drones, cables (e.g., power lines), mechanical equipment (e.g., car engines, gear systems, brake systems, etc.), and the like. Thus, in various aspects, the disclosed solid or semi-solid support reduces or inhibits ice crystal formation at a temperature of from about 0 °C to about -20 °C (e.g., at about 0, -1, -2, -3, -4, -5, -6, -7, -8, -9, -10, -11, -12, -13, -14, -15, -16, -17, -18, -19, or -20 °C). In a further aspect, the disclosed solid or semi-solid support reduces or inhibits ice crystal formation at a temperature of from about -20 °C to about -40 °C (e.g., at about -20, - 21, -22, -23, -24, -25, -26, -27, -28, -29, -30, -31, -32, -33, -34, -35, -36, -37, -38, -39, or -40 °C). In a still further aspect, the disclosed solid or semi-solid support reduces or inhibits ice crystal formation at about -20 °C. In yet a further aspect, the disclosed solid or semi-solid support reduces or inhibits ice crystal formation at a temperature of from about -40 °C to about -200 °C (e.g., at about -40, -45, -50, -55, -60, -65, -70, -75, -80, -85, -90, -95, -100, - 105, -110, -115, -120, -125, -130, -135, -140, -145, -150, -155, -160, -165, -170, -175, -180, - 185, -190, -195, or -200 °C). In an even further aspect, the disclosed solid or semi-solid support reduces or inhibits ice crystal formation at about -196 °C. [00313] In various aspects, the disclosed surface reduces or inhibits ice crystal formation at a temperature from about 0 °C to about -200 °C, from about -10 °C to about -190 °C, from about -20 °C to about -180 °C, from about -30 °C to about -170 °C, from about -40 °C to about -160 °C, from about -50 °C to about -150 °C, from about -60 °C to about -140 °C, from about -70 °C to about -140 °C, from about -80 °C to about -130 °C, from about -90 °C to about -120 °C, or from about -100 °C to about -110 °C. [00314] In various aspects, the disclosed solid or semi-solid support reduces or inhibits ice crystal formation at a temperature from about 0 °C to about -200 °C, from about -10 °C to about -190 °C, from about -20 °C to about -180 °C, from about -30 °C to about -170 °C, from about -40 °C to about -160 °C, from about -50 °C to about -150 °C, from about -60 °C to about -140 °C, from about -70 °C to about -140 °C, from about -80 °C to about -130 °C, from about -90 °C to about -120 °C, or from about -100 °C to about -110 °C. [00315] Methods of covalently attaching a peptide to a surface or a solid or semi-solid support of a surface are well-known in the art. Alternatively, the peptide can be formulated into a composition, and coated onto the surface. See, e.g., Stawikowski and Fields (2002) Curr Protoc Protein Sci. Chapter: Unit-18.1, doi: 10.1002/0471140864.ps1801s26. [00316] In various aspects, attached is via covalent attachment to the surface. In various further aspects, attached is via coating a cyroprotectant composition comprising the peptide on the surface. [00317] In various aspects, the surface is a surface of a solid or semi-solid support, and wherein the support is a glass bead, a silica-based resin, a cellulosic resin, an agarose bead, a polystyrene bead, or a polyacrylamide resin. [00318] In various aspects, the disclosed surface comprises the peptide in a concentration of from about 100 nM to about 1,000 mM. In a further aspect, the disclosed surface comprises the peptide in a concentration of from about 100 nM to about 250 nM, from about 250 nM to about 500 nM, from about 500 nM to about 750 nM, from about 750 nM to about 1 μM, from about 1 μM to about 5 μM, from about 5 μM to about 25 μM, from about 25 μM to about 50 μM, from about 50 μM to about 100 μM, from about 100 μM to about 250 μM, from about 250 μM to about 500 μM, from about 500 μM to about 750 μM, from about 750 μM to about 1 mM, from about 1 mM to about 10 mM, from about 10 mM to about 50 mM, from about 50 mM to about 100 mM, from about 100 mM to about 250 mM, from about 250 mM to about 500 mM, from about 500 mM to about 750 mM, or from about 750 mM to about 1,000 mM. In a still further aspect, the disclosed surface comprises the peptide in a concentration of about 100 nM, about 1 μM, about 10 μM, about 100 μM, about 1 mM, about 10 mM, about 100 mM, or about 1,000 mM. In yet a further aspect, the disclosed surface comprises the peptide in a concentration. [00319] In various aspects, the cryoprotectant composition comprises the peptide in a concentration of from about 100 nM to about 1,000 mM. In a further aspect, the cryoprotectant composition comprises the peptide in a concentration of from about 100 nM to about 250 nM, from about 250 nM to about 500 nM, from about 500 nM to about 750 nM, from about 750 nM to about 1 μM, from about 1 μM to about 5 μM, from about 5 μM to about 25 μM, from about 25 μM to about 50 μM, from about 50 μM to about 100 μM, from about 100 μM to about 250 μM, from about 250 μM to about 500 μM, from about 500 μM to about 750 μM, from about 750 μM to about 1 mM, from about 1 mM to about 10 mM, from about 10 mM to about 50 mM, from about 50 mM to about 100 mM, from about 100 mM to about 250 mM, from about 250 mM to about 500 mM, from about 500 mM to about 750 mM, or from about 750 mM to about 1,000 mM. In a still further aspect, the cryoprotectant composition comprises the peptide in a concentration of about 100 nM, about 1 μM, about 10 μM, about 100 μM, about 1 mM, about 10 mM, about 100 mM, or about 1,000 mM. In yet a further aspect, the cryoprotectant composition comprises the peptide in a concentration. [00320] In various aspects, the disclosed solid or semi-solid support comprises the peptide in a concentration of from about 100 nM to about 1,000 mM. In a further aspect, the disclosed solid or semi-solid support comprises the peptide in a concentration of from about 100 nM to about 250 nM, from about 250 nM to about 500 nM, from about 500 nM to about 750 nM, from about 750 nM to about 1 μM, from about 1 μM to about 5 μM, from about 5 μM to about 25 μM, from about 25 μM to about 50 μM, from about 50 μM to about 100 μM, from about 100 μM to about 250 μM, from about 250 μM to about 500 μM, from about 500 μM to about 750 μM, from about 750 μM to about 1 mM, from about 1 mM to about 10 mM, from about 10 mM to about 50 mM, from about 50 mM to about 100 mM, from about 100 mM to about 250 mM, from about 250 mM to about 500 mM, from about 500 mM to about 750 mM, or from about 750 mM to about 1,000 mM. In a still further aspect, the disclosed solid or semi-solid support comprises the peptide in a concentration of about 100 nM, about 1 μM, about 10 μM, about 100 μM, about 1 mM, about 10 mM, about 100 mM, or about 1,000 mM. In yet a further aspect, the disclosed solid or semi-solid support comprises the peptide in a concentration. [00321] In various aspects, the residue of the peptide comprises an N-terminus, and the N- terminus is covalently attached to the surface. [00322] In various aspects, the residue of the peptide has a structure represented by a formula:

, wherein each occurrence of R¹ is independently a monosaccharide moiety or a disaccharide moiety; wherein each of R¹⁰ and R¹¹ is independently selected from ‒OH and ‒NHAc; wherein each occurrence of R² is independently selected from hydrogen and methyl; wherein R²⁰ is selected from ‒OR³¹, ‒NHR³², ‒N3, a protein tag, a sortase recognition sequence, a sugar residue, and a structure:

wherein R³¹ and R³² are selected from hydrogen, ‒CH2Ph, C1-C8 alkyl, C2-C8 alkyne, C1-C8 azide, tetrazinyl, cyclooctynyl, norbornenyl, and –(CH₂CH₂O)_mCH₃; wherein m is an integer selected from 1 to 100; wherein the ratio of x to y is of from about 3:2 to about 4:1; and wherein the sum of x and y is at least 30, or a pharmaceutically acceptable salt thereof. [00323] In various aspects, each occurrence of R¹ is independently a monosaccharide moiety or a disaccharide moiety having a structure represented by a formula:

wherein each occurrence of R¹⁰ and R¹¹ is independently selected from ‒OH and ‒NHAc.. [00324] As used herein, the term “support” refers to a material or substrate (e.g., a surface) onto which a peptide or a residue of a peptide, as defined herein, adheres. Adherence can be, for example, via chemical bonding, immobilization, dispersion, or association. Typically, a support is a polymeric material such as a network polymeric material. Supports include glasses, semiconductor materials, ceramic materials, metal surfaces, and other substrates on which the peptide or the residue of the peptide, as defined herein, can adhere. Additional examples of supports include, but are not limited to, glass beads, silica-based resins, cellulosic resins, agarose beads, polystyrene beads, or polyacrylamide resins. The support can be solid or semi-solid (e.g., gel-like, such as a polymer support composed of hydrogel polymers) as further described herein. G. M^{ETHODS OF} I^NHIBITING I^CE C^RYSTAL F^{ORMATION IN A} S^AMPLE [00325] In one aspect, disclosed are methods of inhibiting ice crystal formation in a sample, the method comprising contacting the sample with an effective amount of a disclosed peptide. In a further aspect, the disclosed peptide comprises a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, and wherein the peptide has a chain length of at least 30 amino acid residues. [00326] The methods described herein are suitable for use in any number of cryopreservation protocols. For example, in various aspects, the disclosed peptides, compositions, products, supports, and methods are useful for cryopreservation during supercooling to high sub-zero temperatures (e.g., from about 0 °C to about -20 °C). In various further aspect, the disclosed peptides, compositions, products, supports, and methods are useful for cryopreservation during freezing protocols (e.g., from about -20 °C to about -196 °C). Freezing protocols are typically performed at a controlled rate (sometimes referred to as slow freezing) during at least part of the temperature reduction. For example, a biological sample or macromolecule can be contacted with a disclosed peptide, and the temperature can be reduced at a controlled rate (e.g., lowered at a rate of 1 °C. per minute) until the desired temperature is reached. Alternatively, the temperature can be reduced at a controlled rate until a desired temperature is reached (e.g., from about -80° C to about -180° C), and then the sample or macromolecule can be flash frozen (e.g., by immersing the sample or macromolecule in liquid nitrogen or placing the sample or macromolecule above liquid nitrogen). The disclosed peptide should preferably be contacted with the sample or macromolecule being cryopreserved prior to freezing, to ensure that the peptide is in contact with the sample. Were the peptide to contact the sample after freezing, penetration through the ice block to the sample may hinder the ability of the peptide act as a cryoprotectant for the sample. [00327] In various further aspects, the disclosed peptides, compositions, products, supports, and methods are useful for cryogenic freezing protocols (e.g., from about -90 °C to about - 196 °C). For example, a biological sample or macromolecule can be contacted with a disclosed peptide or composition, then plunged into liquid nitrogen or a stream of liquid nitrogen vapor in order to quickly freeze the sample without the formation of ice crystals. No ice lattice exists and so the water within the sample or macromolecule is in an amorphous or glass-like state. Therefore, damaging ice is not formed. [00328] As would be readily appreciated by one of ordinary skill in the art, the concentrations and compositions of a peptide disclosed herein can be modified depending on the particular biological sample and/or macromolecule being cryopreserved and the particular cryopreservation protocol being employed. Thus, in various aspects, the disclosed composition comprises the peptide in a concentration of from about 100 nM to about 1,000 mM. In a further aspect, the disclosed composition comprises the peptide in a concentration of from about 100 nM to about 250 nM, from about 250 nM to about 500 nM, from about 500 nM to about 750 nM, from about 750 nM to about 1 μM, from about 1 μM to about 5 μM, from about 5 μM to about 25 μM, from about 25 μM to about 50 μM, from about 50 μM to about 100 μM, from about 100 μM to about 250 μM, from about 250 μM to about 500 μM, from about 500 μM to about 750 μM, from about 750 μM to about 1 mM, from about 1 mM to about 10 mM, from about 10 mM to about 50 mM, from about 50 mM to about 100 mM, from about 100 mM to about 250 mM, from about 250 mM to about 500 mM, from about 500 mM to about 750 mM, or from about 750 mM to about 1,000 mM. In a still further aspect, the disclosed composition comprises the peptide in a concentration of about 100 nM, about 1 μM, about 10 μM, about 100 μM, about 1 mM, about 10 mM, about 100 mM, or about 1,000 mM. In yet a further aspect, the disclosed composition comprises the peptide in a concentration of about 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 20, 30, 40, 50, 60, 70, 80, 90, or 100 mM. [00329] In various aspects, the disclosed peptide and/or the disclosed composition reduces or inhibits ice crystal formation at a temperature of from about 0 °C to about -20 °C (e.g., at about 0, -1, -2, -3, -4, -5, -6, -7, -8, -9, -10, -11, -12, -13, -14, -15, -16, -17, -18, -19, or -20 °C). In a further aspect, the disclosed peptide and/or the disclosed composition reduces or inhibits ice crystal formation at a temperature of from about -20 °C to about -40 °C (e.g., at about -20, -21, -22, -23, -24, -25, -26, -27, -28, -29, -30, -31, -32, -33, -34, -35, -36, -37, -38, -39, or -40 °C). In a still further aspect, the disclosed peptide and/or the disclosed composition reduces or inhibits ice crystal formation at about -20 °C. In yet a further aspect, the disclosed peptide and/or the disclosed composition reduces or inhibits ice crystal formation at a temperature of from about -40 °C to about -200 °C (e.g., at about -40, -45, -50, -55, -60, -65, -70, -75, -80, -85, -90, -95, -100, -105, -110, -115, -120, -125, -130, -135, -140, -145, -150, -155, -160, -165, -170, -175, -180, -185, -190, -195, or -200 °C). In an even further aspect, the disclosed peptide and/or the disclosed composition reduces or inhibits ice crystal formation at about -196 °C. [00330] In various aspects, the disclosed peptide and/or the disclosed composition reduces or inhibits ice crystal formation at a temperature from about 0 °C to about -200 °C, from about - 10 °C to about -190 °C, from about -20 °C to about -180 °C, from about -30 °C to about -170 °C, from about -40 °C to about -160 °C, from about -50 °C to about -150 °C, from about -60 °C to about -140 °C, from about -70 °C to about -140 °C, from about -80 °C to about -130 °C, from about -90 °C to about -120 °C, or from about -100 °C to about -110 °C. [00331] In various aspects, contacting is via application (e.g., application onto a sample or surface, topical application). In various further aspects, contacting is via coating. In various further aspects, contacting is via spraying or dipping. [00332] In various aspects, contacting is via covalent attachment. For example, as detailed herein, in various aspects, the disclosed peptide can be covalently attached to a surface. [00333] In various aspects, contacting is for a time period of at least 1 hour, at least 2 hours, at least 5 hours, at least 10 hours, at least 20 hours, at least 24 hours, or for longer than 24 hours. In various further aspects, contacting is for a time period of at least 1 day, 2 days, 4 days, 6 days, 7 days, or longer than 7 days. [00334] In various aspects, the method involves repeated contacting steps. For example, in various aspects, the sample can be contacted with the peptide or composition at least once, at least twice, at least three time, at least four times, or more than four times. [00335] In various aspects, the sample is a biological material. Examples of biological materials include, but are not limited to, a non-antifreeze protein (i.e., an enzyme, a hormone, an antibody, a growth factor, a vaccination protein, a therapeutic protein, or a nutrient protein), a microbe (i.e., a virus, a bacteria, an archaea, a fungi, and a protists), a cell component (i.e. a nucleolus, a nucleus, a ribosome, a vesicle, a rough endoplasmic reticulum, a Golgi apparatus, a cytoskeleton, a smooth endoplasmic reticulum, a mitochondria, a vacuole, a cytosol, a lysosome, and a centriole), a cell (e.g., a sperm cell, an egg matrix cell, an embryonic cell, a stem cell), a tissue (i.e., epithelial, connective, nervous, or muscle), and an organ (i.e., heart, kidney, liver, ovary, cornea). [00336] In various aspects, the sample is a food product. Examples of food products for which the disclosed method can be useful include, but are not limited to, ice cream, yogurt, seafood, fruit, and meat products. [00337] In various aspects, the sample is an agricultural product. Examples of agriculture products for which the disclosed method can be useful include, but are not limited to, grains, feeds, soybeans, tree nuts, fruits, and vegetables. [00338] In various aspects, the sample is a cosmetic. Examples of cosmetics for which the disclosed method can be useful include, but are not limited to, lips balms, hair products, makeup, nail products, soaps and lotions. [00339] In various aspects, the method further comprises storing the biological material for a period of time. [00340] In various aspects, storing is at a temperature of about 25 ℃ or less. In a further aspect, storing is at a temperature of abour 20 °C. In a still further aspect, storing is at a temperature of about 15 °C. In a yet further aspect, storing is at a temperature of about 10 °C. In an even further aspect, storing is at a temperature of abour 5 °C. In an even still further aspect, storing is at a temperature of abour 0 °C. In an even further aspect, storing is at a temperature of abour -5 °C. In an even yet further aspect, storing is at a temperature of abour -10 °C. In a further aspect, storing is at a temperature of abour -15 °C. In a still further aspect, storing is at a temperature of about -20 °C. In a yet further aspect, storing is at a temperature of about -25 °C. In an even further aspect, storing is at a temperature of abour - 30 °C. In an even still further aspect, storing is at a temperature of abour -35 °C. In an even further aspect, storing is at a temperature of abour -40 °C. In an even yet further aspect, storing is at a temperature of abour -45 °C. In a further aspect, storing is at a temperature of abour -50 °C. In a still further aspect, storing is at a temperature of about -55 °C. In a yet further aspect, storing is at a temperature of about -60 °C. In an even further aspect, storing is at a temperature of abour -65 °C. In an even still further aspect, storing is at a temperature of abour -70 °C. In an even further aspect, storing is at a temperature of abour -75 °C. In an even yet further aspect, storing is at a temperature of abour -80 °C. [00341] In various aspect, storing is at a temperature of about 5 ℃ or less. In a further aspect, storing is at a temperature of abour 4 °C. In a still further aspect, storing is at a temperature of about 3 °C. In a yet further aspect, storing is at a temperature of about 2 °C. In an even further aspect, storing is at a temperature of abour 2 °C. In an even still further aspect, storing is at a temperature of abour 0 °C. In an even further aspect, storing is at a temperature of abour -1 °C. In an even yet further aspect, storing is at a temperature of abour -2 °C. In a further aspect, storing is at a temperature of abour -3 °C. In a still further aspect, storing is at a temperature of about -4 °C. In a yet further aspect, storing is at a temperature of about -5 °C. H. U^{SE OF} P^EPTIDES [00342] In one aspect, the invention relates to the use of a disclosed peptide or a product of a disclosed method. As detailed herein, the disclosed peptides are useful in preventing or reducing damage caused by ice creation and ice recrystallization and can be formulated into a composition (e.g., a cryoprotectant composition, an agricultural composition, a cosmetic composition) to facilitate use in these areas. [00343] Also provided are the uses of the disclosed peptides and products. In one aspect, the invention relates to use of at least one disclosed peptide; or an acceptable salt thereof. In a further aspect, the peptide used is a product of a disclosed method of making. [00344] In a further aspect, the use relates to a process for preparing a composition comprising an effective amount of a disclosed peptide or a product of a disclosed method of making, or an acceptable salt thereof, wherein an acceptable carrier is intimately mixed with an effective amount of the peptide or the product of a disclosed method of making. [00345] It is understood that the disclosed uses can be employed in connection with the disclosed peptides, products of disclosed methods of making, methods, compositions (e.g., a cryoprotectant composition, an agricultural composition, a cosmetic composition), food products, solid and semi-solid supports, and kits. 1. KITS [00346] In one aspect, disclosed are kits comprising a disclosed peptide and one or more selected from: (a) a biological material; (b) a food product; (c) an agricultural product; (d) a solid or semi-solid support; and (e) a cosmetic. In a further aspect, the peptide comprises a plurality of alanine residues and a plurality of glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, and wherein the peptide has a chain length of at least 30 amino acid residues; and one or more selected from: (a) a biological material; (b) a food product; (c) an agricultural product; (d) a solid or semi-solid support; and (e) a cosmetic. [00347] In various aspects, the kit includes the biological material. In various further aspects, the biological material is selected from a non-antifreeze protein (e.g., an enzyme, a hormone, an antibody, a growth factor, a vaccination protein, a therapeutic protein, or a nutrient protein), a microbe (e.g., a virus, a bacteria, an archaea, a fungi, and a protists), a cell component (e.g. a nucleolus, a nucleus, a ribosome, a vesicle, a rough endoplasmic reticulum, a Golgi apparatus, a cytoskeleton, a smooth endoplasmic reticulum, a mitochondria, a vacuole, a cytosol, a lysosome, and a centriole), a cell (e.g., a sperm cell, an egg matrix cell, an embryonic cell, a stem cell), a tissue (e.g., epithelial, connective, nervous, or muscle), and an organ (e.g., heart, kidney, liver, ovary, cornea). [00348] In various aspects the kit includes the food product. Examples of food products include, but are not limited to, ice cream, yogurt, seafood, fruit, and meat products. [00349] In various aspects, the kit includes the agricultural product. Examples of agriculture products include, but are not limited to, grains, feeds, soybeans, tree nuts, fruits, and vegetables. [00350] In various aspects, the kit includes the solid or semi-solid support. Examples of solid and semi-solid supports include glasses, semiconductor materials, ceramic materials, metal surfaces, and other substrates on which the peptide or the residue of the peptide, as defined herein, can adhere. Additional examples of solid and semi-solid supports include, but are not limited to, glass beads, silica-based resins, cellulosic resins, agarose beads, polystyrene beads, or polyacrylamide resins. The support can be solid or semi-solid (e.g., gel-like, such as a polymer support composed of hydrogel polymers) as further described herein. [00351] In various aspects, the kit includes the cosmetic. Example of cosmetics include, but are not limited to, lips balms, hair products, makeup, nail products, soaps, and lotions. [00352] In a further aspect, the disclosed peptide and the biological material are co- formualated. In a still further aspect, the disclosed peptide and the food product are co- formualated. In a yet further aspect, the disclosed peptide and the agricultural product are co- formualated. In an even further aspect, the disclosed peptide and the solid or semi-solid support are co-formualated. In an even still further aspect, the disclosed peptide and the cosmetic are co-formulated. [00353] All publications and patent applications cited in this specification are herein incorporated by reference, and for any and all purposes, as if each individual publication or patent application were specifically and individually indicated to be incorporated by reference. In the event of an inconsistency between the present disclosure and any publications or patent application incorporated herein by reference, the present disclosure controls. I. E^XAMPLES [00354] The following examples are put forth so as to provide those of ordinary skill in the art with a complete disclosure and description of how the peptides, compositions, food products, solid and semi-solid supports, methods, and kits claimed herein are made and evaluated, and are intended to be purely exemplary of the invention and are not intended to limit the scope of what the inventors regard as their invention. Efforts have been made to ensure accuracy with respect to numbers (e.g., amounts, temperature, etc.), but some errors and deviations should be accounted for. Unless indicated otherwise, parts are parts by weight, temperature is in °C or is at ambient temperature, and pressure is at or near atmospheric. [00355] The Examples are provided herein to illustrate the invention, and should not be construed as limiting the invention in any way. 1. CHEMISTRY EXPERIMENTALS a. I^{NSTRUMENTATION AND GENERAL METHODS} [00356] Reactions were conducted under an inert atmosphere of N₂, and anhydrous reactions were conducted using oven-dried glassware unless otherwise stated. All glassware was oven dried at 120 °C. Hexanes and dichloromethane were purified by first purging with dry N2, followed by passage through columns of activated 3Å molecular sieves. THF was purified by first purging with dry N2, followed by passage through columns of activated alumina. Infrared spectra were recorded on a Bruker Alpha ATR-FTIR Spectrophotometer. All polymerizations were monitored for completion via ATR-FTIR. Deionized water (18 MΩ- cm) was obtained by passing in-house deionized water through a Thermo Scientific MicroPure UV/UF purification unit. Tandem size exclusion chromatography/refractive index (SEC/MALS/RI) was performed on an Agilent 1260 Infinity liquid chromatograph pump equipped with a Wyatt DAWN HELEOS-II light scattering (LS) and Wyatt Optilab T-rEX refractive index (RI) detectors. Separations were achieved using 10⁵, 10⁴, and 10³Å Phenomenex Phenogel 5 μm columns using 0.10 M LiBr in DMF as the eluent at 60 °C. All GPC/LS samples were prepared at concentrations of 3 mg/mL. Dn/dc values were calculated by batch injection of a series of polymer concentrations or by determining the degree of polymerization by ¹H NMR of polyethyleneglycol (PEG) end-capped polymers and fitting to the observed RI data. The applied dn/dc for α/βGalOAc4Thr, α/βGalNAcOAc3Thr, and βGal α GalNAcThr copolymers were 0.0456, 0.0462, and 0.0723, respectively. CD measurements of the polypeptide solutions were recorded in quartz cells with a path length of 0.1 cm, on a JASCO J-1500 CD spectrophotometer.¹H and ¹³C NMR spectra were recorded on a Varian Mercury spectrometer (400 MHz) or a Bruker AVANCE NEO spectrometer (500 MHz) and are reported relative to deuterated solvent. Data for ¹H NMR are reported as follows: chemical shift (δ ppm), multiplicity, coupling constant (Hz) and integration. Data for ¹³C NMR spectra are reported in chemical shift. Common solvent impurities found in spectra are labelled (Kramer, J. R.; Deming, T. J. Biomacromolecules 2010, 11, 3668–3672). b. SYNTHESIS OF SMALL MOLECULES i. P^{REPARATION OF} G^LYCOSYLATED T^HREONINE D^ERIVATIVES (a) N-Α-(CARBOBENZYLOXY)-3-O-(2,3,4,6-TETRA-O- ACETYL-Β-D-GALACTOPYRANOSYL)-L-THREONINE BENZYL ESTER, Z- β-GALOAC₄THROBN AND N-Α- (CARBOBENZYLOXY)-3-O-(2,3,4,6-TETRA-O-ACETYL- ^- D-GALACTOPYRANOSYL)-L-THREONINE BENZYL ESTER, Z- Α-GALOAC₄THR-OBN

[00357] GalOAc4-SPh and Z-Thr-OBn coupling was performed by modifying published procedures (Tseng, P. Het al., (2001) Chem. - A Eur. J.7, 585– 590). Anhydrous CH2Cl2 (0.69 mL) and 3Å mol sieves (0.228 g) were added to a flask containing GalOAc4- SPh (0.0912 g, 1 equiv) and Z-Thr-OBn (0.0946 g, 1.33 equiv) and the mixture was cooled to -45 °C. Then a solution of N-iodosuccinimide (0.186 g, 4 equiv) in acetonitrile (0.828 mL) was added followed by TMS triflate (0.0075 mL, 0.4 equiv). The reaction was stirred for 2 hours and reaction progress was monitored by TLC (2:1 hexanes:ethyl acetate, phosphomolybdic acid). Upon completion, the reaction was diluted with ethyl acetateand filtered through celite and cotton. The filtrate was washed 2× with Na2S2O3, 2× with aqueous sat. NaHCO3, 1× with deionized water. The organic layer was dried over Mg2SO4, filtered, and concentrated. The crude product was purified using column chromatography (2:1 hexanes:ethyl acetate). The fractions were analyzed with TLC (2:1 hexanes:ethyl acetate, phosphomolybdic acid). Like fractions were combined and concentrated resulting in 0.0876 g (63% yield, 1:4.7 ^: β). Anomeric centers were determined by HSQC. [00358] Z-Thr[ β-GalOAc₄]-OBn 1H NMR (500 MHz, CDCl₃) δ 7.37 (dt, J = 6.1, 3.7 Hz, 10H), 5.59 (d, J = 9.1 Hz, 1H), 5.35 – 5.28 (m, 1H), 5.16 (dd, J = 25.9, 2.3 Hz, 5H), 5.12 – 5.05 (m, 2H), 4.93 (ddd, J = 14.0, 10.1, 2.4 Hz, 1H), 4.45 – 4.38 (m, 2H), 4.36 (d, J = 7.9 Hz, 1H), 4.03 (qd, J = 9.8, 5.5 Hz, 2H), 3.65 (t, J = 6.8 Hz, 1H), 2.11 (s, 3H), 2.03 – 1.95 (m, 9H), 1.22 (d, J = 6.4 Hz, 3H). [00359] Z-Thr[α-GalOAc₄]-OBn 1H NMR (400 MHz, CDCl₃) δ 7.41 – 7.30 (m, 10H), 5.48 (d, J = 9.6 Hz, 1H), 5.31 (dt, J = 7.6, 4.0 Hz, 1H), 5.24 (d, J = 12.4 Hz, 1H), 5.16 – 5.05 (m, 4H), 4.94 (d, J = 10.0 Hz, 2H), 4.42 (t, J = 7.2 Hz, 2H), 4.21 (dd, J = 12.0, 3.9 Hz, 1H), 4.17 – 4.04 (m, 2H), 2.12 – 2.01 (m, 12H), 1.24 (s, 3H). (b) N-^Α-(C^{ARBOBENZYLOXY})-O-(2,3,4,6-^TETRA-O-^ACETYL- Β-D-GALACTOPYRANOSYL)-(1,3)-(2-AZIDO-2-DEOXY-4,6- B^ENZYLIDENE-^Α-D-^{GALACTOPYRANOSYL})-L-^THREONINE BENZYL ESTER, Z-THR(ΒGALOAC4-(1,3)-BENZYLIDENE- ΑGALN₃)-OBN

[00360] Z-Thr(benzylidene-αGalN3)-OBn was synthesized using published methods. (Deleray, A. C.; et al., (2022) Biomacromolecules 23, 3, 1453–1461). GalOAc₄-SPh and Z- Thr(benzylidene-αGalN3)-OBn coupling was performed by modifying a published procedure (Tseng, P. H.; et al., (2001) Chem. - A Eur. J. 7(3) 585-590). Anhydrous dichloromethane (0.53 mL) and 3Å molecular sieves (0.17 g) were added to a flask containing GalOAc4-SPh (0.093 g, 1.33 equiv) and Z-Thr-OBn (0.0982 g, 1 equiv) and the mixture was cooled to -45 °C. Next, a solution of N-iodosuccinimide (0.143 g, 4 equiv) in acetonitrile (0.63 mL) was added followed by triflic acid (0.0056 mL, 0.4 equiv). The reaction was stirred for 2 hours and reaction progress was monitored by TLC (2:1 hexanes:ethyl acetate, phosphomolybdic acid). Upon completion, the reaction was diluted with Ethyl acetate and filtered through celite and cotton. The filtrate was washed 2× with aqueous 10% Na₂S₂O₃, then 2× with aqueous saturated NaHCO3, and last 2× with aqueous saturated NaCl. The organic layer was dried over Mg₂SO₄, filtered, and concentrated. The crude product was purified using column chromatography (2:1 hexanes:ethyl acetate). The fractions were analyzed with TLC (2:1 hexanes:ethyl acetate, phosphomolybdic acid). Like fractions were combined and concentrated resulting in 0.122 g (80% yield).¹H NMR (400 MHz, CDCl3) δ 7.55 - 7.49 (m, 2H), 7.41 - 7.33 (m, 13H), 5.67 (d, J = 9.5 Hz, 1H), 5.52 (s, 1H), 5.41 (d, J = 3.5 Hz, 1H), 5.29 (dd, J = 10.4, 7.8 Hz, 1H), 5.21 (s, 2H), 5.16 (d, J = 2.7 Hz, 2H), 5.02 (dd, J = 10.4, 3.5 Hz, 1H), 4.92 (d, J = 3.6 Hz, 1H), 4.75 (d, J = 7.9 Hz, 1H), 4.50 - 4.41 (m, 2H), 4.34 (d, J = 3.2 Hz, 1H), 4.26 - 4.10 (m, 3H), 4.00 (d, J = 12.7 Hz, 1H), 3.97 - 3.89 (m, 2H), 3.75 (dd, J = 10.8, 3.6 Hz, 1H), 3.62 (s, 1H), 2.15 (s, 3H), 2.03 (s, 6H), 1.99 (s, 3H), 1.31 (d, J = 6.2 Hz, 3H). (c) N-^Α-(C^{ARBOBENZYLOXY})-O-(2,3,4,6-^TETRA-O-^ACETYL- Β-D-GALACTOPYRANOSYL)-(1,3)-(2-AZIDO-2-DEOXY-Α-D- GALACTOPYRANOSYL)-L-THREONINE BENZYL ESTER, Z- THR(ΒGALOAC4-(1,3)-BENZYLIDENE-ΑGALN3)-OBN

[00361] Acetic acid (28.9 mL) and DI water (7.5 mL) (4:1 acid:water) were added to a flask containing Z-Thr(pGal(OAc)4-(1,3)-phenylisopropylidene-αGalN3)-OBn (2.0 g). The reaction was heated to 80 °C for 3 hours. The reaction was monitored by TLC (2:1 Ethyl acetate:hexanes, phosphomolybdic acid). Upon completion, the reaction was concentrated with toluene to produce a fluffy white solid (1.81 g, 91%).¹H NMR analysis showed complete removal of the benzylidene, and the product was used directly in the next reaction. (d) N-^Α-(C^{ARBOBENZYLOXY})-O-(2,3,4,6-^TETRA-O-^ACETYL- Β-D-GALACTOPYRANOSYL)-(1,3)-(2-ACETAMIDO-2- D^EOXY-^Α-D-^{GALACTOPYRANOSYL})-L-^{THREONINE BENZYL} ESTER, Z-THR(ΒGALOAC₄-(1,3)-ΑGALNAC)-OBN

[00362] Z-Thr(βGal(OAc)4-(1,3)-αGalN3)-OBn (1.81 g) was dissolved in THE (40 mL), acetic acid (13.3 mL), and acetic anhydride (26.6 mL). Zinc powder (2.1 g) was added to the solution and then saturated aqueous CuSO4 solution (4 mL) was added. The reaction was stirred at room temperature for 1 hour. The reaction was monitored by TLC (1.5:1 ethyl acetate:hexanes, phosphomolybdic acid). Upon completion, the reaction was filtered through celite and cotton, and the filtrate was concentrated with toluene to produce a chalky white solid which was used directly in the next reaction. (e) N-^Α-(C^{ARBOBENZYLOXY})-O-(2,3,4,6-^TETRA-O-^ACETYL- Β-D-GALACTOPYRANOSYL)-(1,3)-(2-ACETAMIDO-2- D^EOXY-4,6-O-^ACETYL-^Α-D-^{GALACTOPYRANOSYL})-L- THREONINE BENZYL ESTER, Z-THR(ΒGALOAC4-(1,3)- ΑG^ALNA^C(OA^C)2)-OB^N

[00363] To acetylate the free hydroxyls, Z-Thr(βGalOAc4-(1,3)-αGalNAc)-OBn (1.81 g) (0.085 g) was cooled to 0 °C and dissolved in acetic anhydride (0.67 mL) and pyridine (1.33 mL). The reaction was stirred overnight and allowed to warm to room temperature. The reaction was monitored by TLC (3:1 ethyl acetate:hexanes, phosphomolybdic acid). Upon completion, the reaction was cooled to 0 °C and quenched with 5 mL DI water. The aqueous layer was extracted 3× with Ethyl acetate. The organic layer was then washed 2× with 1M HCI, then 2× with aqueous saturated NaHCO3, and lastly 2× with aqueous saturated NaCl, and dried over Na₂SO₄. The crude product was purified using column chromatography (3:1 hexanes:ethyl acetate). The fractions were analyzed with TLC (3:1 hexanes:ethyl acetate, phosphomolybdic acid). Like fractions were combined and concentrated resulting in 0.059 g (63% yield).¹H NMR (500 MHz, CDCI3) δ 7.46 - 7.34 (m, 10H), 7.33 (s, 1H), 5.71 (d, J = 8.9 Hz, 1H), 5.48 (d, J = 9.4 Hz, 1H), 5.37 (dd, J = 7.4, 3.3 Hz, 2H), 5.23 (d, J = 11.8 Hz, 1H), 5.16 - 5.07 (m, 2H), 4.97 (dd, J = 10.6, 3.4 Hz, 1H), 4.83 (d, J = 3.8 Hz, 1H), 4.59 (d, J = 7.8 Hz, 1H), 4.46 (s, 2H), 4.24 (d, J = 6.4 Hz, 1H), 4.17 (d, J = 5.1 Hz, 3H), 4.13 - 4.08 (m, 2H), 3.98 (dd, J = 11.3, 7.4 Hz, 1H), 3.91 (s, 1H), 3.80 (dd, J = 11.0, 3.2 Hz, 1H), 2.15 (d, J = 4.5 Hz, 6H), 2.09 (s, 3H), 2.05 (d, J = 1.7 Hz, 9H), 1.99 (s, 3H), 1.35 (d, J = 6.3 Hz, 3H) (f) O-(2,3,4,6-^TETRA-O-^ACETYL-^Β-D-^{GALACTOPYRANOSYL})- (1,3)-(2-ACETAMIDO-2-DEOXY-4,6-O-ACETYL-Α-D- G^{ALACTOPYRANOSYL})-L-^THREONINE, H- THR(ΒGALOAC4-(1,3)-ΑGALNAC(OAC)2)-OH

[00364] Z-Thr(βGalOAc₄-(1,3)-αGalNAc(OAc)₂)-OBn (0.6852 g, lequiv) was dissolved in methanol (28.5 mL, 0.025M) and added to a flask containing 10% palladium on carbon (Pd/C) (0.137 g, 20% starting material mass) under H₂. The reaction was stirred vigorously for 3 hours. The reaction progress was monitor by TLC (1:3 hexanes:ethyl acetate + 1% acetic acid, phosphomolybdic acid). After 3 hours, the reaction was filtered through cotton and a 0.45pm filter to remove the Pd/C. The reaction was then concentrated, resulting in a white solid.¹H NMR analysis confirmed the disappearance of aromatic protons belonging to the carboxybenzyl and benzyl protecting groups. The product was used directly in the next reaction without further purification. (g) N-Α-(BUTOXYCARBONYL)-O-(2,3,4,6-TETRA-O-ACETYL-Β- D-^{GALACTOPYRANOSYL})-(1,3)-(2-^ACETAMIDO-2-^DEOXY- 4,6-O-ACETYL-Α-D-GALACTOPYRANOSYL)-L-THREONINE, B^OC-T^HR(^ΒG^ALOA^C4-(1,3)-^ΑG^ALNA^C(OA^C)2)-OH

[00365] H-Thr(βGalOAc₄-(1,3)-αGalNAc(OAc)₂)-OH (0.525 g, 1 equiv) was added to a 1:1 mixture of THF/water (7 mL) and cooled to 0 °C. In a modification to publish procedures, NaHCO3 (0.749 g, 12.5 equiv) and di-tert-butyl dicarbonate (Boc2O) (0.778 g, 5 equiv) were added consecutively at increased molar equivalents. The reaction was allowed to warm to RT and stirred overnight. The reaction progress was monitored by TLC (1:3 hexanes:ethyl acetate + 1% acetic acid, phosphomolybdic acid). Upon completion, the reaction was washed 3× with diethylether to remove excess Boc2O. The aqueous layer was cooled to 0 °C and acidified to pH 4-5 using acetic acid. The aqueous layer was extracted 3× with dichloromethane and the combined organic layers dried over sodium sulfate. The organic layers were concentrated yielding a white solid. The crude product was purified using column chromatography (eluent 1:3 hexanes:ethyl acetate +1% acetic acid). Fractions were analyzed by TLC (1:3 hexanes:ethyl acetate + 1% acetic acid, phosphomolybdic acid) and combined to produce a white, fluffy solid (0.4935 g, 83% yield over two steps).¹H NMR (400 MHz, CD3OD) δ 5.41 (d, J = 3.3 Hz, 1H), 5.35 (d, J = 3.3 Hz, 1H), 5.05 (dd, J = 10.5, 3.3 Hz, 1H), 5.02 - 4.96 (m, 1H), 4.89 (d, J = 3.8 Hz, 1H), 4.75 (d, J = 7.6 Hz, 1H), 4.34 (dd, J = 11.3, 4.0 Hz, 2H), 4.25 (dd, J = 8.0, 4.5 Hz, 1H), 4.19 - 4.09 (m, 4H), 4.06 (q, J = 6.8 Hz, 1H), 3.98 (td, J = 9.8, 5.4 Hz, 2H), 2.11 (d, J = 10.5 Hz, 7H), 2.03 (t, J = 4.1 Hz, 12H), 1.93 (s, 3H), 1.48 (s, 9H), 1.28 (s, 4H).¹³C NMR (126 MHz, CDCl3) δ 173.31, 172.82, 170.52, 170.49, 170.39, 170.33, 170.15, 170.01, 169.71, 169.37, 156.17, 155.99, 129.05, 128.24, 100.41, 99.74, 80.28, 77.58, 70.90, 70.71, 68.80, 67.75, 66.82, 63.21, 62.85, 61.13, 58.20, 53.22, 49.13, 28.46, 28.38, 22.82, 20.71, 20.56, 18.33. ii. PREPARATION OF GLYCOSYLATED SERINE DERIVATIVES (a) N-^Α-(C^{ARBOBENZYLOXY})-3-O-(2,3,4,6-^TETRA-O- ACETYL-Β-D-GALACTOPYRANOSYL)-L-SERINE BENZYL ESTER, Z- β-GALOAC₄SEROBN AND N-Α- (CARBOBENZYLOXY)-3-O-(2,3,4,6-TETRA-O-ACETYL- ^- D-GALACTOPYRANOSYL)-L-SERINE BENZYL ESTER, Z- Α- GALOAC4SER-OBN

[00366] N-α-(Carbobenzyloxy)-3-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-L-serine benzyl ester, Z- β-GalOAc4SerOBn and N-α-(Carbobenzyloxy)-3-O-(2,3,4,6-tetra-O-acetyl- ^-D-galactopyranosyl)-L-serine benzyl ester, Z- α-GalOAc4Ser-OBn were completed by modifying publish methods (Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453– 1461). (b) N-^Α-(C^{ARBOBENZYLOXY})-O-(2-^AZIDO-4,6-^BENZYLIDENE- 3-O-CHLOROACETYL-2-DEOXY- ^-D- GALACTOPYRANOSYL)-L-SERINE BENZYL ESTER, Z- SER(ΒGALOAC₄-(1,3)-BENZYLIDENE-ΑGALN₃)-OBN

[00367] N-α-(Carbobenzyloxy)-O-(2-azido-4,6-benzylidene-3-O-chloroacetyl-2-deoxy- ^-D- galactopyranosyl)-L-serine benzyl ester was prepared by modifying the procedures described herein. (c) N-^Α-(C^{ARBOBENZYLOXY})-O-(2,3,4,6-^TETRA-O-^ACETYL- Β-D-GALACTOPYRANOSYL)-(1,3)-(2-AZIDO-2-DEOXY-4,6- B^ENZYLIDENE-^Α-D-^{GALACTOPYRANOSYL})-L-^SERINE BENZYL ESTER, Z-SER(ΒGALOAC4-(1,3)-BENZYLIDENE- ΑG^ALN3)-OB^N

[00368] N-α-(Carbobenzyloxy)-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1,3)-(2- azido-2-deoxy-4,6-benzylidene-α-D-galactopyranosyl)-L-serine benzyl ester was prepared by modifying the procedures described herein. (d) N-^Α-(C^{ARBOBENZYLOXY})-O-(2,3,4,6-^TETRA-O-^ACETYL- Β-D-GALACTOPYRANOSYL)-(1,3)-(2-AZIDO-2-DEOXY-Α-D- G^{ALACTOPYRANOSYL})-L-^{SERINE BENZYL ESTER}, Z- SER(ΒGALOAC₄-(1,3)-BENZYLIDENE-ΑGALN₃)-OBN

[00369] N-α-(Carbobenzyloxy)-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1,3)-(2- azido-2-deoxy-α-D-galactopyranosyl)-L-serine benzyl ester was prepared by modifying the procedures describe herein. (e) N-Α-(CARBOBENZYLOXY)-O-(2,3,4,6-TETRA-O-ACETYL- Β-D-GALACTOPYRANOSYL)-(1,3)-(2-ACETAMIDO-2- DEOXY-Α-D-GALACTOPYRANOSYL)-L-SERINE BENZYL ESTER, Z-SER(ΒGALOAC4-(1,3)-ΑGALNAC)-OBN

[00370] N-α-(Carbobenzyloxy)-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1,3)-(2- acetamido-2-deoxy-α-D-galactopyranosyl)-L-serine benzyl ester was prepared by modifying the procedures described herein. (f) N-^Α-(C^{ARBOBENZYLOXY})-O-(2,3,4,6-^TETRA-O-^ACETYL- Β-D-GALACTOPYRANOSYL)-(1,3)-(2-ACETAMIDO-2- D^EOXY-4,6-O-^ACETYL-^Α-D-^{GALACTOPYRANOSYL})-L- SERINE BENZYL ESTER, Z-SER(ΒGALOAC₄-(1,3)- ΑG^ALNA^C(OA^C)2)-OB^N

[00371] N-α-(Carbobenzyloxy)-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1,3)-(2- acetamido-2-deoxy-4,6-O-acetyl-α-D-galactopyranosyl)-L-serine benzyl ester was prepared by modifying the procedures described herein. (g) O-(2,3,4,6-TETRA-O-ACETYL-Β-D-GALACTOPYRANOSYL)- (1,3)-(2-ACETAMIDO-2-DEOXY-4,6-O-ACETYL-Α-D- GALACTOPYRANOSYL)-L-SERINE, H-SER(ΒGALOAC₄- (1,3)-ΑGALNAC(OAC)2)-OH

[00372] O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1,3)-(2-acetamido-2-deoxy-4,6-O- acetyl-α-D-galactopyranosyl)-L-serine was prepared by modifying the procedures describe herein. (h) N-Α-(BUTOXYCARBONYL)-O-(2,3,4,6-TETRA-O-ACETYL-Β- D-^{GALACTOPYRANOSYL})-(1,3)-(2-^ACETAMIDO-2-^DEOXY- 4,6-O-ACETYL-Α-D-GALACTOPYRANOSYL)-L-SERINE, B^OC-S^ER(^ΒG^ALOA^C4-(1,3)-^ΑG^ALNA^C(OA^C)2)-OH

[00373] N-α-(butoxycarbonyl)-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1,3)-(2- acetamido-2-deoxy-4,6-O-acetyl-α-D-galactopyranosyl)-L-serine was prepared by modifying the procedures described herein. iii. PREPARATION OF ALANINE N-CARBOXYANHYDRIDE

[00374] Alanine N-carboxyanhydride (Ala NCA) was synthesized using published methods (Kramer, J. R.; et al., (2015) Proc. Natl. Acad. ScL, 112 (41), 12574-12579).¹H NMR (500 MHz, CDCI3) δ 5.72 (s, 1H), 4.41 (q, J = 7.0 Hz, 1H), 1.58 (d, J = 7.0 Hz, 3H).13C NMR (126 MHz, CDCI3) 6169.98, 151.65, 53.40, 17.95. iv. PREPARATION OF N-CARBOXYANHYDRIDE THREONINE DERIVATIVES (a) O-((2,3,4,6-TETRA-O-ACETYL)- Β-D- G^{ALACTOPYRANOSE}))-L-^THREONINE-N- CARBOXYANHYDRIDE, ΒGAL(OAC)4THR NCA

[00375] O-((2,3,4,6-tetra-O-acetyl)-α-D-galactopyranose))-L-threonine-N-carboxyanhydride (βGal(OAc)₄Thr NCA) was synthesized according to a published method (Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461). (b) O-((2,3,4,6-TETRA-O-ACETYL)- Α-D- GALACTOPYRANOSE))-L-THREONINE-N- CARBOXYANHYDRIDE, ΒGAL(OAC)₄THR NCA

[00376] O-((2,3,4,6-tetra-O-acetyl)-α-D-galactopyranose))-L-threonine-N-carboxyanhydride (βGal(OAc)₄Thr NCA) was synthesized according to a published method (Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461). (c) O-((2-ACETAMIDO-2-DEOXY-3,4,6-TRI-O-ACETYL)-Β-D- GALACTOPYRANOSE))-L-THREONINE-N- C^{ARBOXYANHYDRIDE}, ^ΒG^ALNA^C(OA^C)3T^HR NCA

[00377] O-((2-acetamido-2-deoxy-3,4,6-tri-O-acetyl)-β-D-galactopyranose))-L-threonine-N- carboxyanhydride was completed by modifying publish methods (Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461). The Boc-βGalNAc(OAc)₃Thr (0.1959 g, 1equiv) was dissolved in anhydrous THE (3.57 mL, 0.1M). Triphosgene (0.042 g, 0.4 equiv) was added and the solution was cooled to 0 °C. Distilled TEA (0.0546 mL, 1.1 equiv) was added dropwise. The reaction was stirred for 3 hours and reaction progress was monitored by ATR-FTIR. After 3 hours the reaction was filtered through cotton to remove TEA-HCI salts. The reaction solution was evaporated under reduced pressure. The evaporate was sequestered in a tandem solvent trap system cooled by liquid nitrogen. The traps were immediately quenched with ammonium hydroxide. The crude product was purified using anhydrous silica chromatography (Kramer, J. R.; Deming, T. J. (2010) Biomacromolecules, 11(12), 3668- 3672) with 10% to 20% THF in dichloromethane. The collected fractions were analyzed by ATR-FTIR. NCA-containing fractions were combined resulting in 0.089 g of white solid (52% yield).¹H NMR (500 MHz, CDCl3) δ 7.20 (s, 1H), 6.18 (d, J= 8.6 Hz, 1H), 5.33 (d, J = 3.5 Hz, 1H), 5.24 (dd, J= 11.2, 3.6 Hz, 1H), 4.79 (d, J = 8.3 Hz, 1H), 4.20 (d, J= 5.9 Hz, 1H), 4.19 - 4.06 (m, 3H), 4.00 - 3.87 (m, 2H), 2.13 (d, J= 4.9 Hz, 3H), 2.06 (d, J= 4.3 Hz, 3H), 1.96 (dd, J = 15.9, 5.0 Hz, 6H), 1.37 (d, J= 6.3 Hz, 3H).¹³C NMR (126 MHz, CDCl₃) δ 171.07, 171.01, 170.69, 170.33, 167.50, 100.61, 76.23, 71.24, 69.63, 68.06, 66.85, 62.59, 61.96, 51.58, 25.71, 23.38, 20.77, 17.39. (d) O-(2,3,4,6-TETRA-O-ACETYL-Β-D-GALACTOPYRANOSYL)- (1,3)-(2-^ACETAMIDO-2-^DEOXY-4,6-O-^ACETYL-^A-D- GALACTOPYRANOSYL)-L-THREONINE-N- CARBOXYANHYDRIDE, THR(ΒGAL(OAC)₄-(1,3)- ΑGALNAC(OAC)2) NCA

[00378] The cyclization of Boc-Thr(βGal(OAc)₄-(1,3)-αGalNAc(OAc)₂)-OH was completed by modifying published methods (Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461). The Boc-Thr(βGal(OAc)₄-(1,3)-αGalNAc(OAc)₂)-OH (0.3373 g, 1equiv) was dissolved in anhydrous THF (4.03 mL, 0.1M). Triphosgene (0.048 g, 0.4 equiv) was added and the solution was cooled to 0 °C. Distilled TEA (0.0448 mL, 1.1equiv) was added dropwise. The reaction was stirred for 3 hours and reaction progress was monitored by ATR- FTIR. After 3 hours the reaction was filtered through cotton to remove TEA-HCI salts. The reaction solution was evaporated under reduced pressure. The evaporate was sequestered in a tandem solvent trap system cooled by liquid N₂. The traps were immediately quenched with ammonium hydroxide. The crude product was purified using anhydrous silica chromatography' with 10% to 30% to 50% THF in DCM. The collected fractions were analyzed by ATR-FTIR. NCA containing fractions were combined resulting in 0.2232 g of white solid (72% yield).¹H NMR (500 MHz, CDCl₃) δ 7.34 (s, 1H), 5.97 (d, J = 7.4 Hz, 1H), 5.35 (d, J = 3.1 Hz, 2H), 5.19 (d, J = 3.6 Hz, 1H), 5.12 (dd, J = 10.4, 7.9 Hz, 1H), 4.97 (dd, J = 10.4, 3.5 Hz, 1H), 4.65 (d, J = 8.0 Hz, 1H), 4.39 - 4.31 (m, 1H), 4.31 (s, 1H), 4.23 - 4.10 (m, 5H), 4.00 - 3.88 (m, 3H), 2.17 (s, 3H), 2.09 (d, J = 10.4 Hz, 6H), 2.05 (d, J = 2.6 Hz, 9H), 1.96 (s, 3H), 1.41 (d, J = 6.5 Hz, 3H).¹³C NMR (126 MHz, CDCl₃) δ 171.30, 170.86, 170.69, 170.50, 170.22, 170.20, 168.25, 152.45, 100.18, 99.44, 75.31, 72.23, 71.26, 70.98, 68.59, 68.53, 66.87, 62.86, 62.77, 61.25, 49.59, 23.18, 20.94, 20.88, 20.84, 20.82, 20.80, 20.64, 17.72. v. P^{REPARATION OF} N-^{CARBOXYANHYDRIDE} S^ERINE DERIVATIVES (a) O-((2,3,4,6-TETRA-O-ACETYL)- Β-D- G^{ALACTOPYRANOSE}))-L-^SERINE-N-^{CARBOXYANHYDRIDE}, ΒGAL(OAC)4SER NCA

[00379] O-((2,3,4,6-tetra-O-acetyl)- β-D-galactopyranose))-L-serine-N-carboxyanhydride was completed by modifying publish methods (Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461).

(b) O-((2,3,4,6-^TETRA-O-^ACETYL)- ^Α-D- GALACTOPYRANOSE))-L-SERINE-N-CARBOXYANHYDRIDE, ΒG^AL(OA^C)4T^HR NCA [00380] O-((2,3,4,6-tetra-O-acetyl)- α-D-galactopyranose))-L-serine-N-carboxyanhydride was completed by modifying publish methods (Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461).

(c) O-((2-^ACETAMIDO-2-^DEOXY-3,4,6-^TRI-O-^ACETYL)-^Β-D- GALACTOPYRANOSE))-L-SERINE-N-CARBOXYANHYDRIDE, ΒG^ALNA^C(OA^C)3S^ER NCA [00381] O-((2-acetamido-2-deoxy-3,4,6-tri-O-acetyl)-β-D-galactopyranose))-L-serine-N- carboxyanhydride was completed by modifying publish methods (Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461).

(d) O-(2,3,4,6-^TETRA-O-^ACETYL-^Β-D-^{GALACTOPYRANOSYL})- (1,3)-(2-ACETAMIDO-2-DEOXY-4,6-O-ACETYL-A-D- G^{ALACTOPYRANOSYL})-L-^SERINE-N-^{CARBOXYANHYDRIDE}, SER(ΒGAL(OAC)₄-(1,3)-ΑGALNAC(OAC)₂) NCA [00382] The cyclization of Boc-Ser(βGal(OAc)4-(1,3)-αGalNAc(OAc)2)-OH was completed by modifying published methods (Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461). c. ^SAFGP P^REPARATION i. G^{ENERAL METHOD FOR POLYMERIZATION OF} NCA^S

[00383] All polymerizations were prepared in a nitrogen filled glovebox. NCAs were dissolved in anhydrous THF at 50 mg/mL in a glass vial or bomb tube. To the NCA solution, a 30 mg/mL solution of tetrakis(trimethylphosphine)cobalt ((PMe₃)₄Co) in THF was added and the tube was sealed. The NCA:(PMe3)4Co ratio ranged from 10:1 to 80:1, yielding different length polypeptides. The vials were left in the glove box at room temperature and the bomb tubes were removed from the gloved box and heated at 50 °C for 5-72 hrs. The reaction progress was monitored by ATR-FTIR. Upon completion, the polypeptides were analyzed with SEC/MALS/RI. ii. GENERAL METHOD FOR POLYMERIZATION OF STATISTICAL COPOLYMERS

[00384] Copolymers were prepared in a nitrogen filled glovebox in a manner similar to homopolymers. The NCAs were dissolved in THF at 50 mg/mL and mixed at a variety of NCA molar ratios. (PMe₃)₄Co catalyst in THF (30 mg/mL) was added to the combined NCA solutions and the reaction progressed at RT and was monitored by ATR-FTIR. Polypeptides that remained soluble were analyzed using SEC/MALS/RI. iii. GENERAL METHOD FOR THE DEACETYLATION OF ACO- PROTECTED POLYMERS

[00385] The polypeptide was suspended in 0.25M potassium carbonate in 1:1 methanol and water and stirred overnight. The deacetylated polymer in solution was transferred to a l kDa spin filter and concentrated at 4000 × g for 20 minutes. The concentrate was diluted three times with MilliQ and spin filtered at 4000 × g for 20 minutes each time. The concentrate was recovered, frozen, and lyophilized. Samples can also be dialyzed against MilliQ water in 2000 MWCO dialysis tubing. iv. GENERAL METHOD FOR LABELING GLYCOPOLYPEPTIDES WITH AF594 FLUOROPHORE [00386] The deacetylated polypeptide was added to a 100 uM solution of sodium bicarbonate in MilliQ water for a final polymer concentration of 5 mg/mL. AF594 was dissolved in DMSO at 10 mg/mL.8 molar equivalents of AF594 were added to the polymer sodium bicarbonate solution. The tube containing the solution was wrapped in foil and placed on a shaker plate to react overnight. The solution was transferred to a 1kDa spin filter and concentrated at 4000 × g for 20 minutes. The concentrate was diluted three times with MilliQ and spin filtered at 4000 × g for 20 minutes each time. The concentrate was recovered, frozen, and lyophilized. Samples can also be dialyzed against MilliQ water in 2000 MWCO dialysis tubing. The labeled glycopolypeptide was stored at -20 °C and shielded from light. 2. GENERAL METHODS FOR SAFGP BIOLOGICAL AND ICE BINDING ASSAYS a. G^{ENERAL METHOD FOR PROTEASE DIGESTION OF} GLYCOPOLYPEPTIDES [00387] Polypeptide is added to MilliQ water to make a 10 µg/µL stock solution. Polypeptide stock solution, 2X PBS, and protease (StcE or Proteinase K) were added to a reaction tube such that the protease to substrate ratio is 0.1. StcE was a gift from the lab of Carolyn Bertozzi and was expressed and purified according to literature (Malaker, Stacy A.; et al., (2019) Proc Natl Aced Sci 116(15) 7278-7287). Protease K was obtained from ThermoFisher (#AM2542). The solution is balanced with MilliQ water so that the final concentration of polymer is 1 µg/µL in 1X PBS. The solution was placed in a 37 °C water bath and 10 uL timepoints were removed at 6, 24, 28 hours and after 7 days. Upon removal from the reaction vessel, timepoints are treated at 95 °C for 10 minutes to stop the protease activity. Samples are stored in -80 °C until analysis with electrophoresis. b. GENERAL METHOD FOR ELECTROPHORESIS AND SDS-PAGE [00388] 20 µg of polypeptide (with or without denatured protease) in PBS was combined with 4X loading buffer from BioRad to make a 1X solution of dye and polypeptide. Thermo Fisher Spectra Multicolor Broad Range Protein Ladder was applied to a separate well. The entire volume was applied to a well in a Bis-tris 4-12% gel from BioRad. The gel ran for 40 minutes at 175 V. Pro-Q® Emerald 300 Lipopolysaccharide Gel Stain Kit from ThermoFisher was used to stain the glycopolypeptide. Modifications to the established protocol include staining gel for 100 minutes and creating fresh oxidizer from periodic acid for each gel. After completing the staining process gels were imaged using a standard gel imager and exposed for 4.2 seconds. When establishing a protocol for staining SDS-Page gels containing out polypeptides, Coomassie Blue R-250 and G-250, Gel Code Blue, and silver stain were also tested. None of these stains worked with our glycopolypeptides. c. GENERAL METHOD FOR DETERMINING CELL VIABILITY WITH A CCK8 ^ASSAY [00389] HEK 293 cells were plated at a density of 10,000 cells/well in a 96 well plate. The cells were incubated at 37 °C in 5% CO2 for 24 hours to allow the cells to adhere to the plate. The cells were then treated with polymer dissolved in complete media (DMEM with 10% FBS supplemented with 1% penicillin-streptomycin and 1% L-glutamine) for a final polymer concentration of 0.02, 0.2, 2.0 mg/mL. Additionally, other wells of cells are treated with 100- X Triton to kill cells for a positive control or media to serve a negative control. The treated cells were again incubated at 37 °C in 5% CO₂ for 24 hours. The cells were then dosed with 10 uL of CCK-8 solution (Dojindo) and incubated at 37 °C in 5% CO2 for 3 hours. The absorbance at 450 nm of the treated cells was measured after the 3 hours of incubation using a BioTek Synergy HTK multi-mode reader. d. G^ENERAL M^{ETHOD FOR} O^BSERVING D^YNAMIC I^CE S^HAPING [00390] To observe dynamic ice shaping 10 uL of solution containing polypeptide in 1X PBS was placed on a microscope slide and sandwiched between a cover slip. The stage was rapidly cooled at a rate of 10 °C/min to -30 °C to freeze the polymer solution. The stage was then slowly warmed to - 2.5 °C at a rate of 8 °C/min. Then the stage was warmed to -1.8 °C at a rate of 0.5 °C/min. The stage temperature was then increased at a rate of 0.05 °C/min to - 1.5 to -1 °C depending on the polypeptide solution to isolate individual crystals. The stage was then cooled at 0.02 °C/min to -2 to -1.5 °C to observe dynamic ice shaping. The stage was then toggled between melting and freezing rates to observe the ice crystal change as the temperature was increased and then decreased. Images of the single crystals were taken as the temperature was decreased to observe ice crystal growth. e. GENERAL METHOD FOR COOLING SPLAT ASSAYS [00391] 10 μL of solution containing polypeptide in PBS was dropped from 2 meters through a PVC pipe onto a precooled slide using a micropipette (FIG.43) (Note 1 and 2). The slide was cooled on an aluminum block resting in a bed of dry ice (Note 3). The slide containing the ice splat was quickly moved to the temperature- controlled stage (Linkam LTS120, WCP, and T96 controller) precooled to -6.4 °C. The stage chamber was purged with nitrogen to prevent condensation from growing on the ice splat (Note 4). The ice splat was annealed for 40 minutes and images of the ice crystals were recorded at 0, 20, and 40 minutes using cross polarizers (MOTICAM S3, MOTIC BA310E LED Trinocular) to observe ice recrystallization inhibition. [00392] Notes: (1) To remove the static from the PVC pipe post purchase, unscented dryer sheets were pushed through the pipe and brushed alone the pipe openings. (2) With some polymer solutions, the surface tension made releasing the drop from the pipette difficult. To overcome this problem the outside of the pipette tip was wiped with immersion oil. Excess oil was removed with a clean wipe before dispensing solution. (3) It is important to have the slide positioned close to the opening of the PVC pipe so air flow does not alter the drop's trajectory. (4) The flowrate of nitrogen into the cryostage was reduced to < 0.1L/min after the stage was purged with nitrogen to remove the ambient air introduced when placing the slide on the temperature controlled stage. Reducing the flowrate is important to prevent sublimation. f. GENERAL METHOD FOR QUANTIFYING ICE RECRYSTALLIZATION I^NHIBITION [00393] For all polypeptide solutions, Image J (Fiji) was used to analyze the mean grain size (MGS) of the ice crystals. For each cooling splat, three images were taken of different areas of the crystal. Briefly, ice crystals were traced by hand to determine the MGS. Statistical analysis showed that the 150 μm × 150 μm region of the image resulted in a MGS that is reprehensive of the entire population. The region of the image to analyze was randomly selected. For samples that resulted in little to no IRI activity, 75 crystals were circled moving radially outward from a randomly selected point. In all cases, three images were collected for each splat assay, and the ice crystal areas for each image were averaged. The average and standard deviation of the three images are presented for each splat. g. GENERAL METHOD FOR HUMAN RED BLOOD CELL (HRBC) PREPARATION [00394] hRBCs from a single unidentified patient were received one day after the drawing of the patient blood. Prior to acquiring the cells, the hRBCs underwent one centrifugation step and the plasma and buffy coat were removed. Upon, receiving the cells the hRBCs were dissolved in DPBS and then centrifuged at 500 × g for 5 min. The PBS was removed from the pelleted cells. This process was repeated twice to remove platelets and blood proteins. The hRBC pellet was then resuspended in PBS such that the final volume of cells was -40%. The prepared cells were keptat 4 °C when not in use and all studies were completed within 7 days. h. GENERAL METHOD FOR GLYCOPOLYPEPTIDE CELLULAR INTERNALIZATION STUDIES WITH HEK293 CELLS [00395] HEK 293 cells were plated on three 24 well plates and incubated at 37 °C in 5% CO₂ overnight to allow the cells to adhere. After 24 hours, the cell media was removed. A 100 uM solution of A594-(βGalαGalNAcT0.33-s-A0.66)57 in MilliQ was diluted in complete media to make a 10 uM solution of polypeptide. The solution was sterile-filtered before 300 uL of the solution was applied to the cells. Additionally, 300 uL of complete media was applied to additional wells of cells to serve as the untreated control. The 24 well plates were then placed at 37 °C, RT, and 4 °C to incubate for 1 hour. After one hour, the media was removed and the cells were rinsed 3x with DPBS.500 uL of Hoescht stain was then added to each well and cells were incubated for 10 minutes at room temperature. The cells were then fluorescently imaged to observe the localization of the fluorescent polymer. i. GENERAL METHOD FOR GLYCOPOLYPEPTIDE CELLULAR I^{NTERNALIZATION STUDIES WITH H}RBC^S [00396] 100 uL of washed hRBCs (prepared as detailed above) were added to a 1.5 mL tube in triplicate.11 uL of a 100 uM solution of A594-(βGalαGalNAcT0.33-s-A0.66)57 in MilliQ was added to each vial for a final concentration of 10pM. The vials were then placed at 37°C, RT, and 4 °C to incubate for 1 hour. After one hour, the cells were pelleted by centrifugation at 500 × g for 5 min and the PBS was removed. The cells were rinsed 3× with DPBS and then resuspend.10 uL of cell suspension was applied to a slide and then covered with a coverslip. The cells were then fluorescently imaged to observe the localization of the fluorescent polymer. No internalization was observed. j. GENERAL METHOD FOR FREEZING HEK 293 CELLS FOR CRYOPROTECTION STUDIES [00397] Cells are cultured until 70-80% confluent. Cells are treated with 2 mL of 0.25% trypsin + EDTA for 1 min, neutralized with 4 mL of DMEM complete media, and then centrifuged at 125 × g for 3 min to pellet the cells. The media and trypsin are aspirated away and the pellet is resuspended in cryoprotection media. The 1 mL volumes of suspension were transferred into 2 mL cryovials and placed in a CoolCell (Corning) or Mr. Frosty (Nalgene) controlled freezing unit inside a -80 °C freezer for 24 hrs. After 24 hrs, the vials are thawed and analyzed. k. GENERAL METHOD FOR THAWING HEK 293 CELLS FOR CRYOPROTECTION STUDIES [00398] To thaw frozen cells used cryopreservation studies, cryovials containing 1 mL of cells in cryoprotection media (DMEM with 10% FBS) are transferred from -80 °C to a bed of dry ice. The vials are then rapidly thawed in a 37 °C bath until the ice disappears. The cell suspension is then diluted 10-fold into pre-warmed complete media (DMEM with 10% FBS supplemented with 1% penicillin-streptomycin and 1% L-glutamine) dropwise. The suspension is then centrifuged and the media is aspirated. The cell pellet is resuspended in complete media and a trypan blue assay is performed to determine cell membrane integrity. l. GENERAL METHOD DETERMINING MEMBRANE INTEGRITY WITH TRYPAN BLUE ASSAY [00399] 10 uL of cell suspension is added to 10 uL of trypan blue and mixed. Then 10 uL of the combined solution is applied to a hemocytometer and the total number of cells and the number of blue cells were counted. The percent of cells with intact membranes was determined using the following equation.

m. G^{ENERAL METHOD FOR FREEZING AND THAWING H}RBC^{S FOR} CRYOPROTECTION STUDIES [00400] The cryopreservation of hRBC was conducted following published procedures (Sun, Y.; et al., (2022) Biomacromolecules, 23(3), 1214-1220). In short, 50 uL hRBCs (prepared as discussed previously) were mixed with 50pL of DPBS containing cryoprotectants or control solution in cryovials. The vials were then placed in a liquid nitrogen bath for 20 mins. The samples were then thawed at room temperature for 20 mins. Control samples were also prepared according to this publication. hRBCs were added to water and frozen for 100% hemolysis and for 0% hemolysis, hRBCs were incubated with DPBS at room temperature for 1 hr. For all hRBC cryopreservation experiments, 2-hydroxyethyl starch (Spectrum Chemical, H3012) was used. n. G^{ENERAL METHODS FOR MEASURING H}RBC ^{HEMOLYSIS AND CELL} RECOVERY [00401] Hemolysis and cell recovery were determined with modifications to published procedures (Sun, Y.; et al., (2022) Biomacromolecules, 23(3), 1214-1220)^. After thawing 60 uL of cell suspension was diluted into 540pL of DPBS and centrifuged at 500 × g for 5 min. Then 20 uL of the supernatant was added to 480 pL of DPBS.100 uL of this solution was added to a 96-well plate in triplicate. The absorbance at 414 nm was measured. Hemolysis and cell recovery were determined following the equations in the published procedure (Sun, Y.; et al., (2022) Biomacromolecules, 23(3), 1214-1220). 3. D^ISCUSSION [00402] Without wishing to be bound by theory, tuning of AFGP structure might finally shed light on the various molecular characteristics that drive ice-binding and cryopreservation properties. Here, the application of amino acid N-carboxyanhydride (NCA) polymerization to prepare a small panel of synthetic AFGPs (sAFGPs) is described. The NCA method allows exquisite tuning of the polypeptide backbone MW, composition, and glycosylation simply by monomer and catalyst feed ratios (FIG.1B–F) (Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461; Kramer, J. R.; et al., (2015) Proc. Natl. Acad. Sci.112 (41) 12574–12579. Only milligram quantities of sAFGPS were required, but it is notable that the sAFGP building blocks were prepared on gram-scale and the NCA method even used commercially (Campos-García, V. R.; et al., (2017) Sci. Rep.7 (1), 1–12). sAFGP amino acid composition, MW, and glycans were varied to reveal molecular mechanisms of ice- binding. Further, the interaction of sAFGPs was probed with model biological systems to characterize biodegradation, cytocompatibility, cellular internalization, and cellular cryopreservation. [00403] Refereing to FIG.1A-F, structure of native AFGPs and preparation of sAFGP panel are shown. FIG.1A shows the chemical structure of the AFGP tripeptide repeat and native PPII helical conformation. FIG.1B shows the preparation of tunable sAFGPs by NCA polymerization using transition metal catalysis. FIG.1C shows the structures of the five glycans utilized in the sAFGP panel. sAFGPs were prepared with varying ratios of Ala:glyco- Thr (FIG.1D), molecular weights (FIG.1E), and glycans (FIG.1F). a. DESIGN AND SYNTHESIS OF SAFGP PANEL [00404] Using previously established methods, a panel of sAFGP glycopolypeptides was synthesized via transition metal initiated polymerization of NCAs (FIG.1B)(Kramer, J. R.; et al., (2015) Proc. Natl. Acad. Sci.112(41), 12574–12579; Deleray, A. C.; Kramer, J. R. (2022) Biomacromolecules 23, 3, 1453–1461. High MW native AFGPs (i.e.50–150 residues, 10.5–34 kDa) are reported to have higher antifreeze activity as compared to those of low MW (i.e.12–38 residues, 2.6–7.9 kDa)(DeVries, A. L. (1986) Methods Enzymol., 127(C), 293– 303). However, these experiments were conducted on pooled fractions of varied molar masses since separation of precise MWs is challenging. Therefore, to explore the role of molar mass on antifreeze activity structures were prepared ranging from 28–170 residues (FIG.1E). [00405] Previous work on the role of glycosylation in IRI indicated that activity is reduced or eliminated for structures with missing, oxidized, or peracetylated sugars (Budke, C.; et al., (2014) Cryst. Growth Des.14(9) 4285–4294; Sun, Y.; et al., (2021) Biomacromolecules 22(6), 2595–2603). Tachibana et al. later compared AFGP peptides with 2–7 repeats bearing various glycans or naked Thr (Tachibana, Y.; et al., (2004) Angew. Chemie - Int. Ed.43(7) 856–862). Drastic changes in TH and IRI behavior were observed with only slight structural variations and they report the α-glycosidic linkage and the C2 NHAc group as particularly important for activity. Other studies propose that the Thr methyl group plays a role as well (Pandey, P.; et al., (2019) Phys. Chem. Chem. Phys.21(7) 3903–3917; Carvajal-Rondanelli, et al., (2011) Journal of the Science of Food and Agriculture.91(14) 2507-2510; Nagel, L.; et al., (2012) Beilstein J. Org. Chem.8, 1657–1667). While informative, these studies utilized low MW peptides that can only make a few helical turns in the PPII structure, and even that is unlikely considering that end-groups typically have greater conformational freedom. [00406] To explore the role of glycosylation in PPII structure and antifreeze activity in sAFGPs, glyco-Thr conjugates and glyco-Ser conjugates were prepared bearing ^Gal, βGal, ^GalNAc, βGalNAc, or native disaccharide βGal(1→3)αGalNAc, which were abbreviate as βGalαGalNAc (FIG.1C and FIG.1F). The number of available hydrogen bonds to interact with ice or water will differ in these glycans. Additionally, there could be structural effects. Danishefsky and Chûjô proposed, based on NMR studies on 5-residue glycopeptides, that an intramolecular hydrogen bond between the N-acetyl group and the Thr carbonyl could be the molecular force stabilizing the PPII structure (Mimura, Y.; et al., (1992) Int. J. Biol. Macromol.14(5), 242–248; Coltart, D. M.; et al., (2002) J. Am. Chem. Soc.124(33), 9833– 9844). However, recent CD studies of high MW glycosylated polyThr indicated that the PPII conformation is adopted in structures lacking the N-acetyl group (i.e. Gal rather than GalNAc)( Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461). Polypeptide structure with varied glycans and anomeric orientations has not been probed in combination with Ala in the context of high MW sAFGPs. [00407] Despite nearly 70 years of study, there is still debate as to the molecular details of AFGP ice-binding and the role of hydrophobic Ala methyls vs. hydrophilic sugar hydroxyls. The generally accepted mechanism is via adsorption−inhibition where the protein adopts an ice-binding surface and a non-binding surface (Knight, C. A.; et al., (1995) Cryobiology, 32(1), 23–34; Raymond, J. A.; DeVries, A. L. (1977) Proc. Natl. Acad. Sci. U. S. A.74(6), 2589–2593; Liu, K.; et al., (2016) Proc. Natl. Acad. Sci. U. S. A.113(51), 14739–14744; Ben, R. N. (2001) ChemBioChem 2(3), 161–166). After adsorption to an embryonic ice crystal via the binding surface, the protein non-binding face causes disorder in approaching liquid water molecules. This results in inhibited crystal growth, shaping of ice crystals, and lowering of the Tm. Molecular dynamics modeling of a 14-residue AFGP predicted the PPII secondary structure is essential and that ice-binding occurs via adsorption and nesting of Ala methyls in the cavities at the ice surface, driven by the entropy of dehydration (Mochizuki, K.; et al., (2018) J. Am. Chem. Soc.140(14), 4803–4811). An alternative modeling approach proposed amphipathic binding where both the Ala methyls and glycan hydroxyls cooperatively bind to ice (Pandey, P.; et al., (2019) Phys. Chem. Chem. Phys.21(7) 3903–3917). Ice-binding via the hydrophilic hydroxyls has also been proposed based on experimental data where fluorescently labeled 40-residue AFGPs were observed on specific ice crystal faces and antifreeze activity could be disrupted by sugar-complexing borate (Berger, T.; et al., (2019) J. Am. Chem. Soc.141(48), 19144–19150; Tsuda, S.; et al., (2020) Biomolecules 10(3), 423; Mochizuki, K.; et al., (2018) J. Am. Chem. Soc.140(14), 4803–4811; Meister, K.; et al., (2018) J. Am. Chem. Soc.140 (30), 9365–9368; Ebbinghaus, S.; et al., (2010) J. Am. Chem. Soc.132(35), 12210–12211). Additionally, low MW AFGPs have a higher adsorption affinity for hydrophilic vs. hydrophobic surfaces (Sarno, D. M.; et al., (2003) Langmuir 19(11), 4740–4744; Younes-Metzler, O.; et al., (2011) Colloids Surfaces B Biointerfaces 82 (1), 134–140) and the βGal(1→3)αGalNAc AFGP disaccharide alone as a monolayer can affect ice shaping (Hederos, M.; et al., (2005) J. Phys. Chem. B 109(33), 15849–15859). [00408] To probe the role of Ala methyls vs. glycan hydroxyls in sAFGP structure and activity, glycopolypeptides were prepared with varied densities of the two residues. The native amino acid ratio is 2:1 Ala:Thr. The ratio of glycan hydroxyls was increased by increasing the ratio to 1:1 or 1:2 (FIG.1D). [00409] Ala NCA was prepared from commercially available Ala in one step by treatment with phosgene in tetrahydrofuran (THF)( Kramer, J. R.; et al., (2015) Proc. Natl. Acad. Sci. 112(41), 12574–12579). Peracetylated glyco-Thr amino acid conjugates and peracetylated glyco-Ser amino acid conjugates were prepared using literature protocols (Tseng, P. H.; J et al., (2001) Chem. - A Eur. J. (3), 585–590; Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461; Lambu, M. R.; et al., (2014) RSC Adv.4(22), 11023–11028) and further described herein. For conversion to NCAs, all glyco-Thr and glycol-Ser conjugates were utilized in their tert-butyloxycarbonyl (Boc) protected forms. Prior work on the preparation of glycosylated or acetylated polyThr determined that direct phosgenation in the same manner as Ala results in poor NCA yields (Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461). However, treatment of glyco-Boc-Thr and glyco-Boc-Ser with triphosgene and triethylamine in THF resulted in good yields and complete conversion to NCA. In all cases, NCAs were isolated by anhydrous column chromatography in the fume hood to give highly pure crystalline monomer (Kramer, J. R.; Deming, T. J. (2010) Biomacromolecules, 11(12), 3668–3672). [00410] Glyco-Thr, glyco-Ser, and Ala NCAs were converted to sAFGPs using (PMe3)4Co catalyst in THF (FIG.1B). NCA:catalyst ratios were varied to tune chain length and various monomer feed ratios were employed to tune sAFGP composition. Reactions proceeded efficiently with complete monomer consumption as evidenced by attenuated total reflectance- Fourier transformed infrared spectroscopy (ATR-FTIR). Disappearance of the NCA carbonyl stretches at ca.1850 and 1790 cm^-1 was observed and appearance of peptide carbonyl stretches at ca.1650 and 1540 cm^-1 (FIG.7). FIG.8A-C show the ATR-FTIR spectrums for NCA monomers and FIG.9A-G shows ATR-FTIR spectrums for synthesized sAFGPs^. Peracetylated sAFGPs were characterized by ¹H

NMR and size exclusion chromatography coupled to multi-angle light scattering and refractive index (SEC/MALS/RI) run in dimethylformamide (DMF) with 0.1M LiBr. Representative SEC/MALS/RI data is shown in FIG.2A. MW and degree of polymerization (DP) correlated well with expected values. Representative GPC/MALS data for ( βGal ^GalNAcT_0.33-s-A_0.66)₇₈ is shown in FIG.10. AFGP polypeptides used in this study are summarized in Table 1. [00411] Table 1 shows the antifreeze polymer panel nomenclature, molar masses, and chain lengths for glycosylated threonine polymers. TABLE 1.

[a] Sample name and amino acid composition. [b,c] M_n, and Ð as

determined by SEC/MALS/RI in DMF with 0.1M LiBr at 60 °C. All polymers were analyzed in their peracetylated forms. - indicates samples which were insoluble in the SEC mobile phase and were therefore analyzed by ¹H NMR and Ð was not determined. [d] Observed degree of polymerization (DP). [00412] Table 2 shows the antifreeze polymer panel nomenclature, molar masses, and chain lengths for glycosylated serine polymers. TABLE 2.

[a] Sample name and amino acid composition. [b,c] M_n, and Ð as determined by SEC/MALS/RI in DMF with 0.1M LiBr at 60 °C. All polymers were analyzed in their peracetylated forms. - indicates samples which were insoluble in the SEC mobile phase and were therefore analyzed by ¹H NMR and Ð was not determined. [d] Observed degree of polymerization (DP). b. C^{HARACTERIZATION OF S}AFGP ^STRUCTURE [00413] CD spectroscopy was used to characterize the secondary structures of our panel of sAFGPs. Distinct signatures are observed for the η→π* and π

transitions of PPII, disordered, sheet, or α-helical conformations (Lopes, J. L. S.; et al., (2014) Protein Sci. 23(12), 1765–1772; van Stokkum, I. H.; et al., (1990) Anal. Biochem.191(1), 110–118; Provencher, S. W.; Glöckner, J. (1981) Biochemistry 20(1), 33–37; Chemes, L. B.; et al., (2012) Methods Mol. Biol.895, 387–404). The α-helix is characterized by ellipticity minima at 222 and 208 nm and a maximum at 195 nm; PPII by a small positive maximum at ~218 nm and a large negative minimum at ~197nm; β-sheets by a positive band at ~198 nm and negative band from ~214 to 218 nm; disordered by no positive maximum and minor negative absorbances below 200 nm. PolyAla is a known α-helix former (Yang, J.; et al., (1998) J. Am. Chem. Soc.120(41), 10646–10652). Homopolymers of βGalNAc- or βGalαGalNAc-Thr have not been previously prepared; however, our previous work on αGalNAc-, αGal-, and βGal-bearing polyThr revealed they adopt extended PPII conformations (Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461). It should be noted the αGalNAc amide absorbs with positive ellipticity between 190–200nm (Deleray, A. C.; et al., (2022) Biomacromolecules 23(3), 1453–1461), overlapping with the peptide π

* transition. [00414] For sAFGPs with native 1:2 Thr:Ala and native βGalαGalNAc disaccharide, secondary structures were observed that were dependent upon MW (FIG.2B). The 28mer, which correlates to native AFGP7–AFGP6, adopts a mix of disordered and PPII conformations as evidenced by spectral alignment with that of denatured collagen and known intrinsically disordered proteins (Lopes, J. L. S.; et al., (2014) Protein Sci.23(12), 1765– 1772; Chemes, L. B.; et al., (2012) Methods Mol. Biol.895, 387–404) but with a small absorbance at ~217 nm in the PPII region. This observation is rational considering the PPII helix requires 3 residues per turn. Therefore, a 28mer could only make 9 turns and that is assuming the end-groups participate. It is well known that helical propensity and per-residue dichroism increase with increasing chain length (Kramer, J. R.; et al., (2015) Proc. Natl. Acad. Sci.112(41), 12574–12579; Detwiler, R. E.; et al., (2021) J. Am. Chem. Soc.143(30), 11482–11489). Without wishing to be bound by theory, this phenomenon nicely explains the classic PPII structure observed for chains with 57 and 138 residues with maxima at ~217 nm and minima at ~197 nm. These spectra correlate nicely with those of native AFGP5–AFGP2 (Sun, Y.; et al., (2021) Biomacromolecules 22(6), 2595–2603). Spectra obtained in phosphate buffered saline (PBS) were identical to those obtained in Milli-Q water (FIG.11) and the sAFGP conformation was stable from 4–50 °C (FIG.12). [00415] The disaccharide sAFGP 170mer, which is higher MW than the largest natural AFGP1 of 150 residues, appears to adopt a mix of conformations. This was reproducibly observed over multiple different batches and spectral runs. Without wishing to be bound by theory, the conformation could be a mixture of PPII and α-helical due to the shift of minima to 203nm and the development of a minimum at 223nm. One potential explanation is that larger structures allow formation of Ala-rich microdomains; though, it is surprising that an increase of only 32 residues could result in this effect. However, α-helical conformations have higher intensity absorbances at identical protein concentrations as compared to PPII conformations and therefore could be of low relative abundance. In any case, it was found that the low MW sAFGPs are far less ordered than those of high MW AFGPs which sheds light on the observed antifreeze activity of native AFGPs. [00416] Glycopolypeptides with increasing βGalαGalNAcThr content and decreasing Ala content resulted in a proportional increase in extended PPII structure as evidenced by the increase in positive ellipticity at ~217nm (FIG.2C). The disaccharide-Thr residues are clear drivers of the PPII conformation. Attempts to prepare and examine glycopolypeptides with higher Ala content than 66% were unsuccessful due to the hydrophobicity of Ala resulting in insoluble structures. [00417] Glycan identity also plays a role in sAFGP conformation. Compared to 1:2 Thr:Ala structures bearing native disaccharide βGalαGalNAc, polymers truncated to monosaccharide αGalNAc had lower PPII helical propensity as evidenced by reduced intensity of the absorbance at 217 nm (FIG.2D). This band is either further reduced or disappears for polymers bearing αGal, βGal, βGalNAc which adopt predominantly disordered conformations. Collectively, these data indicate that the NAc group on Gal in the α-linkage partially orients the peptide backbone into PPII helices, and that the structure is further stabilized by the extension of the glycan with βGal(1→3). [00418] Refering to FIG.2A-D, the characterization of sAFGP molar masses and conformations was obtained. FIG.2A shows SEC/MALS/RI indicating differing elution times for peracetylated chains of increasing lengths. FIG.2B–D shows the aqueous CD spectra of deacetylated sAFGPs where FIG.2B are structures with increasing molecular weights, FIG.2C are structures with increasing βGalαGalNAcThr content, and FIG.2D are structures bearing glycans of differing identity and anomeric orientation. FIG.13 shows CD spectra of (βGalT_x-s-A_y)_n at various amino acid concentrations. Spectra in MilliQ at 25 °C. FIG.14 shows CD spectra of (βGalNAcTx-s-Ay)n at various amino acid concentrations. An increase in 6.6% GalNAcThr content increases the solubility of the polymer. Spectra in MilliQ at 25 °C. c. SAFGP ANTIFREEZE ACTIVITY ASSAYS [00419] To investigate the antifreeze properties of the sAFGP structures, IRI activity was quantified and examined ice-shaping properties. For the quantification of IRI activity, cooling splat assays were employed as developed by Knight et al (Knight, C. A.; et al., (1984) Nature 308(5956), 295–296). In short, a solution of sAFGP in PBS was dropped onto a glass slide at -78.5 °C to form a thin wafer. Use of PBS or a saline solution is essential due to the overestimation of IRI activity if observed in pure water (Knight, C. A.; et al., (1995) Cryobiology, 32(1), 23–34; Biggs, C. I.; et al., (2019) Macromolecular Bioscience 19(7)). The wafer was imaged at -6.4 °C at various timepoints on a temperature-controlled microscope stage. Typically, ice wafers are annealed at a temperature ranging from 6–8˚C to ensure that a eutectic phase is present at the crystal boundary and the ice is able to undergo recrystallization water (Knight, C. A.; et al., (1995) Cryobiology, 32(1), 23–34; Biggs, C. I.; et al., (2019) Macromolecular Bioscience 19(7)). From the images, ice MGS was determined using image processing software or manual measurements. To ensure statistical significance, three images were obtained for each sample, and grain sizes within a minimum of three 150 µm² regions per sample were measured. Regions toward the center of the wafer, rather than near the edges, were selected. Pure PBS was selected as a control and 5 weight % dimethylsulfoxide (DMSO) for comparison since this is a common molecule utilized in cellular cryopreservation (Liu, Z.; et al., (2022) J. Am. Chem. Soc.144(13), 5685–5701). [00420] Native AFGPs are known to influence ice crystal shape by irreversible binding to the prism faces of embryonic ice crystals (FIG.3A). Adsorption binding by AFGPs inhibits crystal growth on the prism faces resulting in formation of characteristic hexagonal crystals that grow along the c-axis and eventually form bipyramidal spicular crystals (Meister, K.; et al., (2018) J. Am. Chem. Soc.140 (30), 9365–9368). Ice-shaping can be observed via cryostage microscopy by raising the temperature of an ice wafer until only single crystals remain. The temperature is then lowered gradually and the slow growth of the single crystals is imaged. [00421] Ice-shaping and IRI results for sAFGPs of ca.50 residues and with varied βGalαGalNAcThr:Ala ratios are shown in (FIG.3B-D). It was found that both IRI activity and ice-shaping properties increased with increasing Ala content (FIG.3B-D). Polymers with 33% Ala displayed no IRI activity since there was no statistical difference in MGS relative to PBS alone. Similarly, there was no observable effect on ice crystal shape. An increase in Ala content to 50% resulted in minor IRI activity as evidenced by a 22% reduction in relative MGS. These polymers had little effect on crystal shape. By contrast, sAFGPs with the native 66% Ala and 33% βGalαGalNAcThr displayed potent IRI activity. Relative MGS was reduced by a remarkable 95%, which is analogous to the activity of native AFGPs (Liu, S.; et al., (2018) Org. Lett.7(12), 2385–2388; Biggs, C. I.; et al., (2019) Macromolecular Bioscience 19(7), 1900082; Balcerzak, A. K.; et al., (2014) RSC Adv.4(80), 42682–42696). Additionally, these polymers demonstrated essentially identical ice-shaping properties to those of native AFGPs (Berger, T.; et al., (2019) J. Am. Chem. Soc.141(48), 19144–19150; Meister, K.; et al., (2018) J. Am. Chem. Soc.140 (30), 9365–9368). It was observed that single crystals adopted predominantly hexagonal and bipyramidal structures, indicating that the sAFGPs bind to the prism plane of the crystal inducing c-axis growth. Without wishing to be bound by theory, these data indicate that Ala is required for the ice-binding properties of (s)AFGPs. [00422] Referring to FIG.3A-D, ice binding properties of sAFGPs with varying amino acid compositions are shown. FIG.3A shows a cartoon illustration of ice binding and shaping in the presence of sAFGPs composed of 1:2, 1:1, or 2:1 βGalαGalNAcThr:Ala. FIG.3B shows images of cooling splat assays and IRI activity for 71 µM sAFGP or 5 wt.% DMSO in PBS, or PBS alone. FIG.3C shows quantified IRI data as % MGS relative to PBS; mean and standard deviation, ** indicates p < 0.01. FIG.3D shows a ice shaping experiments with 71 µM sAFGP in PBS. [00423] Ice recrystallization inhibition using (GalNAcSer_0.2-s-Ala_0.8)₁₅₀ at 0.5 mg/mL in PBS as compared to PBS alone (scale bar = 200 µm) is shown in FIG.37. [00424] FIG.22 shows images of cooling splat assays and IRI activity for ( βGal ^GalNAcT0.33-s-A0.66)28. FIG.23 shows images of cooling splat assays and IRI activity for ( βGal ^GalNAcT_0.33-s-A_0.66)₅₇. FIG.24 shows images of cooling splat assays and IRI activity for ( βGal ^GalNAcT_0.33-s-A_0.66)₁₇₀. FIG.25 shows images of cooling splat assays and IRI activity for ( βGal ^GalNAcT0.5-s-A0.5)52. FIG.26 shows images of cooling splat assays and IRI activity for ( βGal ^GalNAcT0.66-s-A0.33)46. FIG.27 shows images of cooling splat assays and IRI activity for ( αGalNAcT_0.33-s-A_0.66)₉₉. FIG.28 shows images of cooling splat assays and IRI activity for α GalT0.33-s-A0.66)93. FIG.29 shows images of cooling splat assays and IRI activity for ( βGalNAcT0.33-s-A0.66)93. FIG.30 shows images of cooling splat assays and IRI activity for ( βGalT_0.33-s-A_0.66)₉₃. FIG.31 shows images of cooling splat assays and IRI activity for 28mer, 57mer and 170mer of ( βGalαGalNAcT_0.33-s- A_0.66)_n at 70.7 µM. FIG.32 shows images of cooling splat assays and IRI activity for x:y ratios of 1:2, 1:1, and 2:1 ( βGalαGalNAcT_x-s-A_y)_n at 70.7 µM. FIG.33 shows images of cooling splat assays and IRI activity for sugar residues αGal, αGalNAc, βGal, and βGalNAc glycoT0.33-s-A0.66)93 at 70.7 µM. FIG.34 shows images of cooling splat assays and IRI activity for 28mer, 57mer and 170mer of ( βGalαGalNAcT_0.33-s-A_0.66)_n at 0.5 mg/mL. FIG. 35 shows images of cooling splat assays and IRI activity for sugar residues αGal, αGalNAc, βGal, and βGalNAc glycoT0.33-s-A0.66)93 at 0.5 mg/mL. FIG.36 shows images of cooling splat assays and IRI activity for controls with PBS, 5% DMSO, 10% DMSO, 50 µM PVA and 100 µM PVA. [00425] IRI and ice-shaping were also dependent upon sAFGP molecular weight (FIG.4A- C). Polymers of the native 1:2 βGalαGalNAcThr:Ala ratio and degrees of polymerization of 28, 57, or 170 had IRI activity that increased with chain length. Absolute MGS is shown in FIG.4A and MGS relative to PBS is shown in FIG.4B. Compared to ice MGS in PBS alone, sAFGP 28mers offered an 89% reduction, 57mers a 94% reduction, and 170mers a 97% reduction. These data correlate nicely with literature reports on fractionated native AFGPs where pooled structures of MWs ranging from 33.7–10.5kDa (AFGP1-5) showed higher antifreeze activity than structures of 2.65 kDa (AFGP8)( Budke, C.; et al., (2014) Cryst. Growth Des.14(9) 4285–4294; Meister, K.; et al., (2018) J. Am. Chem. Soc.140 (30), 9365–9368). Ice-shaping ability also increased with sAFGP chain length since 28mers yielded amorphous, rounded crystals similar to those formed in PBS alone, while crystals formed in the presence of 57mers and 170mers had angular faces with hexagonal or rectangular shapes (FIG.4C). FIG.15 shows ice shaping of ( βGalαGalNAcT_0.33-s-A_0.66)_n where DP = 28, 57, 170 at 0.5 mg/mL. Scale bar = 100 μm. FIG.16 shows ice shaping of (glycoT_0.33-s-A_0.66)₉₃ at 0.5 mg/mL. Scale bar = 100 μm. [00426] Finally, the ice-shaping and IRI activity of polymers bearing varied glycans and with the native 1:2 Thr:Ala ratio was investigated. A moderate chain length of ca.90 amino acids was targeted since native AFGPs range from 12–150 residues. IRI experiments were conducted side-by-side with varied chain lengths of sAFGPs with the native disaccharide, emerging cryoprotectant PVA, and common cryoprotectant DMSO at 5 weight %. Two PVA (MWavg 13–23kDa) concentrations were selected based on literature values (Inada, T.; Lu, S. S. I; (2003) Cryst. Growth Des.3 (5), 747–752; Congdon, T.; et al., (2013) Biomacromolecules 14(5), 1578–1586). [00427] FIG.17 shows quantified IRI data as % MGS relative to PBS for ( βGal ^GalNAcT0.33-s-A0.66)170, PVA, and DMSO. sAFGP concentration is 71 µM in PBS. PVA concentrations are indicated on plot. PVA and DMSO in PBS. IRI experiments were conducted alongside the emerging cryoprotectant PVA (MWavg 13–23kDa, similar to the MW range of native AFGPs). 5% DMSO was selected because it is commonly used as a cryoprotective agent at this concentration. Ice crystal MGS was determined from cooling splat assays. Mean and standard deviation are plotted. Statistical significance presented in Table S1. [00428] As shown in FIG.4B, all sAFGPs independent of glycan identity displayed excellent IRI activity. sAFGPs lacking NAc groups (αGal and βGal) had slightly lower activity than structures with NAc (αGalNAc and βGalNAc), but were still potent antifreeze molecules. Ice crystal MGSs from solutions of (αGalT0.33-s-A0.66)93 and (βGalT0.33-s-A0.66)93 were reduced to 12% and 15% of the MGS of PBS alone. (αGalNAcT_0.33-s-A_0.66)₉₃ and (βGalNAcT0.33-s-A0.66)93 were more active and resulted in MGSs that were 8% and 5% of the MGS of PBS. IRI activity on mass rather than a molar basis was also compared and a similar trend was observed where the NAc glycans had higher activity (see SI).5% DMSO resulted in only a 54% relative reduction. [00429] Referring to FIG.4A-C, ice binding data for sAFGPs composed of the native 1:2 glycoT:A ratio and with varied chain lengths and varied glycan structures is shown. FIG.4A shows the observed absolute MGS at varied concentrations for sAFGPs with the native βGalαGalNAc disaccharide and with chain lengths of 28, 57, 170 residues. FIG.4B shows the quantified IRI data as % MGS relative to PBS for native disaccharide sAFGPs of varied chain lengths as compared to sAFGP 93mers bearing glycans of varied structure and anomeric linkages, PVA, or DMSO; sAFGP concentration is 71 µM in PBS; PVA and DMSO are at the indicated concentrations in PBS; ice crystal MGS was determined from cooling splat assays; mean and standard deviation; table of statistical significance is in the SI. FIG.4C shows the ice shaping experiments for native disaccharide sAFGPs of varied chain lengths as compared to sAFGP 93mers bearing glycans of varied structure and anomeric linkages; sAFGP concentration is 71 µM in PBS. [00430] IRI activity of lower MW ( βGalαGalNAcT_0.33-s-A_0.66)₅₇ was comparable to that of higher MW (βGalNAcT_0.33-s-A_0.66)₉₃ at equivalent concentrations. Ice-binding and IRI activity of PVA is known to increase with increasing MW (Inada, T.; Lu, S. S. I; (2003) Cryst. Growth Des.3 (5), 747–752; Congdon, T.; et al., (2013) Biomacromolecules 14(5), 1578–1586; Georgiou, P. G.; et al., (2022) Biomacromolecules 23(12), 5285–5296;Budke, C.; Koop, T. (2006) ChemPhysChem 7(12), 2601–2606). Therefore, PVA of 13–23 kDa was selected as sample similar to the molar mass range of native AFGPs and our sAFGPs for comparison. In a side-by-side comparison, a higher concentration of 100 µM PVA was required to achieve a similar reduction in MGS as our sAFGPs. IRI activity on a mass rather than molar basis was also examined but the same trends were observed (see SI). Overall, the highest MW sAFGP ( βGalαGalNAcT_0.33-s-A_0.66)₁₇₀ demonstrated the strongest IRI properties. [00431] Prior work has shown loss of antifreeze activity due to oxidation, alkylation, and borylation of AFGP disaccharides (Sun, Y.; et al., (2021) Biomacromolecules 22(6), 2595– 2603; Shier, W. T.; et al., (1972) BBA - Protein Struct.263(2), 406–413). The most comprehensive and widely cited study of glycan structure to date was conducted by Tachibana et al. nearly 20 years ago (Tachibana, Y.; et al., (2004) Angew. Chemie - Int. Ed. 43(7) 856–862). Synthetic AFGP fragments were prepared by coupling Ala-Ala-Thr tripeptide monomers using diphenylphosphorylazide. The Thr bore the native disaccharide with α vs β linkage, αGal vs αGalNAc, and several other glycan structures. In this study, the α-linkage, the C2 NAc group, and the disaccharide were essential for activity. The data as described herein is in stark contrast. Structures bearing both mono- and di- saccharides, α and β linkages, and with and without C2 NAc all have potent IRI activity. In the prior work, conclusions were drawn from structures with only ca.6–9 amino acids. Here, the structures are on par with native AFGPs of up to 150 residues. Interestingly, the data also indicate the tripeptide repeat is unnecessary since our structures have statistically distributed residues. [00432] Ice-shaping trends generally followed that of IRI where polymers with higher IRI activity more strongly induced growth along the crystal c-axis (FIG.4C). sAFGPs presenting αGal or βGal induced a mixture of rounded amorphous and rectangular morphologies, while crystals formed in the presence of αGalNAc- or βGalNAc-bearing polymers essentially all adopted angular-faced ordered structures. Interestingly, (αGalNAcT0.33-s-A0.66)93, which bears a truncated version of the native disaccharide, induced predominantly hexagonal crystal growth similar to crystals formed from solutions of native AFGPs (Budke, C.; et al., (2014) Cryst. Growth Des.14(9) 4285–4294; Meister, K.; et al., (2018) J. Am. Chem. Soc.140 (30), 9365–9368) and the disaccharide sAFGPs (identical chemical composition to native AFGP). Without wishing to be bound by theory, these data indicate that the αGalNAcThr group is important for ice-binding. The intramolecular hydrogen bond between the NAc and the peptide carbonyl observed by others (Mimura, Y.; et al., (1992) Int. J. Biol. Macromol.14(5), 242–248; Coltart, D. M.; et al., (2002) J. Am. Chem. Soc.124(33), 9833–9844) could potentially orient the Thr methyl groups favorably for interaction with ice surfaces or induce long-range structural effects optimal for ice-binding. d. CYTOCOMPATIBILITY, CELL INTERNALIZATION, AND DEGRADATION OF SAFGPS [00433] Considering the many biomedical applications of sAFGPs, information was sought about their interaction with living tissues in terms of cytotoxicity, degradation, and cellular internalization. In Antarctic fish, AFGPs were found in the interstitial fluid of all body tissues examined except brain tissue, but no tissue showed any intracellular accumulation of AFGPs from the blood (Ahlgren, J. A.; et al., (1988) J. Exp. Biol.137549–563). However, little is known regarding intracellular accumulation of AFGPs, or synthetic mimics, in the context of cryopreservation applications. A single report describes rapid internalization of fluorophore- labeled AFGP8 (1.5 mg/mL, 37 °C) in both WRL 68 human embryonic liver cells and trout gill cells (Lui, S.; et al., (2007) Biomacromolecules 8(5) 1456–1462). [00434] To investigate if cellular internalization is relevant to cryopreservation applications, ( βGal ^GalNAcT0.33-s-A0.66)57 was fluorescently tagged with AF594 using N- hydroxysuccinimide ester chemistry. For internalization experiments, human red blood cells (hRBCs) and white blood cells (Raji) were selected as suspension cell models of therapeutic interest and human embryonic kidney (HEK) 293 cells as an adherent cell line in widespread laboratory use. HEK293 cells were also selected to benchmark against the previously described internalization study using native AFGP8. All cells were incubated with 10 µM sAFGP-594 for 1 hour at 37 °C and then imaged. It was found that the sAFGPs were substantially internalized and localized throughout Raji and HEK cells but did not accumulate in hRBCs ((FIG.5A) for HEK, for Raji (FIG.18) and hRBC data)). Since mature mammalian RBCs do not endocytose under normal conditions (Schekman, R.; Singer, S. J. (1976) Proc. Natl. Acad. Sci. U. S. A.73(11) 4075–4079), Without wishing to be bound by theory, the uptake mechanism was believed to be endocytic rather than passive translocation across the cell membrane. To further validate the sAFGPs are endocytosed, internalization was examined at temperatures endocytosis is inhibited (4 °C, 23 °C) and little to no sAFGP was observed inside the cells (FIG.5A). Further studies are underway to determine the precise endocytic mechanism at play. [00435] With the knowledge that the sAFGPs can be internalized into a variety of cells lines, it needed to be determined if they could be degraded by natural proteases. This would be a stark advantage over other proposed polymeric cryoprotectants. As models, proteinase K (ProK) and secreted protease of C1 esterase (StcE) were chosen. ProK is non-specific and cleaves peptide bonds preferentially after hydrophobic amino acids (Rawlings, N. D.; Salvesen, G. (2013) Handb. Proteolytic Enzym., 1–3 and StcE is a glycoprotease that cleaves before αGalNAc-bearing Ser/Thr residues (Malaker, S. A.; et al., (2019) Proc Natl Acad Sci 116(15) 7278–7287). ( βGal ^GalNAcT0.33-s-A0.66)98 was selected as an sAFGP of moderate molar mass, treated with Pro K and StcE, and aliquots were removed at various timepoints up to one week. Samples were analyzed by SDS-PAGE and stained with a glycoprotein-specific fluorescent stain. It was found that ProK efficiently degraded the sAFGP within 3 hours while StcE only partially degraded the sample over the course of a week (FIG.5B). StcE apparently prefers the monosaccharide over the AFGP disaccharide. In any case, the sAFGPs are can be degraded by natural proteases. FIG.19 shows how the concentration of sAFGP needed for protease digestion studies using SDS-Page was determined. ( βGal ^GalNAcT_0.33- s-A_0.66)₅₇ was used for this experiment. [00436] Finally, the structures were examined for cytocompatibility. Without wishing to be bound by theory, no toxic effects were expected due to our sAFGPs considering that native AFGPs are present at up to 4 weight % (~25 mg/mL) in fish blood (Devries, A. L. (1982) Comp. Biochem. Physiol. -- Part A Physiol.73(4) 627-640) and various similar synthetic glycopolypeptides have been shown by our lab and others to be non-toxic and well tolerated by human cells (Kramer, J. R.; et al., (2015) Proc. Natl. Acad. Sci.112(41), 12574–12579; Clauss, Z.S., et al., (2021) Nat Commun 12, 6472; Shi, S.; et al., (2021) Sci. China Technol. Sci.64(3), 641–650; Leclère, M.; et al., (2011) Bioconjug. Chem.22(9), 1804–1810). ( βGalαGalNAcT0.33-s-A0.66)57 and HEK293 cells were selected as a representative model since it had already validated cell internalization in this pair. CCK8 assays were conducted after 24 hours of treatment at 37 °C with varied sAFGP concentrations relevant to IRI activity. Cells were treated with media alone as a negative control and Triton X-100 as a positive control. At the highest sAFGP concentration tested, there were no statistically significant effects on cellular viability observed (FIG.5C). It is notable that prior to cryopreservation, cells are typically suspended and growth media is exchanged for freezing media containing suitable cryoprotectant agents. Exposure to cryoprotectants is usually minimal as the media exchange is conducted cold and immediately prior to cell freezing. Considering this workflow, no toxic effects after 24-hour sAFGP exposure at 37 °C indicate these materials are suitable for cryopreservation applications. FIG.20 shows cryopreservation of HEK293 cells with varying treatments. Viability determined by CCK8 assay. Cells treated with 20mg/mL sAFGP ( βGalαGalNAcT0.33-s-A0.66)57 and PVA(MWavg 13-23 kDa. Statistical significance determined with a one-way ANOVA and pos-hoc Tukey tests. ns indicates nonsignificant and **** indicates p<0.00001. [00437] Refereing to FIG.5A-C, cellular internalization, biodegradation, and cytocompatibility of sAFGPs with the native 1:2 glycoT:A composition and bearing the native disaccharide is shown. FIG.5A shows the internalization of sAFGP AF594- ( βGal ^GalNAcT0.33-s-A0.66)57 in HEK293 cells at 0, 23, or 37 ˚C. FIG.5B shows the SDS- PAGE of protease-treated ( βGal ^GalNAcT0.33-s-A0.66)98 at varied timepoints. FIG.5C shows the HEK 293 cell viability as determined by CCK8 assay following 24-hour incubation with sAFGP ( βGal ^GalNAcT0.33-s-A0.66)57 at the indicated concentrations; mean and standard deviation; ** indicates p < 0.01. e. SAFGPS AS CELLULAR CRYOPROTECTANTS [00438] One of the most impactful potential applications of AFGPs is in biomedical cryopreservation. The use of cryoprotective agents to induce vitrification (crystal-free glassy ice) in cell-freezing solutions was first explored in 1949 via glycerol (olge, C.; S et al., (1949) Nature., 164666) and subsequently DMSO (Lovelock, J. E.; Bishop, M. W. H. (1959) Nature, 1834672), 1394–1395). Remarkably, little has changed in over 70 years and growth media supplemented with 5–10 wt. % DMSO or 5–30 wt. % glycerol are still standard freezing protocols for mammalian cells. Both molecules pass through cell membranes and form strong hydrogen bonds with water, slowing diffusion and delaying the formation and growth of ice crystals (He, Z.; L; et al., (2018) Acc. Chem. Res.2018, 51 (5), 1082–1091). However, DMSO and glycerol have well-known toxic effects (Best, B. P. (2015) Rejuvenation Res 18(5), 422; Si, W.; et al., (2004) Am. J. Primatol.62(4), 301–306; Graham, J. E.; et al., (2015) Am. J. Vet. Res.76(6), 487–493; Kielberg, V. (2010) Tech Note 14 (1), 2; Verheijen, M.; et al., (2019) Sci. Rep.9 (1); Hengstler, J. G.; et al., (2000) Drug Metabolism Reviews.3281-118; Fahy, G. M.; (2010) Cryobiology 60(3) S45-s53). HES is a newer potential vitrifying cryoprotectant favorable due to lack of membrane permeability and easy removal by cell washing (Stolzing, A.; N; et al., (2012) Transfus. Apher. Sci.46(2) 137–147; Lionetti, F. J.; et al., (2004) Cryobiology 1976, 13 (5), 489–499). HES is better tolerated by cells than DMSO or glycerol, but is still associated with osmotic shock, apoptosis, and hemolysis at higher concentrations (Stolzing, A.; N; et al., (2012) Transfus. Apher. Sci.46(2) 137–14; Graham, J. E.; et al., (2015) Am. J. Vet. Res.76(6), 487–493). Additionally, excessive solution viscosity presents processing challenges. [00439] AFGPs have been proposed as a solution to replace or reduce reliance on chemical vitrification agents. Decades of literature investigating AFGPs as cryoprotectants report conflicting results on improved viability after freezing for a wide variety of cell types and even whole organs (Robles, V.; et al., (2019) Biomolecules 9(5) 181; Ekpo, M. D.; et al., (2022) Int. J. Mol. Sci. , 23(5) 2639; Payne, S. R.; et al., (1994) Cryobiology 31(2), 180–184; Wang, T.; et al., (1994) Cryobiology 31 (2), 185–192). A careful survey of study methodologies revealed a broad range of protein concentrations (i.e.0.1µg–40 mg/mL), media compositions, and freezing protocols; plus experiments were typically performed in combination with traditional cryoprotectants (glycerol, DMSO, HES) which were also applied in differing concentrations (Hays, L. M.; et al., (1996) Proc. Natl. Acad. Sci. U. S. A. 93(13):6835-6840; Leclère, M.; et al., (2011) Bioconjug. Chem.22(9), 1804–1810; Robles, V.; et al., (2019) Biomolecules 9 (5) 181; Heisig, M.; et al., (2015) PLoS One 10 (2). Overall, the field has not yet achieved consensus on the various factors for optimal cryopreservation nor how antifreeze proteins should be applied. [00440] Therefore, for an initial study examining our sAFGPs as cryoprotectants, a benchmark was chosen against a very recent study utilizing native AFGPs to freeze hRBCs in combination with HES (Sun, Y.; et al., (2022) Biomacromolecules 23 (3), 1214–1220). In the report, flash freezing hRBCs in liquid nitrogen in 130 mg/mL HES solution followed by slow thaw at ~20 °C resulted in 12% survival. Addition of AFGP_1–5 at 1–800 µg/mL resulted in an increase in cell recovery of up to 24%, but the effect did not scale with AFGP concentration and was optimized at 200 µg/mL. Cell survival with PBS alone was 14% and addition of AFGP_1–5 at 0.1–1000 µg/mL was actually detrimental to hRBC survival above 10 µg/mL, when the samples were rapidly thawed at 45˚C. [00441] Flash freezing hRBCs in liquid nitrogen cryoprotection media supplemented with 130 mg/mL HES and 0–400 µg/mL ( βGal ^GalNAcT0.33-s-A0.66)170 resulted in 80% cell recovery after thawing at 23 °C for HES alone (FIG.6A and FIG.6B). Survival was 3% for PBS alone. Data shown in FIG.6A-C are the result of two separate experiments performed in triplicate. Cell survival with HES was so high that any effects from our sAFGPs were not observable. Lower cell survival in the prior work might be attributed to differences in HES molecular weight or functionalization degree, which was not reported. Another potential difference could be in their varying thaw methods which seemed to also affect survival in PBS alone. Further, native AFGPs can only be fractionated and utilized as heterogeneous mixtures of isoforms, thus convoluting data interpretation. In any case, to observe the effects of sAFGPs on cryopreservation, a range where lower cell recovery was observed was sought. Therefore, hRBC hemolysis was examined over a range of HES concentrations (see SI) and selected 40 mg/mL HES since 20% post-thaw viability was observed under these conditions. [00442] hRBCs were again flash frozen with 40 mg/mL HES and supplemented with 0–400 µg/mL sAFGP. After 20 minutes, the samples were thawed at 23 °C and hemolysis assays were conducted. The sAFGPs did not have a statistically significant effect on hRBC survival. Considering the effects of native AFGPs in combination with HES were modest in the prior report, that native AFGPs alone were actually detrimental to the hRBCs, and that decades of literature report disparate outcomes, this result was not surprising. Similar cryopreservation assays were conducted using HEK cells with various freezing methodologies where no strong effects of the sAFGPs were observed (see SI). Considering the potent IRI and ice shaping activity of these molecules essentially equivalent to that of native AFGPs, further work in the area of freezing methodology and HES structure characterization is needed. Work is underway but is outside the scope of this study. [00443] Refering to FIG.6A-C, cryopreservation of hRBCs in sAFGP supplemented HES solutions or PBS alone is shown. FIG.6A shows schematic representation of hRBC cryopreservation experimental workflow and cell hemolysis as the assessment metric of cell survival. FIG.6B and FIG.6C show the post-thaw intact hRBC cell recovery by hemolysis assays after freezing with sAFGP ( βGal ^GalNAcT0.33-s-A0.66)170 and 130mg/mL HES (FIG. 6B) or 40mg/mL HES (FIG.6C). Within each experiment, the cell recovery is not statistically different across the varied treatments. FIG.21 shows cryopreservation of hRBC with varying HES concentrations. f. C^ONCLUSIONS [00444] AFGPs are of great interest for application as cryoprotectants in agriculture, food, surface coatings, and in biomedical tissue cryopreservation. Yet, isolation of AFGPs from polar organisms is cumbersome and impractical, impeding studies of this unique class of structures. Even their molecular mechanisms of action are still debated. Here, a rapid and scalable route to synthetic AFGPs that allows facile tuning of molecular properties from molar mass to glycan and amino acid compositions is presented. A small panel of structures with varied properties was examined and determined hydrophobic Ala plays a key role in ice- binding and that antifreeze activity increases with molecular weight. Five glycan structures were examined and while the native disaccharide was most potent, all displayed antifreeze activity. 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It is intended that the specification and examples be considered as exemplary only, with a true scope and spirit of the invention being indicated by the following claims.

Claims

CLAIMS What is claimed is: 1. A peptide comprising a plurality of alanine residues and a plurality of glycosylated residues selected from glycosylated threonine residues, glycosylated serine residues, and a mixture of glycosylated threonine residues and glycosylated serine residues, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is from about 3:2 to about 4:1, and wherein the peptide has a chain length of at least 30 amino acid residues.

2. The peptide of claim 1, wherein the peptide consists essentially of the plurality of alanine residues and the plurality of glycosylated residues.

3. The peptide of claim 1 or claim 2, wherein the plurality of alanine residues is present in the peptide in an amount of about 70 wt% or less.

4. The peptide of claim 1 or claim 2, wherein the plurality of alanine residues is present in the peptide in an amount of about 66 wt% or less.

5. The peptide of any one of claims 1 to 4, wherein the peptide contains less than 36 sequential Ala-Ala-Thr repeating units.

6. The peptide of any one of claims 1 to 4, wherein the plurality of glycosylated residues are glycosylated with one or more of αGal, βGal, αGalNAc, βGalNAc, βGal(1→3)αGalNAc, αLac, or βLac.

7. The peptide of any one of claims 1 to 6, wherein the plurality of glycosylated residues are glycosylated threonine residues.

8. The peptide of any one of claims 1 to 6, wherein the plurality of glycosylated residues are glycosylated serine residues.

9. The peptide of any one of claims 1 to 6, wherein the plurality of glycosylated residues are a mixture of glycosylated threonine residues and glycosylated serine residues.

10. The peptide of any one of claims 1 to 9, wherein the ratio of the plurality of alanine residues to the plurality of glycosylated residues is not about 2:1.

11. The peptide of any one of claims 1 to 10, wherein the peptide has a chain length of at least 30 amino acid residues.

12. The peptide of any one of claims 1 to 10, wherein the peptide has a chain length of at least 50 amino acid residues.

13. The peptide of any one of claims 1 to 10, wherein the peptide has a chain length of at least 100 amino acid residues.

14. The peptide of any one of claims 1 to 10, wherein the peptide has a chain length of at least 150 amino acid residues.

15. The peptide of any one of claims 1 to 10, wherein the peptide has a chain length of from 30 amino acid residues to 500 amino acid residues.

16. The peptide of any one of claims 1 to 15, wherein the peptide has a number average molecular weight (M_n) of at least about 5,000.

17. The peptide of any one of claims 1 to 15, wherein the peptide has a number average molecular weight (Mn) of at least about 15,000.

18. The peptide of any one of claims 1 to 15, wherein the peptide has a number average molecular weight (Mn) of from about 5,000 to about 50,000.

19. The peptide of any one of claims 1 to 15, wherein the peptide has a number average molecular weight (M_n) of from about 15,000 to about 50,000.

20. The peptide of any one of claims 1 to 19, wherein the peptide has a degree of polymerization (DP) of at least about 25.

21. The peptide of any one of claims 1 to 19, wherein the peptide has a degree of polymerization (DP) of at least about 50.

22. The peptide of any one of claims 1 to 19, wherein the peptide has a degree of polymerization (DP) of at least about 100.

23. The peptide of any one of claims 1 to 19, wherein the peptide has a degree of polymerization (DP) from about 100 to about 330.

24. The peptide of any one of claims 1 to 23, wherein the peptide has a structure represented by a formula:

, wherein n is an integer selected from 15 to about 300; wherein each occurrence of R¹ is independently a monosaccharide moiety or a disaccharide moiety; wherein each occurrence of R² is independently selected from hydrogen and methyl; wherein the ratio of x to y is of from about 2:3 to about 1:4; and wherein the sum of x and y is at least 30, or a pharmaceutically acceptable salt thereof.

25. The peptide of claim 24, wherein x is 6 or greater and y is 18 or greater.

26. The peptide of claim 24, wherein x is 10 or greater and y is 30 or greater.

27. The peptide of claim 24, wherein x is from 20 to 120 and y is from 60 to 180.

28. The peptide of claim 24, wherein x is from 20 to 120 and y is from 60 to 180.

29. The peptide of any one of claims 24 to 28, wherein each occurrence of R¹ is independently selected from a glucose moiety, an N-acetylglmannosamine moiety, a mannose moiety, an N-acetylglmannosamine moiety, a fucose moiety, a sialic acid moiety, a fructose moiety, a lactose moiety, a sucrose moiety, a glucuronic acid moiety, a manuronic acid moiety, a gulose moiety, a guloronic acid moiety, a xylose moiety, a ribose moiety, an allose moiety, an altrose moiety, an idose moiety, and a talose moiety.

30. The peptide of any one of claims 24 to 28, wherein each occurrence of R¹ is independently a monosaccharide moiety or a disaccharide moiety having a structure represented by a formula:

_, wherein each occurrence of R¹⁰ and R¹¹ is independently selected from ‒OH and ‒NHAc.

31. The peptide of claim 30, wherein each occurrence of R¹⁰ is ‒OH.

32. The peptide of any one of claims 24 to 28, wherein each occurrence of R¹ is independently a monosaccharide moiety or a disaccharide moiety having a structure represented by a formula:

wherein each occurrence of R¹⁰ is independently selected from ‒OH and ‒NHAc.

33. The peptide of claim 32, wherein each occurrence of R¹⁰ is ‒OH.

34. The peptide of any one of claims 24 to 33, wherein the ratio of x to y is about 2:3 to about 1:4.

35. The peptide of any one of claims 24 to 34, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

36. The peptide of any one of claims 24 to 34, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

37. The peptide of any one of claims 24 to 34, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

38. The peptide of any one of claims 24 to 34, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

39. The peptide of any one of claims 24 to 34, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

40. The peptide of any one of claims 24 to 34, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

41. The peptide of any one of claims 24 to 34, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

42. The peptide of any one of claims 24 to 34, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

43. The peptide of any one of claims 24 to 34, wherein the peptide has a structure represented by a formula:

, wherein R²⁰ is selected from ‒OR³¹, ‒NHR³², ‒N3, a protein tag, a sortase recognition sequence, a sugar residue, and a structure:

wherein R³¹ and R³² are selected from hydrogen, ‒CH2Ph, C1-C8 alkyl, C2-C8 alkyne, C1-C8 azide, tetrazinyl, cyclooctynyl, norbornenyl, and –(CH₂CH₂O)_mCH₃; and wherein m is an integer selected from 1 to 100.

44. The peptide of claim 43, wherein the protein tag is selected from CBP, FLAG< GST, HA, HBH, MBP, Myc, poly His, S-tag, SUMO, TAP, TRX, and V5.

45. The peptide of claim 43 or claim 44, wherein the sortase recognition sequence is selected from LPXTG (SEQ ID NO: 1), LPXTGG (SEQ ID NO: 2), LPXTGGG (SEQ ID NO: 3), and LPXTGGGG (SEQ ID NO: 4), wherein X is a natural or unnatural amino acid.

46. The peptide of claim 45, wherein the natural amino acid is selected from serine, threonine, asparagine, glutamine, cysteine, selenocysteine, glycine, proline, alanine, valine, isoleucine, leucine, methionine, phenylalanine, tyrosine, and tryptophan.

47. The peptide of claim 45, wherein the natural amino acid is selected from glutamic acid, aspartic acid, arginine, histidine, and lysine.

48. The peptide of any one of claims 45 to 47, wherein the unnatural amino acid is selected from hydroxyproline, beta-alanine, citrulline, ornithine, norleucine, 3-nitrotyrosine, nitroarginine, and pyroglutamic acid.

49. The peptide of claim 43 or claim 44, wherein the sortase recognition sequence is selected from LPETG (SEQ ID NO: 5), LPETGG (SEQ ID NO: 6), LPETGGG (SEQ ID NO: 7), and LPETGGGG (SEQ ID NO: 8).

50. The peptide of any one of claims 43 to 49, wherein the sugar residue is a residue of a sugar selected from fructose, glucose, and lactose.

51. The peptide of any one of claims 43 to 49, wherein R²⁰ is selected from ‒OR³¹, ‒NR³², ‒N3, and a structure:

.

52. The peptide of any one of claims 43 to 49, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

53. The peptide of any one of claims 43 to 49, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

54. The peptide of any one of claims 43 to 49, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

55. The peptide of any one of claims 43 to 49, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

56. The peptide of any one of claims 43 to 49, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

57. The peptide of any one of claims 43 to 49, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

58. The peptide of any one of claims 43 to 49, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

59. The peptide of any one of claims 43 to 49, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

60. The peptide of any one of claims 43 to 49, wherein the peptide has a structure represented by a formula:

, or a pharmaceutically acceptable salt thereof.

61. A cryoprotectant composition comprising an effective amount of the peptide of any one of claims 1 to 60 and one or more selected from: (a) a non-antifreeze protein; (b) a microbe; (c) a cell component; and (d) a cell.

62. The cryoprotectant composition of claim 61, wherein the non-antifreeze protein is selected from an enzyme, a hormone, an antibody, a growth factor, a vaccination protein, a therapeutic protein, or a nutrient protein.

63. A food product comprising the peptide of any one of claims 1 to 60.

64. The food product of claim 63, wherein the food product is selected from ice cream, yogurt, seafood, fruit, and a meat product.

65. An agricultural composition comprising the peptide of any one of claims 1 to 60.

66. A solid or semi-solid support comprising a surface covalently attached to a residue of the peptide of any one of claims 1 to 60.

67. The solid or semi-solid support of claim 66, wherein the residue of the peptide comprises an N-terminus, and wherein the N-terminus is covalently attached to the surface.

68. The solid or semi-solid support of claim 66 or claim 67, wherein the residue of the peptide has a structure represented by a formula:

wherein each occurrence of R¹ is independently a monosaccharide moiety or a disaccharide moiety; wherein each of R¹⁰ and R¹¹ is independently selected from ‒OH and ‒NHAc; wherein each occurrence of R² is independently selected from hydrogen and methyl; wherein R²⁰ is selected from ‒OR³¹, ‒NHR³², ‒N3, a protein tag, a sortase recognition sequence, a sugar residue, and a structure:

wherein R³¹ and R³² are selected from hydrogen, ‒CH2Ph, C1-C8 alkyl, C2-C8 alkyne, C1-C8 azide, tetrazinyl, cyclooctynyl, norbornenyl, and –(CH2CH2O)mCH3; wherein m is an integer selected from 1 to 100; wherein the ratio of x to y is of from about 2:3 to about 1:4; and wherein the sum of x and y is at least 30, or a pharmaceutically acceptable salt thereof.

69. The solid or semi-solid support of claim 68, wherein each occurrence of R¹ is independently a monosaccharide moiety or a disaccharide moiety having a structure represented by a formula:

wherein each occurrence of R¹⁰ and R¹¹ is independently selected from ‒OH and ‒NHAc.

70. The solid or semi-solid support of any one of claims 66 to 69, wherein the support is a glass bead, a silica-based resin, a cellulosic resin, an agarose bead, a polystyrene bead, or a polyacrylamide resin.

71. A cosmetic composition comprising the peptide of any one of claims 1 to 60.

72. A method of inhibiting ice crystal formation in a sample, the method comprising contacting the sample with an effective amount of the peptide of any one of claims 1 to 60.

73. The method of claim 72, wherein the sample is a biological material.

74. The method of claim 73, wherein the biological material is selected from a non- antifreeze protein, a microbe, a cell component, a cell, a tissue, and an organ.

75. The method of claim 74, wherein the cell is selected from a sperm cell, an egg matrix cell, an embryonic cell, and a stem cell.

76. The method of claim 72, wherein the sample is a food product.

77. The method of claim 72, wherein the sample is an agricultural product.

78. The method of claim 72, wherein the sample is a solid or semi-solid support.

79. The method of claim 72, wherein the sample is a cosmetic.

80. The method of claim 72, further comprising storing the biological material for a period of time.

81. The method of claim 80, wherein storing is at a temperature of about 25 ℃ or less.

82. The method of claim 80, wherein storing is at a temperature of about 4 ℃ or less.

83. A kit comprising the peptide of any one of claims 1 to 60 and one or more selected from: (a) a biological material; (b) a food product; (c) an agricultural product; (d) a solid or semi-solid support; and (e) a cosmetic.