Fusion proteins / peptides, methods and uses thereof

Abstract

Provided herein are fusion proteins / peptides and biopolymers comprising keratin and keratin associated peptide sequences. The fusion proteins and biopolymers may further comprise elastin-like, silk-like, collagen or collagen-like, resilin-like, abductin-like peptide, and / or linker-like sequences. The fusion proteins and biopolymers may exhibit the functional properties derived from each of the various peptide sequences incorporated therein, like elasticity, hydration, recovery, texture, or antimicrobial and UV protections. Additionally, provided herein are methods for obtaining and characterization of fusion proteins and biopolymers comprising keratin and keratin associated peptide sequences. The fusion proteins and biopolymers comprising keratin and keratin associated peptide sequences may be included in compositions for improving the properties of hair, skin, and nails.

Description

D E S C R I P T I O N FUSION PROTEINS / PEPTIDES, METHODS AND USES THEREOF TECHNICAL FIELD

[0001] The present disclosure relates fusion proteins / peptides with binding modules and biopolymers for hair and skin care, namely fusion proteins with keratin binding modules and biopolymers.

[0002] The present disclosure pertains to fusion proteins and peptides designed for use in hair and skin applications, including cosmetic and skin formulations. BACKGROUND

[0003] Fusion proteins or chimeric proteins are proteins created through the joining of two or more genes that originally code for separate proteins, peptides or modules. Translation of this fusion gene results in single or multiple polypeptides with functional properties derived from each of the original sequence. Some fusion proteins combine whole peptides and therefore contain all functional domains of the original proteins. However, other fusion proteins, especially those that occur naturally, combine only portions of coding sequences and therefore do not maintain the original functions of the parental genes that formed them. Novel recombinant technologies have made it possible to improve fusion proteins design for use in fields as diverse as biodetection, agriculture, paper and food industries, as well as biopharmaceuticals. GENERAL DESCRIPTION

[0004] Proteins, peptides, and peptide components, or blocks such as silk and collagen, have been used as ingredients in compositions for hair, skin, and nail care. In some cases, they are used to strengthen and moisturize hair, skin, and nails. In some cases, they are used to improve the appearance of hair, skin, and nails, and for protection against environmental and chemical damages. They may not, however, always provide the desired functions when used in hair, skin, and nail care products. For example, the isoelectric points of many natural proteins are lower than desired, therefore the affinity of the protein for the negatively charged hair, skin, and nails is not strong enough. Further, due to their high molecular weight and hydrophobicity, manyproteins have poor solubility. Structural proteins, such as silk and collagen, may be chemically degraded resulting in a diverse mixture of molecular weight components / blocks with variable properties. To enhance solubility for inclusion in products, these proteins are often modified chemically. However, the chemical modification of these proteins may affect their desired characteristics. Often, more than one protein may be needed to meet all the desired characteristics of a given composition, and this may lead to an increase in the cost and production time for the product. As a result, there remains an unmet need for designer proteins that overcome the inherent limitations of natural products. These designer proteins may provide better compositions for hair, skin, and nail products.

[0005] These facts are disclosed in order to illustrate the technical problem addressed by the present disclosure.

[0006] The present disclosure relates to a novel class of fusion proteins and peptides specifically designed for optimal performance in hair, nail and skin applications, encompassing cosmetic and dermatological formulations. The fusion peptide / proteins of the present disclosure exhibit remarkable efficacy in addressing various cosmetic and skin related problems. The present disclosure relates to these new fusion peptide / protein, synthesis and uses in hair, nail or skincare.

[0007] Additional aspects and advantages of the present disclosure will become readily apparent to those skilled in this art from the following description, wherein only illustrative embodiments of the present disclosure are shown and described. As will be realized, the present disclosure is capable of other and different embodiments, and its several details are capable of modifications in various obvious respects, all without departing from the disclosure.

[0008] The present disclosure relates to fusion proteins comprising a keratin peptide and biopolymers comprising a keratin peptide for hair and skin care.

[0009] The present disclosure relates to cosmetic and personal care compositions and, more specifically, to novel fusion proteins with binding modules designed for improved affinity, binding properties, strengthens of hair, nail and / or skin. In some embodiments, the fusion protein effect on strengthening hair is determined by a Young’s modulus. In some instances, the effect on strengthening hair is determined as a relative difference in the Young’s modulus of hair treated with and without a fusion protein / peptide or composition comprising the fusion protein / peptide according to the disclosure. In some instances, treating hair with the fusion protein / peptideimproves hair integrity. In some instances, hair integrity is determined by Differential Scanning Calorimetry (DSC).

[0010] In some aspects, disclosed herein is a fusion protein / peptide comprising: (a) a keratin or keratin associated peptide block; and (b) at least a polypeptide block selected from a list consisting of: (i) an elastin or elastin-like polypeptide (ELP) block, (ii) a silk or silk-like polypeptide (SLP) block, (iii) a collagen or collagen-like polypeptide (CLP) block, (iv) a resilin or resilin-like polypeptide (RLP) block, (v) an abductin or abductin-like polypeptide (ALP) block, (vi) a linker component as a spacer-like, or (vii) a combination of two or more selected from (i) to (vi).

[0011] In the present disclosure, a keratin or keratin associated peptide block may be selected or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity of the following list: SEQ ID NO.8, SEQ ID NO.9, SEQ ID NO.10, SEQ ID NO.48, SEQ ID NO.66, SEQ ID NO.67, SEQ ID NO.68, SEQ ID NO.69, SEQ ID NO.101, SEQ ID NO.102, SEQ ID NO.103, and SEQ ID NO.70-81.

[0012] In the present disclosure an elastin or elastin-like polypeptide (ELP) block may be selected or a sequence comprising at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity of the following list: SEQ ID NO.11-23, SEQ ID NO.49-55, SEQ ID NO.82-91, and SEQ ID NO.104.

[0013] In the present disclosure a silk or silk-like polypeptide (SLP) block may be selected or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity of the following list: SEQ ID NO.24-32, SEQ ID NO.56, SEQ ID NO.105, and SEQ ID NO.92.

[0014] In the present disclosure a collagen or collagen-like polypeptide (CLP) block may be selected or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity of the following list: SEQ ID NO.33, SEQ ID NO.57-59, SEQ ID NO.93-95, and SEQ ID NO.106.

[0015] In the present disclosure a resilin or resilin-like polypeptide (RLP) block may be selected or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity of the following list: SEQ ID NO.34-35, SEQ ID NO.60, SEQ ID NO.96, and SEQ ID NO.107.

[0016]

[0017] In the present disclosure an abductin or abductin-like polypeptide (ALP) block may be selected or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity of the following list: SEQ ID NO.36-42, SEQ ID NO.61, and SEQ ID NO.108.In the present disclosure a linker component as a spacer-like may be selected or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity of the following list: SEQ ID NO 97-100.

[0018] In some embodiments for better results, the polypeptide block may comprise an elastin or elastin like polypeptide (ELP) block.

[0019] In some embodiments for better results, the elastin or elastin like polypeptide block comprises 8 to 30 amino acids; preferably 10-30 amino acids, more preferably 15-30 amino acids.

[0020] In some embodiments for better results, the polypeptide block may comprise a linker block as a spacer-like.

[0021] In some embodiments for better results, the linker block comprises a hydrophilic block comprising 1 to 75 amino acids; preferably 10 to 50 amino acids. In some embodiments, the hydrophilic block comprises hydrophilic amino acids. In some embodiments, the hydrophilic amino acids comprise serine, threonine, glutamine, asparagine, glutamate, or aspartate.

[0022] In some embodiments for better results, the linker block adopts an alpha-helix conformation. In some embodiments, the linker block adopts a random coil conformation. In some embodiments, the secondary structure of the fusion peptide is determined using circular dichroism (CD) spectroscopy.

[0023] In some embodiments for better results, the linker block comprises 1 to 3 amino acids repeated 0 to 25 times, preferably 1 to 20 times.

[0024] In some embodiments for better results, the linker block comprises 1 to 210 to 25 times.

[0025] In some embodiments for better results, the keratin or keratin associated peptide block comprises SEQ ID NO: 8: GGVCGPSPPCITT, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO: 8.

[0026] In some embodiments for better results, the keratin or keratin associated peptide block comprises SEQ ID NO: 9: GGVCGPSPPC, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO: 9.

[0027] In some embodiments for better results, the keratin or keratin associated peptide block comprises SEQ ID NO: 10: CGPSPPCITT, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO: 10.

[0028] In some embodiments for better results, the keratin or keratin associated peptide block comprises SEQ ID NO: 68: CLPCLPAASC, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO: 68.

[0029] In some embodiments for better results, the keratin or keratin associated peptide block comprises SEQ ID NO: 73: CVSSCCKPQCC, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO: 73.

[0030] In some embodiments for better results, the keratin or keratin associated peptide block comprises SEQ ID NO: 74: PITCRRTCYH, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO: 74.

[0031] In some embodiments for better results, the keratin or keratin associated peptide block comprises SEQ ID NO: 75: DCKLPCNPCA, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO: 75.

[0032] In some embodiments for better results, the keratin or keratin associated peptide block comprises SEQ ID NO: 76: CLPCLPAASC, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO: 76.

[0033] In some embodiments for better results, the keratin or keratin associated peptide block comprises SEQ ID NO: 77: CEPAICEPSC, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO: 77.

[0034] In some embodiments for better results, the fusion protein / peptide comprises SEQ ID NO. 1: GGVCGPSPPCITTVPGVGVPGVGVPGLGVPGVGVPGVGR, or a sequence at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO: 1.

[0035] In some embodiments for better results, the fusion protein comprises SEQ ID NO. 2: GGVCGPSPPCITTVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG, or a sequence at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO: 2.

[0036] In some embodiments for better results, the fusion protein comprises SEQ ID NO. 7: GGVCGPSPPCITTVPGVGVPGVGVPGLGVPGVGVPGVG, or a sequence at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO: 7.

[0037] In some embodiments for better results, the polypeptide block comprises the silk or silk like polypeptide (SLP) block.

[0038] In some embodiments, the fusion protein comprises SEQ ID NO: 3: GGVCGPSPPCITTGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS, or a sequence at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO: 3.

[0039] In some embodiments, the polypeptide block comprises the collagen or collagen-like polypeptide (CLP) block.

[0040] In some embodiments, the fusion protein comprises SEQ ID NO: 5: GGVCGPSPPCITTGPTGPTGPAGPRGLQGLQGLQGERGEQGPT, or a sequence at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO: 5.

[0041] In some embodiments, the polypeptide block comprises the resilin or resilin-like polypeptide (RLP) block.

[0042] In some embodiments, the fusion protein comprises SEQ ID NO: 4: GGVCGPSPPCITTGGRPSDSYGAPGGGN, or a sequence at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO: 4.

[0043] In some embodiments, the polypeptide block comprises the abductin or abductin polypeptide (ALP) block.

[0044] In some embodiments, the fusion protein comprises SEQ ID NO. 6: GGVCGPSPPCITTGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS, or a sequence at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO: 6.

[0045] In certain embodiments, the fusion protein / peptide has the sequence: GGVCGPSPPCITTGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS (SEQ ID NO: 6).

[0046] In certain embodiments, the fusion protein / peptide has the sequence: GVGVPGVGVPGLGVPGVGVPGVG (SEQ ID NO: 22).

[0047] In certain embodiments, the fusion protein / peptide has the sequence: GAGAGSGAGAGSGAGAGSGAGAGSGAGAGS (SEQ ID NO: 32).

[0048] In certain embodiments, the fusion protein / peptide has the sequence: GPTGPTGPAGPRGLQGLQGLQGERGEQGPT (SEQ ID NO: 33).

[0049] In certain embodiments, the fusion protein / peptide has the sequence: GGVCGPSPPCITTGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ (SEQ ID NO: 44).

[0050] In certain embodiments, the fusion protein / peptide has the sequence: GGVCGPSPPCITTAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK (SEQ ID NO: 45).

[0051] In certain embodiments, the fusion protein / peptide has the sequence: GGVCGPSPPCITTLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK (SEQ ID NO: 46).

[0052] In certain embodiments, the fusion protein / peptide has the sequence: GGVCGPSPPCITTGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA (SEQ ID NO: 47).

[0053] In certain embodiment, the linker block comprises a spacer-like repetitive sequence block. The linker may comprise about 1 to about 3 amino acids repeated 0 to 25 times. The linker may comprise 1-2 amino acids repeated 10 to 25 times.

[0054] In certain embodiment, the present disclosure provides a fusion protein having at least 90% sequence identity any one of the following sequences: GGVCGPSPPCITTVPGVGVPGVGVPGLGVPGVGVPGVGR (SEQ ID NO: 1); GGVCGPSPPCITTVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG (SEQ ID NO: 2); GGVCGPSPPCITTGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS (SEQ ID NO: 3); GGVCGPSPPCITTGGRPSDSYGAPGGGN (SEQ ID NO: 4); GGVCGPSPPCITTGPTGPTGPAGPRGLQGLQGLQGERGEQGPT (SEQ ID NO: 5); GGVCGPSPPCITTGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS (SEQ ID NO: 6); or GGVCGPSPPCITTVPGVGVPGVGVPGLGVPGVGVPGVG (SEQ ID NO: 7); GGVCGPSPPCITTGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ (SEQ ID NO: 44); GGVCGPSPPCITTAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK (SEQ ID NO: 45); GGVCGPSPPCITTLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK (SEQ ID NO: 46); GGVCGPSPPCITTGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA (SEQ ID NO: 47).

[0055] The fusion protein according to embodiments of the disclosure, comprises a keratin or keratin associated peptide block having a length of from 6 to 16 amino acids, a silk or “SLP” having a repeat sequence with a length of 6 to 8 amino acids, and / or a silk or SLP having a length of 15 to 30 amino acids; a collagen or “CLP” having a repeat sequence with a length of 3 amino acids, and / or the collagen or CLP having a length of 15 to 30 amino acids; a elastin or “ELP” having a repeat sequence with a length of 5 amino acids, and / or the elastin or ELP having a length of 15 to 30 amino acids; a resilin or “RLP” having a repeat sequence with a length of 11 to 15 aminoacids, and / or the resilin or RLP having a length of 15 to 30 amino acids; and the abductin or “ALP” having a repeat sequence with a length of 4 to 10 amino acids, and / or the abductin or ALP has a length of 15 to 30 amino acids.

[0056] In some embodiments, the fusion protein has an average molecular weight of about 1 kDa to about 144 kDa. In some embodiments, the fusion protein has an average molecular weight of about 10 kDa to about 144 kDa. In some embodiments, the fusion protein has an average molecular weight of about 35 kDa to about 130 kDa.

[0057] In some embodiments, the fusion protein has an average molecular weight ranging from about 1 kDa to about 5 kDa, from about 5 kDa to about 10 kDa, from about 6 kDa to about 17 kDa, from about 10 kDa to about 15 kDa, from about 14 kDa to about 30 kDa, from between about 15 kDa to about 20 kDa, from about 17 kDa to about 39 kDa, from about 20 kDa to about 25 kDa, from about 25 kDa to about 30 kDa, from about 30 kDa to about 35 kDa, from about 35 kDa to about 40 kDa, from about 39 kDa to about 54 kDa, from about 39 kDa to about 80 kDa, from about 40 kDa to about 45 kDa, from about 45 kDa to about 50 kDa, from about 50 kDa to about 55 kDa, from about 55 kDa to about 60 kDa, from about 60 kDa to about 100 kDa, and from about 80 kDa to about 144 kDa.

[0058] In some embodiments, the fusion protein comprises a sequence having at least 80% sequence identity to any one of SEQ ID NOS: 1-7, 44-47, or 200-552.

[0059] In some embodiments, the fusion protein comprises a sequence having at least 90%, 95%, 96%, 97%, 98% or 99% sequence identity to any one of SEQ ID NOS: 1-7, 44-47, or 200-552.

[0060] In some embodiments, the fusion protein comprises a sequence identical to any one of SEQ ID NOS: 1-7, 44-47, or 200-552.

[0061] In some aspects, provided herein is a composition comprising the fusion protein according to embodiments of the disclosure for improving elasticity, recovery, hydration, integrity, hydrophobicity, texture, antibacterial, emulsifier properties, mechanical properties, thermal protection, or UV protection, or a combination of two or more thereof, of hair, nails or skin.

[0062] In some embodiments, the composition improves the elasticity, recovery, hydration, integrity, texture, antibacterial protections, or UV protection, or a combination of two or more thereof, of the skin.

[0063] In some embodiments, the composition improves the mechanical properties, color, texture, shape, hydration, integrity, recovery, hydrophobicity, or thermal protection, or a combination of two or more thereof, of the hair.

[0064] In some embodiments, the composition improves the mechanical properties, integrity, antimicrobial properties, or UV protection, or a combination of two or more thereof, of the nails.

[0065] In some embodiments, the composition further comprises urea, ammonium thioglycolate, thioanisole, benzyl alcohol, tris(hydroxymethyl)aminomethane, phosphate buffer, sodium chloride, citrate buffer, or ethanol, or a combination of two or more thereof.

[0066] In some aspects, provided herein is a use of a composition comprising the fusion protein according to embodiments of the disclosure as an enhancer agent of one or more properties of hair, nails or skin. In some embodiments, a use of a composition comprises using the fusion protein as an agent for enhancing elasticity, hydration, recovery, texture, antimicrobial and / or UV protections of hair, nails and skin.

[0067] In some aspects, provided herein is a fusion protein / peptide comprising: (a) at least one keratin or keratin associated peptide block; and (b) (i) an elastin or elastin-like peptide (ELP) block, (ii) a silk or silk-like peptide (SLP) block, (iii) a collagen or collagen-like peptide block (CLP), (iv) a resilin or resilin-like peptide block (RLP), (v) an abductin or abductin peptide (ALP) block, or (vi) a combination of two or more selected from (i) to (v).

[0068] In some embodiments, the fusion protein / peptide is represented by: [Bn1- Am- Bn- Co- Bn2]pFormula (I); or [Bn1 - Co - Bn - Am - Bn2]p Formula (II); or [Bn1 - Bn - Co - Am -Bn2]p Formula (III); or [Bn1 - Co - Am - Bn - Bn2]p Formula (IV) wherein,“A” comprises a peptide sequence comprising the at least one keratin or keratin associated peptide block, wherein “m” is an integer from 1 to 10; “B” comprises a peptide sequence comprising from 1 to 40 amino acids, wherein each “n”, n1”, and “n2” is independently an integer from 0 to 25; “C” comprises a peptide sequence having the structure Dq-Er-Fs-Gt-Hu; wherein “D” is the silk or silk-like polypeptide (SLP) block; wherein “E” comprises the collagen or collagen-like polypeptide (CLP) block; wherein “F” comprises the elastin or elastin-like polypeptide (ELP) block; wherein “G” comprises the resilin or resilin-like polypeptide (RLP) block; wherein “H” comprises the abductin or abductin-like polypeptide (ALP) block; wherein “q” is an integer from 0 to 100, “r” is an integer from 0 to 200, “s” is an integer from 0 to 220, “t” is an integer from 0 to 80, and “u” is an integer from 0 to 70; wherein “o” is an integer from 0 to 30; and “p” is an integer between 1 and 40; wherein at least one of “n”, n1”, and “n2” or “o” is not 0.

[0069] In some embodiments, each “n”, n1”, and “n2” is independently an integer from 0 to 25.

[0070] In some embodiments, “o” is an integer from 1 to 30.

[0071] In some embodiments, each “n”, n1”, and “n2” is an integer from 0 to 25 and “o” is an integer from 1 to 30.

[0072] In some embodiments, “p” is an integer from 3 to 37. In some embodiments, “p” is an integer from 8 to 15. In some embodiments, “p” is an integer from 10 to 12.

[0073] In some embodiments, “B” comprises a peptide sequence comprising from 1 to 40 amino acids. In some embodiments, “B” comprises a peptide sequence comprising more from 2 to 25 amino acids. In some embodiments, “B” comprises a peptide sequence comprising from 4 to 25 amino acids.

[0074] In some embodiments, “B” comprises a peptide sequence having XnZc and / or ZcXn; wherein “Xn” is proline, leucine, isoleucine, glutamic acid, aspartic acid, glutamine, lysine, alanine, arginine or threonine; and wherein “Zc” comprises glycine, alanine, lysine, proline, methionine, glutamine, arginine, threonine, valine, glutamic acid, aspartic acid, or asparagine.

[0075] In some embodiments, the at least one keratin or keratin associated peptide block has a length of from 6 to 16 amino acids, “D” comprises a polypeptide sequence comprising SEQ ID NO:24: GAGAGS, SEQ ID NO: 25: GAGSGA, SEQ ID NO: 26: GAGAGY, SEQ ID NO: 27: GAGYGA, SEQ ID NO: 28: GAGAGA, SEQ ID NO: 29: GAGAGV, SEQ ID NO: 30: GAGVGA, or SEQ ID NO: 31: GAGAGVGY, or a combination of two or more thereof; “E” comprises a polypeptide sequence GX1Z, wherein “X1” is proline, leucine, isoleucine, glutamic acid, aspartic acid, glutamine, lysine, alanine, arginine or threonine; and wherein Z is glycine, alanine, lysine, proline, methionine, glutamine, arginine, threonine, valine, glutamic acid, aspartic acid, or asparagine; “F” comprises a polypeptide sequence comprising SEQ ID NO: 21: VPGX2G and / or SEQ ID NO: 13: VPAVG, wherein “X2” is arginine, histidine, lysine, aspartic acid, glutamic acid, serine, threonine, asparagine, glutamine, cysteine, glycine, alanine, valine, isoleucine, leucine, methionine, phenylalanine, tyrosine, or tryptophan; “G” comprises a polypeptide sequence comprising SEQ ID NO: 34: GGRPSDSYGAPGGGN and / or SEQ ID NO: 35: GAPAQTPSSQY; “H” comprises a polypeptide sequence comprising SEQ ID NO: 36: GGFGGMGGGS, SEQ ID NO: 37: MGGG, SEQ ID NO: 38: FGGMG, SEQ ID NO: 39: FGGMGGG, SEQ ID NO: 40: GGFGGMGGG, or SEQ ID NO: 41: FGGMGGGNAG, or a combination of two or more thereof. In some embodiments, the keratin or keratin associated peptide block comprises SEQ ID NOs: 8, 9, 10, 66-81, 101-103, or a fragment thereof, or a combination of two or more thereof.

[0076] In some embodiments, “A” comprises a peptide sequence X3kCX35CX3k, wherein “X3” comprises glycine, alanine, valine, isoleucine, leucine, phenylalanine, proline, serine, threonine, asparagine, glutamine, cysteine, methionine, phenylalanine, tyrosine, tryptophan, aspartate, glutamate, histidine, lysine, or arginine, and “k” is an integer from 0 to 3.

[0077] In some embodiments, “A” comprises SEQ ID NO: 8: GGVCGPSPPCITT, SEQ ID NO: 9: GGVCGPSPPC, SEQ ID NO: 10: CGPSPPCITT, SEQ ID NO. 66: CGPSPPC, or SEQ ID NO. 67: GVCGPSPPC.

[0078] In some embodiments, the fusion protein / peptide has an average molecular weight from about 1 kDa to about 144 kDa. In some embodiments, the fusion protein / peptide has an average molecular weight from about 10 kDa to about 144 kDa In some embodiments, the fusion protein / peptide has an average molecular weight from about 35 kDa to about 130 kDa.

[0079] In some embodiments, the fusion protein / peptide has an average molecular weight from about 1 kDa to about 5 kDa, from about 5 kDa to about 10 kDa, from about 6 kDa to about 17 kDa, from about 10 kDa to about 15 kDa, from about 14 kDa to about 30 kDa, from between about 15 kDa to about 20 kDa, from about 17 kDa to about 39 kDa, from about 20 kDa to about25 kDa, from about 25 kDa to about 30 kDa, from about 30 kDa to about 35 kDa, from about 35 kDa to about 40 kDa, from about 39 kDa to about 54 kDa, from about 39 kDa to about 80 kDa, from about 40 kDa to about 45 kDa, from about 45 kDa to about 50 kDa, from about 50 kDa to about 55 kDa, from about 55 kDa to about 60 kDa, from about 60 kDa to about 100 kDa, and from about 80 kDa to about 144 kDa.

[0080] In some embodiments, the fusion protein has a secondary structure. In some embodiments, the secondary structure comprises an alpha (α) helix, 310helix, pi (π) helix , beta (β)-turn, β-sheet, coil, or a combination thereof.

[0081] In some embodiments, the silk or silk like peptide (SLP) block forms an alpha helix, 310helix, pi helix, beta (β)-turn, β-sheet, coil, or a combination thereof. In some embodiments, the silk or silk like peptide (SLP) block forms a β-sheet-rich structure.

[0082] In some embodiments, the elastin or elastin-like peptide (ELP) block forms an alpha helix, 310helix, pi helix, beta (β)-turn, β-sheet, coil, or a combination thereof. In some embodiments, the elastin or elastin-like peptide (ELP) block form a β-turn-rich structure.

[0083] In some embodiments, the linker block forms an alpha helix, 310helix, pi helix, beta (β)- turn, β-sheet, coil, or a combination thereof. In some embodiments, the linker block forms an alpha helix. In some embodiments, the linker block forms a coil. In some embodiments, the linker forms a coil.

[0084] In some embodiments, the elastin-like peptide (ELP) block is thermoresponsive. In some embodiments, the ELP block may be responsive to changes in pH. In some embodiments, the ELP block may be responsive over a range of temperatures. In some embodiments, the ELP block may be response to salts.

[0085] In some embodiments, provided herein is a use of the fusion protein, fusion protein / peptide or composition according to embodiments of the disclosure as a cosmetic, such as a cosmetic of hair, nails or skin.

[0086] In some embodiments, the cosmetic product is suitable for hair care or hair treatment.

[0087] In some aspects, provided herein is a method of obtaining the fusion protein of the present disclosure, comprising: inoculating a liquid medium with a microorganism containing a gene for the expression of the desired fusion protein; allowing the microorganism to multiply during a certain incubation period and inducing the expression under influence of a promoter;and retrieving the desired fusion protein from the obtained microorganisms by purifying the protein from endogenous contaminants.

[0088] In some embodiments, the microorganism Escherichia coli. In some embodiments, the microorganism is Komagataella phaffii.

[0089] In some embodiments, the fusion protein is purified from endogenous contaminants.

[0090] Another aspect relates to a composition comprising the fusion protein / peptide of the present disclosure for improving elasticity, recovery, hydration, integrity, hydrophobicity, texture, antibacterial, emulsifier properties, mechanical properties, thermal protection, or UV protection, or a combination of two or more thereof, of hair, nails or skin.

[0091] In some embodiments, the composition improves the elasticity, recovery, hydration, integrity, texture, antibacterial protections, or UV protection, or a combination of two or more thereof, of the skin.

[0092] In some embodiments, the amount of fusion protein / peptide ranges from 0.0001 % – 20 %(w / w); preferably the amount of fusion protein / peptide ranges from 0.001% – 5 % (w / w);.0.1% to about 1% w / w).

[0093] In some embodiments, the composition improves the mechanical properties, color, texture, shape, hydration, integrity, recovery, hydrophobicity, or thermal protection, or a combination of two or more thereof, of the hair.

[0094] In some embodiments, the composition improves the mechanical properties, integrity, antimicrobial properties, or UV protection, or a combination of two or more thereof, of the nails.

[0095] In some embodiments, the at least one excipient suitable for dermatological use is selected is from the following list: surfactant, emulsifier, preservative, thickener, organic polymer, humectant, silicone, oil, fragrance, vitamin, buffer, antimicrobial agent, antibacterial agent, disinfectant, chelating agent or mixtures thereof.

[0096] In some embodiments, the composition may comprise at least one excipient suitable for dermatological use.

[0097] In some embodiments, the at least one excipient suitable for dermatological use is selected is from the following list: ethanol, benzyl alcohol, diol molecule, urea, ammonium thioglycolate, thioanisole, tris(hydroxymethyl)aminomethane, phosphate buffer, sodium chloride, citrate buffer, or ethanol, or a combination of two or more thereof.

[0098] In some embodiments, the diol molecule is selected from: ethylene glycol, propylene diol, butylene glycol, butylene diol, or mixtures thereof.

[0099] In some embodiments, the composition may comprise: 0 -30 % (w / v) of ethanol, preferably 10-20%(w / v); 3 % (w / v) of benzyl alcohol; preferably 0.5-2%(w / v); 0-20% (w / v) of a diol molecule, preferably 10-15% (w / v).

[0100] In some embodiments, the composition may further comprise a propellant, a fragrance, an oil, or mixture thereof.

[0101] In some embodiments, the composition may be used in hair treatment.

[0102] The fusion protein / peptide or composition of the present disclosure may be used as a cosmetic, namely as a cosmetic of hair, nails or skin.

[0103] In some embodiments, the cosmetic product is suitable for hair care or hair treatment.

[0104] Another aspect relates to a shampoo, lotion, serum, cream, conditioner, foam, elixir, oil, aerosol or mask comprising a composition / fusion protein / peptide of the present disclosure.

[0105] Another aspect relates to a composition comprising the fusion protein of the present disclosure as an enhancer agent of one or more properties of hair, nails or skin, or as an agent for enhancing elasticity, hydration, recovery, texture, antimicrobial and / or UV protections of hair, nails and skin.

[0106] Another aspect relates to a method of obtaining the fusion protein / peptide of the present disclosure, comprising the steps of: inoculating a liquid medium with microorganism containing a gene for the expression of the desired fusion protein; allowing the microorganism to multiply during a certain incubation period and inducing the expression under influence of a promoter; and retrieving the desired fusion protein / peptide from the obtained microorganisms by purifying the protein from endogenous contaminants.

[0107] In an embodiment, the microorganism Escherichia coli.

[0108] In an embodiment, the fusion protein / peptide is purified from endogenous contaminants.

[0109] Another aspect relates to a method for obtaining the fusion protein / peptide of the present disclosure by solid-state synthesis comprising the steps of: initiating solid-state synthesis combining a keratin or keratin associated peptide block and at least a polypeptide block selected from a list consisting of: (i) an elastin or elastin-like polypeptide (ELP) block, (ii) a silk or silk-likepolypeptide (SLP) block, (iii) a collagen or collagen-like polypeptide (CLP) block, (iv) a resilin or resilin-like polypeptide (RLP) block, (v) an abductin or abductin-like polypeptide (ALP) block, or (vi) a combination of two or more blocks selected from (i) to (v); executing solid-phase reactions to obtain a stable peptide. BRIEF DESCRIPTION OF THE DRAWINGS

[0110] The following figures provide embodiments for illustrating the disclosure and should not be seen as limiting the scope of disclosure.

[0111] Figure 1 shows a linear vector map of an expression vector comprising a promoter, the target fusion protein sequence, linker sequence, a C-terminal affinity tag sequence, and AmpR gene and corresponding promoter according to embodiments of the disclosure.

[0112] Figure 2 shows a linear vector map of an expression vector comprising a promoter, a N- terminal affinity tag sequence, a linker sequence, the target fusion protein, and AmpR gene and corresponding promoter according to embodiments of the disclosure.

[0113] Figure 3 shows the penetration / location of peptides labeled with FITC (fluorescence probe) and applied in hair fiber by the observation in fluorescence microscopy. Most of the peptides were able to penetrate the cuticle until the cortex, especially peptides SEQ ID NO: 2, SEQ ID NO: 45, SEQ ID NO: 46 and SEQ ID NO:47. DETAILED DESCRIPTION

[0114] The present disclosure relates to fusion proteins / peptides.

[0115] An aspect of the present disclosure relates to fusion proteins / peptides comprising an effective amount of a repeat sequence of various proteins that can be used for improving properties of the hair, skin, and nails.

[0116] Another aspect of the present disclosure relates to a composition comprising the fusion proteins / peptides of the present disclosure.

[0117] In some embodiments, the fusion proteins / peptides may be used in a hair care composition, a skin care composition, a nail care composition, a cosmetic composition, or a pharmaceutical composition.

[0118] In some embodiments, the fusion protein / peptide and compositions comprise an effective amount of a repeat sequence of various proteins / peptides is advantageous in that the fusion protein / peptide may provide compositions with desired characteristic(s). The desired characteristics may include elasticity and stimuli-responsive behavior.

[0119] Keratin and keratin associated proteins are the main constituents of human hair, skin, and nails. Keratin and keratin associated proteins typically have a high sulfur content due to the presence of cysteine amino acids. The presence of sulfur is essential to the structure of hair, skin, and nails, as it allows for the formation of disulfide bonds between peptide chains. The presence of disulfide bonds (i.e., bridges) is largely responsible for the structure and texture of the hair, skin, and nails. Damage to the disulfide bridges (i.e., bonds) between keratin may alter the appearance and texture of the hair, skin, and nails. Maintaining the integrity of disulfide bonds between keratins may help to keep hair, skin, and nails healthy and prevent cracking or breakage. Fusion Proteins

[0120] In some embodiments, the fusion protein is a keratin fusion protein comprising a keratin or keratin associated peptide block derived from keratin protein fractions. The keratin and keratin associated fusion proteins described herein may bind with hair, skin, and nails with high affinity and repair keratinous fiber damage through the formation of new disulfide bonds. The keratin or keratin associated peptide block of the fusion proteins may have a sequence containing one or more cysteine amino acids which naturally form disulfide bonds with other free cysteine amino acids in the hair, skin, and nails. The formation of new disulfide bonds may help to restore the mechanical properties of the hair, skin, and nails, including elasticity, resistance, and appearance.

[0121] In some embodiments, the fusion proteins disclosed herein comprise amino acid sequences (the term “peptides” may be used interchangeably to refer to the amino acid sequences) that may be joined by a covalent bond or any other type of bond that leads to a structure which maintains the properties of the fusion proteins of the present disclosure. The bond may be selected from, but is not limited to, hydrogen bonds, ion pairing, hydrophobic association, or inclusion complex formation.

[0122] In some embodiments, the keratin or keratin associated fusion proteins / peptides comprise at least one keratin or keratin associated peptide block.

[0123] In some embodiments, a keratin, keratin peptide, or keratin associated peptide includes a wild-type keratin peptide, a functional fragment of a wild-type keratin peptide, or a peptide having at least 90% identity to a wild-type keratin peptide or a functional fragment of a wild-type keratin peptide. The wild-type keratin peptide may be keratin 85 having SEQ ID NO: 48. The wild- type peptide keratin peptide may comprise SEQ ID NO: 8, 9, 10, 66, or 67. In some embodiments, the keratin, keratin peptide, or keratin associated peptide forms one or more disulfide bonds with hair. In some embodiments, the keratin, keratin peptide, or keratin associated peptide forms one or more disulfide bonds with skin. In some embodiments, the keratin, keratin peptide, or keratin associated peptide forms one or more disulfide bonds with nails.

[0124] In a non-limiting example embodiment, a functional fragment of a wild-type keratin peptide comprises at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 contiguous amino acids of a wild- type keratin peptide. In a non-limiting example embodiment, a functional fragment of a wild- type keratin peptide comprises at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids having at least 90% identity to a wild-type keratin peptide. In a non-limiting example embodiment, a functional fragment of a wild-type keratin peptide comprises at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids, where the at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids comprise one or more cysteine amino acids. For instance, one or more cysteine amino acids is 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26 or 27 cysteine amino acids. In a non-limiting example embodiment, a functional fragment of a wild-type keratin peptide comprises at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids, where at least 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20%, 30%, 40%, or 50% of the at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids are cysteine amino acids. A non-limiting example embodiment of a keratin or keratin peptide is provided in SEQ ID NO: 48.

[0125] In some embodiments, a keratin associated peptide (sometimes referred to as a keratin associated protein) includes a peptide that forms a disulfide bond with wild-type keratin. In some embodiments, a keratin associated peptide comprises at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids, and the at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids are at least 90% identical to a wild-type keratin peptide sequence. The wild-type keratin peptide may be keratin 85 having SEQ ID NO: 48. The wild-type peptide keratin peptide may comprise SEQ ID NO: 8, 9, 10, 66, or 67.

[0126] In some embodiments, the number of amino acids in the keratin or keratin associated peptide component of the fusion protein is about 6 residues to about 16 residues.

[0127] In some embodiments, the number of amino acids in the keratin or keratin associated peptide component of the fusion protein is about 6 residues.

[0128] In some embodiments, the number of amino acids in the keratin or keratin associated peptide component of the fusion protein is about 7 residues.

[0129] In some embodiments, the number of amino acids in the keratin or keratin associated peptide component of the fusion protein is about 8 residues.

[0130] In some embodiments, the number of amino acids in the keratin or keratin associated peptide component of the fusion protein is about 9 residues.

[0131] In some embodiments, the number of amino acids in the keratin or keratin associated peptide component of the fusion protein is about 10 residues.

[0132] In some embodiments, the number of amino acids in the keratin or keratin associated peptide component of the fusion protein is about 11 residues.

[0133] In some embodiments, the number of amino acids in the keratin or keratin associated peptide component of the fusion protein is about 12 residues.

[0134] In some embodiments, the number of amino acids in the keratin or keratin associated peptide component of the fusion protein is about 13 residues.

[0135] In some embodiments, the number of amino acids in the keratin or keratin associated peptide component of the fusion protein is about 14 residues.

[0136] In some embodiments, the number of amino acids in the keratin or keratin associated peptide component of the fusion protein is about 15 residues.

[0137] In some embodiments, the number of amino acids in the keratin or keratin associated peptide component of the fusion protein is about 16 residues.

[0138] In some embodiments, the keratin or keratin associated peptide block of the fusion protein possess a high cysteine content in order to enrich certain properties of the keratin or keratin associated peptide block, such as, for example, to enhance formation of intermolecular cross-linking. The total cysteine content ranges from 10% to 50% of the total number of amino acids in the keratin or keratin associated peptide block.

[0139] In some embodiments, the total cysteine content of the keratin or keratin associated peptide is greater than 15% of the total number of amino acids in the keratin or keratin associated peptide block of the fusion protein / peptide.

[0140] In some embodiments, the keratin or keratin associated peptide block of the fusion protein / peptide comprises 2 cysteine residues.

[0141] In some embodiments, the keratin or keratin associated peptide block of the fusion protein comprises 3 cysteine residues.

[0142] In some embodiments, the keratin or keratin associated peptide block of the fusion protein comprises 4 cysteine residues.

[0143] In some embodiments, the keratin or keratin associated peptide block of the fusion protein comprises 5 cysteine residues.

[0144] In some embodiments, the keratin or keratin associated peptide block of the fusion protein / peptide comprises the peptide sequence (X3)kC(X3)5C(X3)k.

[0145] In some embodiments, each “X3” is independently glycine, alanine, valine, isoleucine, leucine, phenylalanine, proline, serine, threonine, asparagine, glutamine, cysteine, methionine, phenylalanine, tyrosine, tryptophan, aspartate, glutamate, histidine, lysine, or arginine.

[0146] In some embodiments, each “k” is independently an integer ranging from 0 to 3. If k is 2, then (X3)khas a first X3and a second X3, where each X3is independently glycine, alanine, valine, isoleucine, leucine, phenylalanine, proline, serine, threonine, asparagine, glutamine, cysteine, methionine, phenylalanine, tyrosine, tryptophan, aspartate, glutamate, histidine, lysine, or arginine. If k is 3, then (X3)k has a first X3, a second X3, and a third X3, where each X3is independently glycine, alanine, valine, isoleucine, leucine, phenylalanine, proline, serine, threonine, asparagine, glutamine, cysteine, methionine, phenylalanine, tyrosine, tryptophan, aspartate, glutamate, histidine, lysine, or arginine. (X3)5 has a first X3, a second X3, a third X3, a fourth X3, and a fifth X3, where each X3is independently glycine, alanine, valine, isoleucine, leucine, phenylalanine, proline, serine, threonine, asparagine, glutamine, cysteine, methionine, phenylalanine, tyrosine, tryptophan, aspartate, glutamate, histidine, lysine, or arginine.

[0147] In some embodiments, the keratin or keratin associated peptide component of the fusion protein comprises: GGVCGPSPPCITT (SEQ ID NO: 8), GGVCGPSPPC (SEQ ID NO: 9), CGPSPPCITT(SEQ ID NO: 10), CGPSPPC (SEQ ID NO: 66), GVCGPSPPC (SEQ ID NO: 67), or a sequence of SEQ ID NOS: 70-81, or a combination or two or more thereof.

[0148] In some embodiments, the keratin or keratin associated peptide sequence is GGVCGPSPPCITT (SEQ ID NO: 8). In some embodiments, the keratin or keratin associated peptide sequence is GGVCGPSPPC (SEQ ID NO: 9). In some embodiments, the keratin or keratin associated peptide sequence is CGPSPPCITT (SEQ ID NO: 10).

[0149] In some embodiments, the keratin or keratin associated fusion proteins further comprise a elastin or an elastin-like polypeptide (ELP) block, a silk or silk-like polypeptide (SLP) block, a collagen or collagen or collagen-like polypeptide (CLP) block, a resilin or resilin-like polypeptide (RLP) block, an abductin or abductin-like polypeptide block (ALP), or combinations or two or more thereof, such as, for example, a silk-elastin-like polypeptide (SELP) block.

[0150] In some embodiments, the keratin or keratin associated fusion proteins disclosed herein further comprise an elastin or elastin-like polypeptide (ELP) block. In some embodiments, elastin- like polypeptide (ELP) refers to a peptide, including a synthetic peptide, comprising an amino acid sequence having a similar secondary structure, tertiary structure, or amino acid sequence, or a combination of two or more thereof, to a wild-type elastin protein (e.g., SEQ ID NO: 55), or a fragment of a wild-type elastin protein. In some embodiments, a fragment includes a sequence having at least 4, 5, 6, 7, 8, 9, or 10 amino acids 100% identical to a sequence of wild-type elastin protein. Non-limiting example elastin and ELPs include SEQ ID NOS: 11-23, 49-55 and 82-91.

[0151] ELPs may comprise polymeric or oligomeric repeating peptide sequences of an elastin protein. In an example embodiment, an elastin or ELP comprises SEQ ID NO: 49 ((VPGXG)n, where n is 1 to 10 and each X is independently any amino acid), or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 49. In some embodiments, each X is independently valine or leucine. In some embodiments, n is 5. In some embodiments, n is 6.

[0152] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 50 (VPGVG), or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 50. The elastin or ELP may comprise 1 to 10 sequences having SEQ ID NO: 50, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 50. The 1 to 10 sequences may be connected, e.g., VPGVGVPGVGVPGVGVPGVGVPGVGVPGVG (SEQ ID NO: 23), or may be separated by one or more amino acids, e.g., by another ELP as in VPGVGVPGVGVPGLGVPGVGVPGVG (SEQ ID NO: 54).

[0153] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 51 (VPGLG), or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 51. The elastin or ELP may comprise 1 to 10 sequences having SEQ ID NO: 51, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 51. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids.

[0154] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 52 (VPGVGVPGL), or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 52. The elastin or ELP may comprise 1 to 10 sequences having SEQ ID NO: 52, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 52. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids.

[0155] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 53 (VPGVGVPGVGVPGLGVPGVGVPGVGR) or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 53. The elastin or ELP may comprise 1 to 10 sequences having SEQ ID NO: 53, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 53. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids.

[0156] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 23 (VPGVGVPGVGVPGVGVPGVGVPGVGVPGVG), or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 23. The elastin or ELP may comprise 1 to 10 sequences having SEQ ID NO: 23, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 23. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids.

[0157] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 54 (VPGVGVPGVGVPGLGVPGVGVPGVG), or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 54. The elastin or ELP may comprise 1 to 10 sequences having SEQ ID NO: 54, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 54. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids.

[0158] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 22 (GVGVPGVGVPGLGVPGVGVPGVG), or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 22. The elastin or ELP may comprise 1 to 10 sequences having SEQ IDNO: 22, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 22. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids.

[0159] In some embodiments, an elastin or ELP comprises a polymeric or oligomeric repeating peptide sequence of an elastin peptide. In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 4 amino acid residues.

[0160] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 5 amino acid residues. As a non-limiting example, SEQ ID NOS: 49, 50 or 51.

[0161] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 6 amino acid residues.

[0162] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 7 amino acid residues.

[0163] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 8 amino acid residues.

[0164] Non-limiting example repeating peptide sequences include polytetra-, polypenta-, polyhexa-, polyhepta-, polyocta-, and polynonapeptides, including but not limited to, VPGG (SEQ ID NO: 11), IPGG (SEQ ID NO: 12) VPAVG (SEQ ID NO: 13), AVGVP (SEQ ID NO: 14), IPGVG (SEQ ID NO: 15), LPGVG (SEQ ID NO: 16), VAPGVG (SEQ ID NO: 17), GVGVPGVG (SEQ ID NO: 18), VPGFGVGAG (SEQ ID NO: 19), VPGVGVPGG (SEQ ID NO: 20), VPGX2G (SEQ ID NO: 21), SEQ ID NO: 49 ((VPGXG)n, where n is 1 to 10 and each X is independently any amino acid), SEQ ID NO: 50 (VPGVG), SEQ ID NO: 51 (VPGLG), and SEQ ID NO: 52 (VPGVGVPGL), and combinations of two or more thereof.

[0165] In some embodiments, “X2” is a naturally occurring or a non-naturally occurring amino acid.

[0166] In some embodiments, elastin or ELPs are polymeric or oligomeric repeats of the pentapeptide VPAVG (SEQ ID NO: 13).

[0167] In some embodiments, elastin or ELPs are polymeric or oligomeric repeats of the pentapeptide VPGX2G, wherein “X2” is an amino acid selected from the group consisting of arginine, histidine, lysine, aspartic acid, glutamic acid, serine, threonine, asparagine, glutamine, cysteine, glycine, alanine, valine, isoleucine, leucine, methionine, phenylalanine, tyrosine, ortryptophan. In some embodiments, “X2” may be leucine. In some embodiments, “X2” is asparagine.

[0168] In some embodiments, “X2” is valine.

[0169] In some embodiments, the elastin or ELP is defined by the peptide sequence GVGVPGVGVPGLGVPGVGVPGVG (SEQ ID NO: 22).

[0170] In another embodiment, the elastin or ELP is defined by the sequence VPGVGVPGVGVPGVGVPGVGVPGVGVPGVG (SEQ ID NO: 23).

[0171] In some embodiments, the elastin or elastin-like polypeptide (ELP) component forms β- sheet-rich domains.

[0172] In some embodiments, the elastin or ELP component comprises amorphous domains. In some embodiments, the elastin or ELP component comprises crystalline domains. In some embodiments, the elastin or ELP component comprises both crystalline and amorphous domains.

[0173] In some embodiments, the elastin or ELP component are stimuli-responsive. In some embodiments, the ELP component is thermoresponsive. In some embodiments, the ELP component may be responsive to changes in pH. In some embodiments, the ELP component may be responsive over a range of temperatures. In some embodiments, the ELP component may be response to salts.

[0174] In some embodiments, the keratin or keratin associated fusion proteins / peptides disclosed herein comprise a silk or silk-like polypeptide (SLP) component. In some embodiments, silk-like polypeptide (SLP) refers to a peptide, including a synthetic peptide, having a similar secondary structure, tertiary structure, or amino acid sequence, or a combination of two or more thereof, to a wild-type silk protein (e.g., SEQ ID NO: 56), or a fragment of a wild-type silk protein. In some embodiments, a fragment includes a sequence having at least 4, 5, 6, 7, 8, 9, or 10 amino acids 100% identical to a sequence of wild-type silk protein. The wild-type silk protein may be fibroin. Non-limiting example silk and SLPs include SEQ ID NOS: 24-32, 56, and 92.

[0175] SLPs may comprise polymeric or oligomeric repeating peptide sequences of a silk protein. In an example embodiment, a silk or SLP comprises SEQ ID NO: 24 GAGAGS, or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 24. In an example embodiment, a silk or SLP comprises SEQ ID NO: 24, or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 24. The silk or SLP may comprise 1 to 10 sequenceshaving SEQ ID NO: 24, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 24. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids.

[0176] In some embodiments, a silk or SLP comprises a polymeric or oligomeric repeating peptide sequence of a silk peptide, where each polymeric or oligomeric repeating peptide sequence comprises or has 6 amino acid residues.

[0177] In some embodiments, a silk or SLP comprises a polymeric or oligomeric repeating peptide sequence of a silk peptide, where each polymeric or oligomeric repeating peptide sequence comprises or has 7 amino acid residues.

[0178] In some embodiments, a silk or SLP comprises a polymeric or oligomeric repeating peptide sequence of a silk peptide, where each polymeric or oligomeric repeating peptide sequence comprises or has 8 amino acid residues.

[0179] Non-limiting example repeating peptide sequences include polytetra-, polypenta-, polyhexa-, polyhepta-, polyocta-, and polynonapeptides, including but not limited to, GAGAGS (SEQ ID NO: 24), GAGSGA (SEQ ID NO: 25), GAGAGY (SEQ ID NO: 26), GAGYGA (SEQ ID NO: 27), GAGAGA (SEQ ID NO: 28), GAGAGV (SEQ ID NO: 29), GAGVGA (SEQ ID NO: 30), and GAGAGVGY (SEQ ID NO: 31), and combinations of two or more thereof.

[0180] In some embodiments, the silk or SLPs are polymeric or oligomeric repeats of the pentapeptide GAGAGS (SEQ ID NO: 24).

[0181] In some embodiments, the silk or SLP is peptide sequence GAGAGSGAGAGSGAGAGSGAGAGSGAGAGS (SEQ ID NO: 32).

[0182] In some embodiments, the silk or SLP is peptide sequence GAGX1GX2(SEQ ID NO: 92), wherein X1and X2are independently any amino acid, optionally wherein X1is A, S, Y, or V, optionally wherein X2is S, A, Y, or V.

[0183] In some embodiments, the silk or SLP is peptide sequence GYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGAGV GYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGS (SEQ ID NO: 56).

[0184] In some embodiments, the silk or silk-like (SLP) block forms β-sheet-rich domains.

[0185] In some embodiments, the silk or SLP component block crystalline domains. In some embodiments, the silk or SLP block comprises amorphous domains. In some embodiments, the SLP block comprises both crystalline and amorphous domains.

[0186] In some embodiments, the keratin or keratin associated fusion proteins disclosed herein comprise a collagen or collagen-like polypeptide (CLP) block. In some embodiments, a collagen- like polypeptide (CLP) refers to a peptide, including a synthetic peptide, having a similar secondary structure, tertiary structure, or amino acid sequence, or a combination of two or more thereof, to a wild-type collagen protein (e.g., SEQ ID NO: 59), or a fragment of a wild-type collagen protein. In some embodiments, a fragment includes a sequence having at least 3, 4, 5, 6, 7, 8, 9, or 10 amino acids 100% identical to a sequence of wild-type collagen protein. Non-limiting example collagen and CLPs include SEQ ID NOS: 33, 57-59, 93-95, and 106 as well as fragments having amino acids “GTP” and / or “GLQ”.

[0187] CLPs may comprise polymeric or oligomeric repeating peptide sequences of a collagen peptide. In an example embodiment, a collagen or CLP comprises the sequence GTP. The collagen or CLP may comprise 1 to 10 sequences comprising the sequence GTP. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids. The 1 to 10 sequences may be, for example, 2 or 3. For example, the collagen or CLP may comprise GPTGPT (SEQ ID NO: 57), GLQGLQ (SEQ ID NO: 58), GPAGPA (SEQ ID NO: 95), or GPTGPTGPAGPRGLQGLQGLQGERGEQGPT (SEQ ID NO: 33). In an example embodiment, collagen or CLP comprises the sequence GLQ. The collagen or CLP may comprise 1 to 10 sequences comprising the sequence GLQ. The 1 to 10 sequences may be, for example, 2 or 3. The 1 to 10 sequences may be connected or may be separated by one or more amino acids. For example, collagen or CLP may comprise GLQGLQ (SEQ ID NO: 58) or GPTGPTGPAGPRGLQGLQGLQGERGEQGPT (SEQ ID NO: 33). In an example embodiment, collagen or CLP comprises the sequence GPT. The collagen or CLP may comprise 1 to 10 sequences comprising the sequence GPT. The 1 to 10 sequences may be, for example, 2 or 3. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids. For example, collagen or CLP may comprise GPTGPT (SEQ ID NO: 57) or GPTGPTGPAGPRGLQGLQGLQGERGEQGPT (SEQ ID NO: 33). The collagen or CLP may comprise 1 to 10 sequences comprising the sequence GXP, wherein X is any amino acid. The 1 to 10 sequences may be, for example, 2 or 3. The 1 to 10 sequences may be connected or may be separated by one or more amino acids. For example, the collagen or CLP may comprise GXPGXP(SEQ ID NO: 93). The collagen or CLP may comprise 1 to 10 sequences comprising the sequence GZP, wherein Z is 4-hydroxyproline. The 1 to 10 sequences may be, for example, 2 or 3. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids. For example, the collagen or CLP may comprise GLQGLQ (SEQ ID NO: 94).

[0188] In some embodiments, each polymeric or oligomeric repeating peptide sequences of the collagen or collagen-like polypeptide (CLP) block comprise or have 3 amino acid residues. As non- limiting examples, the 3 amino acid residues may include GTP, GLQ, GXP (X is any amino acid), GZP (Z is 4-hydroxyproline), and GX1H.

[0189] In some embodiments, the repeating peptide sequence includes polytetra-, polypenta-, polyhexa-, polyhepta-, polyocta-, and polynonapeptides, including but not limited to, GX1H.

[0190] In some embodiments, “X1” comprises proline, leucine, isoleucine, glutamic acid, aspartic acid, glutamine, lysine, alanine, arginine and threonine; and wherein “H” comprises an amino acid selected from the group consisting of glycine, alanine, lysine, proline, methionine, glutamine, arginine, threonine, valine, glutamic acid, aspartic acid, or asparagine.

[0191] In some embodiments, the collagen or CLP is defined by the peptide sequence GPTGPTGPAGPRGLQGLQGLQGERGEQGPT (SEQ ID NO: 33).

[0192] In some embodiments, the collagen or CLP is defined by the peptide sequence SEQ ID NO: 59.

[0193] In some embodiments, the collagen or CLP forms alpha-helices (α-helices). In some embodiments, multiple collagen or CLPs form a triple helix. In some embodiments, the collagen or CLP forms a 3.613 helix. In some embodiments, the collagen or CLP forms a polyproline-type II helix. In some embodiments, the collagen or CLP forms at least one helix loop.

[0194] In some embodiments, the keratin or keratin associated fusion proteins disclosed herein comprise a resilin or resilin-like polypeptide (RLP) block. In some embodiments, resilin-like polypeptide (RLP) refers to a peptide, including a synthetic peptide having a similar secondary structure, tertiary structure, or amino acid sequence, or a combination of two or more thereof, to a wild-type resilin protein (e.g., SEQ ID NO: 60), or a fragment of a wild-type resilin protein. In some embodiments, a fragment includes a sequence having at least 4, 5, 6, 7, 8, 9, or 10 amino acids 100% identical to a sequence of wild-type silk protein. Non-limiting example resilin and RLPs include SEQ ID NOS: 34-35, 60, 96, and 107.

[0195] RLPs may comprise polymeric or oligomeric repeating peptide sequences of a resilin peptide. In example embodiments, the polymeric or oligomeric repeating peptide sequence is a fragment of a wild-type resilin peptide having about 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 amino acids.

[0196] In some embodiments, each polymeric or oligomeric repeating peptide sequences of the resilin or resilin-like polypeptide (RLP) block comprise or have 11 amino acid residues. In some embodiments, each polymeric or oligomeric repeating peptide sequences of the resilin or resilin- like polypeptide (RLP) block comprise or have 12 amino acid residues. In some embodiments, each polymeric or oligomeric repeating peptide sequences of the resilin or resilin-like polypeptide (RLP) block comprise or have 13 amino acid residues. In some embodiments, each polymeric or oligomeric repeating peptide sequences of the resilin or resilin-like polypeptide (RLP) block comprise or have 14 amino acid residues. In some embodiments, each polymeric or oligomeric repeating peptide sequences of the resilin or resilin-like polypeptide (RLP) block comprise or have 15 amino acid residues. In some embodiments, the repeating peptide sequence includes polypenta-, polyhexa-, polyhepta-, polyocta-, and polynonapeptides, including but not limited to, GGRPSDSYGAPGGGN (SEQ ID NO: 34), GAPAQTPSSQY (SEQ ID No: 35), AQTPSSQYGAP (SEQ ID NO: 96), and combinations thereof. In some embodiments, the resilin or RLP is defined by the peptide sequence GGRPSDSYGAPGGGN (SEQ ID NO: 34). In some embodiments, the resilin or RLP is defined by the peptide sequence SEQ ID NO: 60. In some embodiments, the resilin or RLP is defined by the peptide sequence SEQ ID NO: 107. In some embodiments, the resilin or RLP is defined by the peptide sequence GAPAQTPSSQY (SEQ ID NO: 35). In some embodiments, the resilin or RLP is defined by the peptide sequence AQTPSSQYGAP (SEQ ID NO: 96).

[0197] In some embodiments, the keratin or keratin associated fusion proteins disclosed herein comprise an abductin or abductin-like polypeptide (ALP) block. In some embodiments, abductin- like polypeptide (ALP) refers to a peptide, including a synthetic peptide, comprising an amino acid sequence having a similar secondary structure, tertiary structure, or amino acid sequence, or a combination of two or more thereof, to a wild-type abductin protein (e.g., SEQ ID NO: 61), or a fragment of a wild-type abductin protein. In some embodiments, a fragment includes a sequence having at least 4, 5, 6, 7, 8, 9, or 10 amino acids 100% identical to a sequence of wild-type abductin protein. Non-limiting example abductin and ALPs include SEQ ID NOS: 36-42 and 61. ALPs may comprise polymeric or oligomeric repeating peptide sequences of an abductin protein.

[0198] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 4 amino acid residues of an abductin protein. In some embodiments, each polymeric or oligomeric repeating peptide sequence has or comprises 5 amino acid residues of an abductin protein. In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 6 amino acid residues of an abductin protein.

[0199] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 7 amino acid residues of an abductin protein. In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 8 amino acid residues of an abductin protein. In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 9 amino acid residues of an abductin protein. In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 10 amino acid residues of an abductin protein. In some embodiments, the repeating peptide sequences are various polytetra-, polypenta-, polyhexa-, polyhepta-, polyocta, and polynonapeptides, including but not limited to, GGFGGMGGGS (SEQ ID NO: 36), MGGG (SEQ ID NO: 37), FGGMG (SEQ ID NO: 38), FGGMGGG (SEQ ID NO: 39), GGFGGMGGG (SEQ ID NO: 40), FGGMGGGNAG (SEQ ID NO: 41), and combinations thereof. In some embodiments, the abductin or ALP is defined by the peptide sequence GGFGGMGGGSGGFGGMGGGSGGFGGMGGGS (SEQ ID NO: 42). In some embodiments, the abductin or ALP is defined by the peptide sequence MNAYICLAACLIAAVSAAGYGGGAGSMGGTGGMGGGMNAGGFGGMGGMGGGKGGFGGIGGFGGGM GGGPGGFGGMGGFGGMAAKGGFGGMGSGMGGFGGMGGGNAGFGGMGGGNAGFGGMGGQGGFG GKGY (SEQ ID NO: 61).

[0200] In example embodiments, abductin or ALP comprises SEQ ID NO: 36, or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 36. The abductin or ALP may comprise 1 to 10 sequences having SEQ ID NO: 36, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 36. The 1 to 10 sequences may be connected, e.g., SEQ ID NO: 42, or may be separated by one or more amino acids.

[0201] In some embodiments, the fusion protein comprises a linker component. In some embodiments, the linker component is a spacer-like. In some embodiments, the linker component is interspaced between a keratin or keratin associated peptide and a polypeptide component. In some embodiments, the linker component is interspaced between each of the polypeptide components. In some embodiments, the linker or spacer-like comprises (GQ)n,wherein n is an integer between 1 and 20. In some embodiments, the linker or spacer-like comprises (AK)n, wherein n is an integer between 1 and 20. In some embodiments, the linker or spacer-like (LK)n, wherein n is an integer between 1 and 20. In some embodiments, the linker or spacer-like comprises (GA)n, wherein n is an integer between 1 and 20. In some embodiments, the linker or spacer-like comprises the sequence GQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ (SEQ ID NO: 97), AKAKAKAKAKAKAKAKAKAKAKAKAKAKAK (SEQ ID NO: 98), LKLKLKLKLKLKLKLKLKLKLKLKLKLKLK (SEQ ID NO: 99), GAGAGAGAGAGAGAGAGAGAGAGAGAGAGA (SEQ ID NO: 100), or a combination thereof. In some embodiments, the linker or spacer-like comprises a fragment of GQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ (SEQ ID NO: 97), AKAKAKAKAKAKAKAKAKAKAKAKAKAKAK (SEQ ID NO: 98), LKLKLKLKLKLKLKLKLKLKLKLKLKLKLK (SEQ ID NO: 99), GAGAGAGAGAGAGAGAGAGAGAGAGAGAGA (SEQ ID NO: 100), or a combination thereof. In some embodiments, the linker or spacer-like comprises (GQ)n, where n is 1-20. In some embodiments, the linker or spacer-like comprises (AK)n, where n is 1-20. In some embodiments, the linker or spacer-like comprises (LK)n, where n is 1-20. In some embodiments, the linker or spacer-like comprises (GA)n, where n is 1-20.

[0202] Table 1. Non-Limiting Example Peptide Sequences SEQ Sequences ID NO: Keratin / Keratin-like peptides (KLPs) 8 GGVCGPSPPCITT 9 GGVCGPSPPC 10 CGPSPPCITT 48 MSCRSYRISSGCGVTRNFSSCSAVAPKTGNRCCISAAPYRGVSCYRGLTGFGSRSLCNLGSCGPRIA VGGFRAGSCGRSFGYRSGGVCGPSPPCITTVSVNESLLTPLNLEIDPNAQCVKQEEKEQIKSLNSRF AAFIDKVRFLEQQNKLLETKWQFYQNQRCCESNLEPLFSGYIETLRREAECVEANSGRLASELNHV QEVLEGYKKKYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLRRLYEEEIRVLQ AHISDTSVIVKMDNSRDLNMDCIIAEIKAQYDDVASRSRAEAESWYRSKCEEMKATVIRHGETLRR TKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALSDARCKLAELEGALQKAKQDM ACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHRLCEGVGSVNVCVSSSRGGVSCGGLSYSTTPGRQ ITSGPSAIGGSITVVAPDSCAPCQPRSSSFSCGSSRSVRFA 66 CGPSPPC 67 GVCGPSPPC 68 CLPCLPAASC 69 CLPAASC 101 VSSCCKPQCC 102 CCKPQCC103 CCQSSCCKPS 70 YGGSSGGG 71 FGGGS 72 CCQSSCCKPSC 73 CVSSCCKPQCC 74 PITCRRTCYH 75 DCKLPCNPCA 76 CLPCLPAASC 77 CEPAICEPSC 78 CQCSCCKPYCS 79 FCGFPSCSTSC 80 CTPPSCCQLHHA 81 SCCAPVYCCK Elastin / Elastin-like peptides (ELPs) 11 VPGG 12 IPGG 13 VPAVG 14 AVGVP 15 IPGVG 16 LPGVG 17 VAPGVG 18 GVGVPGVG 19 VPGFGVGAG 20 VPGVGVPGG 21 VPGX2G 22 GVGVPGVGVPGLGVPGVGVPGVG 23 VPGVGVPGVGVPGVGVPGVGVPGVGVPGVG 49 (VPGXG)n, where n is 1 to 10 and each X is independently any amino acid 50 VPGVG 51 VPGLG 52 VPGVGVPGL 53 VPGVGVPGVGVPGLGVPGVGVPGVGR 54 VPGVGVPGVGVPGLGVPGVGVPGVG 55 LLNLAGLVPGVGVAPGVGVAPGVGVAPGVGLAPGVGVAPGVGVAPGVGVAPGIGPGGVAAAA KSAAKVAAKAQLRAAAGLGAGIPGLGVGVGVPGLGVGAGVPGLGVGAGVPGFGAVPGALAAAK AAKYGAAVPGVLGGLGALGGVGIPGGVVGAGPAAAAAAAKAAAKAAQFGLVGAAGLGGLGVG GLGVPGVGGLGGIPPAAAAKAAKYGAAGLGGVLGGAGQFPLGGVAARPGFGLSPIFPGGACLGK ACGRKRK 82 IPGLG 83 GYGVP 84 GGGVP 85 IPGVGIPGLG 86 IPGVGVPGLG 87 VPGVGVPGLG 88 VPGVGIPGVG 89 VPGVGIPGLG 90 GYGVPGGGVP91 IPGVGAVGVP 104 MAGLTAAAPRPGVLLLLLSILHPSRPGGVPGAIPGGVPGGVFYPGAGLGALGGGALGPGGKPLKP VPGGLAGAGLGAGLGAFPAVTFPGALVPGGVADAAAAYKAAKAGAGLGGVPGVGGLGVSAGA VVPQPGAGVKPGKVPGVGLPGVYPGGVLPGARFPGVGVLPGVPTGAGVKPKAPGVGGAFAGIP GVGPFGGPQPGVPLGYPIKAPKLPGGYGLPYTTGKLPYGYGPGGVAGAAGKAGYPTGTGVGPQA AAAAAAKAAAKFGAGAAGVLPGVGGAGVPGVPGAIPGIGGIAGVGTPAAAAAAAAAAKAAKYG AAAGLVPGGPGFGPGVVGVPGAGVPGVGVPGAGIPVVPGAGIPGAAVPGVVSPEAAAKAAAKA AKYGARPGVGVGGIPTYGVGAGGFPGFGVGVGGIPGVAGVPGVGGVPGVGGVPGVGISPEAQA AAAAKAAKYGAAGAGVLGGLVPGAPGAVPGVPGTGGVPGVGTPAAAAAKAAAKAAQFGLVPG VGVAPGVGVAPGVGVAPGVGLAPGVGVAPGVGVAPGVGVAPGIGPGGVAAAAKSAAKVAAKA QLRAAAGLGAGIPGLGVGVGVPGLGVGAGVPGLGVGAGVPGFGAGADEGVRRSLSPELREGDPS SSQHLPSTPSSPRVPGALAAAKAAKYGAAVPGVLGGLGALGGVGIPGGVVGAGPAAAAAAAKAA AKAAQFGLVGAAGLGGLGVGGLGVPGVGGLGGIPPAAAAKAAKYGAAGLGGVLGGAGQFPLGG VAARPGFGLSPIFPGGACLGKACGRKRK Silk / Silk-like peptides (SLPs) 24 GAGAGS 25 GAGSGA 26 GAGAGY 27 GAGYGA 28 GAGAGA 29 GAGAGV 30 GAGVGA 31 GAGAGVGY 32 GAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 56 GYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAG SGAGAGYGAGAGVGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGS 105 MRVKTFVILCCALQYVAYTNANINDFDEDYFGSDVTVQSSNTTDEIIRDASGAVIEEQITTKKMQRK NKNHGILGKNEKMIKTFVITTDSDGNESIVEEDVLMKTLSDGTVAQSYVAADAGAYSQSGPYVSNS GYSTHQGYTSDFSTSAAVGAGAGAGAAAGSGAGAGAGYGAASGAGAGAGAGAGAGYGTGAG AGAGAGYGAGAGAGAGAGYGAGAGAGAGAGYGAGAGAGAGAGYGAGAGAGAGAGYGAGA GAGAGAGYGAASGAGAGAGYGQGVGSGAASGAGAGAGAGSAAGSGAGAGAGTGAGAGYGA GAGAGAGAGYGAASGTGAGYGAGAGAGYGGASGAGAGAGAGAGAGAGAGYGTGAGYGAGA GAGAGAGAGAGYGAGAGAGYGAGYGVGAGAGYGAGYGAGAGSGAASGAGSGAGAGSGAGA GSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGTGAGSGAGAGYGAGAGAGYGA GAGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGAGAGYGAGAGAGY GAGAGVGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS GAGAGSGAGAGSGAGVGYGAGVGAGYGAGYGAGAGAGYGAGAGSGAASGAGAGAGAGAGT GSSGFGPYVANGGYSRSDGYEYAWSSDFGTGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS GAGAGYGAGVGVGYGAGYGAGAGAGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGS GAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGVGSGAGAGSGAGAGVGYGAGA GVGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGA GSGAGAGSGAGVGYGAGVGAGYGAGYGAGAGAGYGAGAGSGAASGAGAGSGAGAGSGAGA GSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGA GAGYGAGYGAGAGAGYGAGAGSGAASGAGSGAGAGSGAGAGAGSGAGAGSGAGAGSGAGA GSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGYGAGAGAGYGAGAGSGAASGAGAGSGAGA GSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGVGYGAGYGAGAGAGYGAGAGSGAAS GAGAGAGAGAGTGSSGFGPYVAHGGYSGYEYAWSSESDFGTGSGAGAGSGAGAGSGAGAGSG AGAGSGAGYGAGVGAGYGAGYGAGAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGYGAGAGAGYGAGAGSGAGSGAGAG SGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGYGAGAG AGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGVGSGAGAGSGAGAGSGAGAGSGAGAG YGAGYGAGAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSG AGAGSGAGVGYGAGVGAGYGAGYGAGAGAGYGAGAGSGAASGAGAGAGAGAGTGSSGFGPY VANGGYSGYEYAWSSESDFGTGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGYGAGA GAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGS GSGAGAGSGAGAGSGAGAGYGAGVGAGYGVGYGAGAGAGYGAGAGSGAASGAGAGAGAGA GTGSSGFGPYVAHGGYSGYEYAWSSESDFGTGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAG SGAGAGSGAGAGYGAGVGAGYGAAYGAGAGAGYGAGAGSGAASGAGAGSGAGAGSGAGAG SGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGAGAGYGAG AGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGSGSGAGAGSGAGAGSGAGAG YGAGVGAGYGAGYGAGAGAGYGAGAGSGAGSGAGAGSGAGAGYGAGAGAGYGAGYGAGAG AGYGAGAGTGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGSGSGAGAG SGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGAGAGYGAGYGAGAGAGYGAGAGSGAG SGAGAGSGAGAGSGAGAGSGAGAGYGAGYGAGAGSGAASGAGAGAGAGAGTGSSGFGPYVA HGGYSGYEYAWSSESDFGTGSGAGAGSGAGAGAGAGAGSGAGAGYGAGVGAGYGAGYGAGA GAGYGAGAGSGTGSGAGAGSGAGAGYGAGVGAGYGAGAGSGAAFGAGAGAGAGSGAGAGS GAGAGSGAGAGSGAGAGSGAGAGYGAGYGAGVGAGYGAGAGSGAASGAGAGSGAGAGSGA GAGSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGYGAGAGAGYGAGAGSGAASGAGAGSGA GAGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGAGSGAGAGYGAGAGSGAASGAGA GAGAGAGTGSSGFGPYVANGGYSGYEYAWSSESDFGTGSGAGAGSGAGAGSGAGAGSGAGAG SGAGAGYGAGVGAGYGAGYGAGAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAG SGAGAGSGAGAGSGAGAGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSG AGAGSGAGAGYGAGVGAGYGVGYGAGAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSG AGAGSGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGAGYGVGYGAGAGAGYGAGAG SGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGAGYG VGYGAGAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAG AGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGYG AGVGAGYGVGYGAGVGAGYGAGAGSGAASGAGAGSGAGAGAGSGAGAGSGAGAGSGAGAG SGAGAGSGAGAGSGAGAGYGAGYGAGVGAGYGAGAGVGYGAGAGAGYGAGAGSGAASGAG AGAGSGAGAGTGAGAGSGAGAGYGAGAGSGAASGAGAGAGAGAGTGSSGFGPYVANGGYSG YEYAWSSESDFGTGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGAGSGA GSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGAGSGTGSGAGAGSGAGAGSGAGAGS GAGAGSGAGAGSGAGAGSGVGAGYGVGYGAGAGAGYGVGYGAGAGAGYGAGAGSGTGSGA GAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGAGYGVGYGAGAGAGY GAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGS GAGAGSGAGAGYGVGYGAGAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGSGAGA GSGAGAGSGAGAGSGAGAGYGAGVGAGYGVGYGAGAGAGYGAGAGSGAGSGAGAGSGAGA GSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGY GAGVGAGYGVGYGAGAGAGYGAGAGSGAASGAGAGAGAGAGTGSSGFGPYVANGGYSGYEY AWSSESDFGTGSGAGAGSGAGAGSGAGAGYGAGYGAGVGAGYGAGAGVGYGAGAGAGYGA GAGSGAASGAGAGAGAGAGSGAGAGSGAGAGAGSGAGAGYGAGYGIGVGAGYGAGAGVGY GAGAGAGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGY GAGYGAGVGAGYGAGAGVGYGAGAGAGYGAGAGSGAASGAGAGAGAGAGAGSGAGAGSGA GAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGYGG AGAGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGAGSGAA SGAGAGAGAGAGTGSSGFGPYVNGGYSGYEYAWSSESDFGTGSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGYGAGAGAGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGSGAG AGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGYGAGAGAGYGAGAGSG AASGAGAGSGAGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAG AGYGAGYGAGVGAGYGAGAGVGYGAGAGAGYGAGAGSGAASGAGAGSGSGAGSGAGAGSG AGAGSGAGAGAGSGAGAGSGAGAGSGAGAGYGAGYGAGAGSGAASGAGAGAGAGAGTGSS GFGPYVANGGYSGYEYAWSSESDFGTGSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGYGAG AGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAG AGYGAGYGAGAGAGYGAGAGVGYGAGAGAGYGAGAGSGAGSGAGAGSGSGAGAGSGSGAG SGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGYGIGVGAGYGAGAGV GYGAGAGAGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGA GSGAGAGSGAGAGSGAGAGYGAGAGVGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGA GSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGAGYGAGYGAGVGAGYGAGAGYGAGYGV GAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGYGAGA GAGYGAGAGAGYGAGAGSGAASGAGAGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGAGY GAGAGSGAASGAGAGSGAGAGAGAGAGAGSGAGAGSGAGAGYGAGAGSGAASGAGAGAGA GTGSSGFGPYVANGGYSRREGYEYAWSSKSDFETGSGAASGAGAGAGSGAGAGSGAGAGSGAG AGSGAGAGGSVSYGAGRGYGQGAGSAASSVSSASSRSYDYSRRNVRKNCGIPRRQLVVKFRALPC VNC 92 GAGX1GX2, wherein X1and X2are independently any amino acid, optionally wherein X1is A, S, Y, or V, optionally wherein X2is S, A, Y, or V Collagen / Collagen-like peptides (CLPs) 33 GPTGPTGPAGPRGLQGLQGLQGERGEQGPT 57 GPTGPT 58 GLQGLQ 59 MFSFVDLRLLLLLAATALLTHGQEEGQVEGQDEDIPPITCVQNGLRYHDRDVWKPEPCRICVCDN GKVLCDDVICDETKNCPGAEVPEGECCPVCPDGSESPTDQETTGVEGPKGDTGPRGPRGPAGPP GRDGIPGQPGLPGPPGPPGPPGPPGLGGNFAPQLSYGYDEKSTGGISVPGPMGPSGPRGLPGPP GAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARG LPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGAP GPAGARGNDGATGAAGPPGPTGPAGPPGFPGAVGAKGEAGPQGPRGSEGPQGVRGEPGPPGP AGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQGPGGPPGPKGNSGEPGAP GSKGDTGAKGEPGPVGVQGPPGPAGEEGKRGARGEPGPTGLPGPPGERGGPGSRGFPGADGV AGPKGPAGERGSPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGR PGPPGPPGARGQAGVMGFPGPKGAAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGPPGPA GPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPGEQGVPGDLGAPGPSGARGERGFPGERGV QGPPGPAGPRGANGAPGNDGAKGDAGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGD AGPKGADGSPGKDGVRGLTGPIGPPGPAGAPGDKGESGPSGPAGPTGARGAPGDRGEPGPPGP AGFAGPPGADGQPGAKGEPGDAGAKGDAGPPGPAGPAGPPGPIGNVGAPGAKGARGSAGPP GATGFPGAAGRVGPPGPSGNAGPPGPPGPAGKEGGKGPRGETGPAGRPGEVGPPGPPGPAGE KGSPGADGPAGAPGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGP PGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVG PAGKSGDRGET 93 GXPGXP (each X is independently any amino acid) 94 GZPGZP (each Z is 4-hydroxyproline) 95 GPAGPA 106 MLGTLTPLSSLLLLLLVLVLGCGPRASSGGGAGGAAGYAPVKYIQPMQKGPVGPPFREGKGQYLE MPLPLLPMDLKGEPGPPGKPGPRGPPGPPGFPGKPGMGKPGLHGQPGPAGPPGFSRMGKAGP PGLPGKVGPPGQPGLRGEPGIRGDQGLRGPPGPPGLPGPSGITIPGKPGAQGVPGPPGFQGEPGPQGEPGPPGDRGLKGDNGVGQPGLPGAPGQGGAPGPPGLPGPAGLGKPGLDGLPGAPGDKGE SGPPGVPGPRGEPGAVGPKGPPGVDGVGVPGAAGLPGPQGPSGAKGEPGTRGPPGLIGPTGYG MPGLPGPKGDRGPAGVPGLLGDRGEPGEDGEPGEQGPQGLGGPPGLPGSAGLPGRRGPPGPK GEAGPGGPPGVPGIRGDQGPSGLAGKPGVPGERGLPGAHGPPGPTGPKGEPGFTGRPGGPGVA GALGQKGDLGLPGQPGLRGPSGIPGLQGPAGPIGPQGLPGLKGEPGLPGPPGEGRAGEPGTAGP TGPPGVPGSPGITGPPGPPGPPGPPGAPGAFDETGIAGLHLPNGGVEGAVLGKGGKPQFGLGELS AHATPAFTAVLTSPFPASGMPVKFDRTLYNGHSGYNPATGIFTCPVGGVYYFAYHVHVKGTNVW VALYKNNVPATYTYDEYKKGYLDQASGGAVLQLRPNDQVWVQMPSDQANGLYSTEYIHSSFSGF LLCPT Resilin / Resilin-like peptides (RLP) 34 GGRPSDSYGAPGGGN 35 GAPAQTPSSQY 60 MFKLLGLTLLMAMVVLGRPEPPVNSYLPPSDSYGAPGQSGPGGRPSDSYGAPGGGNGGRPSDSY GAPGQGQGQGQGQGGYAGKPSDTYGAPGGGNGNGGRPSSSYGAPGGGNGGRPSDTYGAPG GGNGGRPSDTYGAPGGGGNGNGGRPSSSYGAPGQGQGNGNGGRSSSSYGAPGGGNGGRPSD TYGAPGGGNGGRPSDTYGAPGGGNNGGRPSSSYGAPGGGNGGRPSDTYGAPGGGNGNGSGG RPSSSYGAPGQGQGGFGGRPSDSYGAPGQNQKPSDSYGAPGSGNGNGGRPSSSYGAPGSGPG GRPSDSYGPPASGSGAGGAGGSGPGGADYDNDEPAKYEFNYQVEDAPSGLSFGHSEMRDGDFT TGQYNVLLPDGRKQIVEYEADQQGYRPQIRYEGDANDGSGPSGPGGPGGQNLGADGYSSGRPG NGNGNGNGGYSGGRPGGQDLGPSGYSGGRPGGQDLGAGGYSNGKPGGQDLGPGGYSGGRP GGQDLGRDGYSGGRPGGQDLGASGYSNGRPGGNGNGGSDGGRVIIGGRVIGGQDGGDQGYS GGRPGGQDLGRDGYSSGRPGGRPGGNGQDSQDGQGYSSGRPGQGGRNGFGPGGQNGDNDG SGYRY 96 AQTPSSQYGAP 107 MFKLLGLTLLMAMVVLGRPEPPVNSYLPPSDSYGAPGQSGPGGRPSDSYGAPGGGNGGRPSDSY GAPGQGQGQGQGQGGYAGKPSDTYGAPGGGNGNGGRPSSSYGAPGGGNGGRPSDTYGAPG GGNGGRPSDTYGAPGGGGNGNGGRPSSSYGAPGQGQGNGNGGRSSSSYGAPGGGNGGRPSD TYGAPGGGNGGRPSDTYGAPGGGNNGGRPSSSYGAPGGGNGGRPSDTYGAPGGGNGNGSGG RPSSSYGAPGQGQGGFGGRPSDSYGAPGQNQKPSDSYGAPGSGNGNGGRPSSSYGAPGSGPG GRPSDSYGPPASGSGAGGAGGSGPGGADYDNDEPAKYEFNYQVEDAPSGLSFGHSEMRDGDFT TGQYNVLLPDGRKQIVEYEADQQGYRPQIRYEGDANDGSGPSGPGGPGGQNLGADGYSSGRPG NGNGNGNGGYSGGRPGGQDLGPSGYSGGRPGGQDLGAGGYSNGKPGGQDLGPGGYSGGRP GGQDLGRDGYSGGRPGGQDLGASGYSNGRPGGNGNGGSDGGRVIIGGRVIGGQDGGDQGYS GGRPGGQDLGRDGYSSGRPGGRPGGNGQDSQDGQGYSSGRPGQGGRNGFGPGGQNGDNDG SGYRY Abductin / Abductin-like peptides (ALP) 36 GGFGGMGGGS 37 MGGG 38 FGGMG 39 FGGMGGG 40 GGFGGMGGG 41 FGGMGGGNAG 42 GGFGGMGGGSGGFGGMGGGSGGFGGMGGGS 61 MNAYICLAACLIAAVSAAGYGGGAGSMGGTGGMGGGMNAGGFGGMGGMGGGKGGFGGIG GFGGGMGGGPGGFGGMGGFGGMAAKGGFGGMGSGMGGFGGMGGGNAGFGGMGGGNA GFGGMGGQGGFGGKGY 108 GGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNG GRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGQGQGQGQGQGQGQGQGQGQGGVCGPSPPCIT TGQGQGQGQGQGQGQGQGQGQVPAVGVPAVGVPAVGVPAVGVPAVGVPAVGVPAVGVPA VGVPAVGVPAVGGQGQGQGQGQGQGQGQGQGQGGVCGPSPPCITTGQGQGQGQGQGQG QGQGQGQGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYG APGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGA PGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGN Linker / Spacer-like peptides 97 GQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 98 AKAKAKAKAKAKAKAKAKAKAKAKAKAKAK 99 LKLKLKLKLKLKLKLKLKLKLKLKLKLKLK 100 GAGAGAGAGAGAGAGAGAGAGAGAGAGAGA (GQ)n, where n is 1-20 (AK)n, where n is 1-20 (LK)n, where n is 1-20 (GA)n, where n is 1-20

[0203] Table 1 provides example embodiments of elastin, elastin-like polypeptide (ELP), silk, silk- like polypeptide (SLP), collagen, collagen-like polypeptide (CLP), resilin, resilin-like polypeptide (RLP), abductin, and abductin polypeptide (ALP) peptides.

[0204] Table 2. Non-Limiting Example Peptide Fusion Sequences SEQ ID Sequences NO: Elastin / ELP and Keratin Fusion Proteins 1 GGVCGPSPPCITTVPGVGVPGVGVPGLGVPGVGVPGVGR 2 GGVCGPSPPCITTVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG 7 GGVCGPSPPCITTVPGVGVPGVGVPGLGVPGVGVPGVG 200 GGVCGPSPPCVPGVGVPGVGVPGLGVPGVGVPGVGR 201 GGVCGPSPPCVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG 202 GGVCGPSPPCVPGVGVPGVGVPGLGVPGVGVPGVG 203 CGPSPPCITTVPGVGVPGVGVPGLGVPGVGVPGVGR 204 CGPSPPCITTVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG 205 CGPSPPCITTVPGVGVPGVGVPGLGVPGVGVPGVG 206 YGGSSGGGVPGVGVPGVGVPGLGVPGVGVPGVGR 207 YGGSSGGGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG 208 YGGSSGGGVPGVGVPGVGVPGLGVPGVGVPGVG 209 FGGGSVPGVGVPGVGVPGLGVPGVGVPGVGR 210 FGGGSVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG 211 FGGGSVPGVGVPGVGVPGLGVPGVGVPGVG 212 CCQSSCCKPSCVPGVGVPGVGVPGLGVPGVGVPGVGR 213 CCQSSCCKPSCVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG 214 CCQSSCCKPSCVPGVGVPGVGVPGLGVPGVGVPGVG 215 CVSSCCKPQCCVPGVGVPGVGVPGLGVPGVGVPGVGR 216 CVSSCCKPQCCVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG 217 CVSSCCKPQCCVPGVGVPGVGVPGLGVPGVGVPGVG 218 PITCRRTCYHVPGVGVPGVGVPGLGVPGVGVPGVGRPITCRRTCYHVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG PITCRRTCYHVPGVGVPGVGVPGLGVPGVGVPGVG DCKLPCNPCAVPGVGVPGVGVPGLGVPGVGVPGVGR DCKLPCNPCAVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG DCKLPCNPCAVPGVGVPGVGVPGLGVPGVGVPGVG CLPCLPAASCVPGVGVPGVGVPGLGVPGVGVPGVGR CLPCLPAASCVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG CLPCLPAASCVPGVGVPGVGVPGLGVPGVGVPGVG CEPAICEPSCVPGVGVPGVGVPGLGVPGVGVPGVGR CEPAICEPSCVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG CEPAICEPSCVPGVGVPGVGVPGLGVPGVGVPGVG CQCSCCKPYCSVPGVGVPGVGVPGLGVPGVGVPGVGR CQCSCCKPYCSVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG CQCSCCKPYCSVPGVGVPGVGVPGLGVPGVGVPGVG FCGFPSCSTSCVPGVGVPGVGVPGLGVPGVGVPGVGR FCGFPSCSTSCVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG FCGFPSCSTSCVPGVGVPGVGVPGLGVPGVGVPGVG CTPPSCCQLHHAVPGVGVPGVGVPGLGVPGVGVPGVGR CTPPSCCQLHHAVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG CTPPSCCQLHHAVPGVGVPGVGVPGLGVPGVGVPGVG SCCAPVYCCKVPGVGVPGVGVPGLGVPGVGVPGVGR SCCAPVYCCKVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG SCCAPVYCCKVPGVGVPGVGVPGLGVPGVGVPGVG GGVCGPSPPCITT(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP, GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereof GGVCGPSPPC(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP, GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereof CGPSPPCITT(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP, GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereof YGGSSGGG(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP, GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereof FGGGS(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP,GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereof CCQSSCCKPSC(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP, GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereof CVSSCCKPQCC(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP, GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereof PITCRRTCYH(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP, GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereof DCKLPCNPCA(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP, GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereof CLPCLPAASC(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP, GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereof CEPAICEPSC(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP, GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereof CQCSCCKPYCS(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP, GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereof FCGFPSCSTSC(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP, GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereof CTPPSCCQLHHA(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP, GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereofSCCAPVYCCK(X), wherein X comprises VPGG, IPGG, VPAVG, AVGVP, IPGVG, LPGVG, VAPGVG, GVGVPGVG, VPGFGVGAG, VPGVGVPGG, GVGVPGVGVPGLGVPGVGVPGVG, VPGVG, VPGLG, VPGVGVPGL, IPGLG, GYGVP, GGGVP, IPGVGIPGLG, IPGVGVPGLG, VPGVGVPGLG, VPGVGIPGVG, VPGVGIPGLG, GYGVPGGGVP, or IPGVGAVGVP, or a combination of two or more thereof GGVCGPSPPCITT(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is about 5 GGVCGPSPPC(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is about 5 CGPSPPCITT(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is about 5 YGGSSGGG(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is about 5 FGGGS(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is about 5 CCQSSCCKPSC(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is about 5 CVSSCCKPQCC(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is about 5 PITCRRTCYH(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is about 5 DCKLPCNPCA(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is about 5 CLPCLPAASC(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is about 5 CEPAICEPSC(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is about 5 CQCSCCKPYCS(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is about 5 FCGFPSCSTSC(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is about 5 CTPPSCCQLHHA(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is about 5SCCAPVYCCK(VPGXG)n, where n is 1 to 10 and each X is independently any amino acid, optionally, wherein each X is independently V or L, and further optionally n is 271 about 5 Silk / SLP and Keratin Fusion Proteins 3 GGVCGPSPPCITTGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 272 GGVCGPSPPCGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 273 CGPSPPCITTGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 274 YGGSSGGGGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 275 FGGGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 276 CCQSSCCKPSCGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 277 CVSSCCKPQCCGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 278 PITCRRTCYHGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 279 DCKLPCNPCAGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 280 CLPCLPAASCGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 281 CEPAICEPSCGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 282 CQCSCCKPYCSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 283 FCGFPSCSTSCGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 284 CTPPSCCQLHHAGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS 285 SCCAPVYCCKGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS GGVCGPSPPCITTGAGX1GX2, wherein X1 and X2 are independently any amino acid, 286 optionally wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or V GGVCGPSPPCGAGX1GX2, wherein X1 and X2 are independently any amino acid, 287 optionally wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or V CGPSPPCITTGAGX1GX2, wherein X1 and X2 are independently any amino acid, 288 optionally wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or V YGGSSGGGGAGX1GX2, wherein X1 and X2 are independently any amino acid, 289 optionally wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or V FGGGSGAGX1GX2, wherein X1 and X2 are independently any amino acid, optionally 290 wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or V CCQSSCCKPSCGAGX1GX2, wherein X1 and X2 are independently any amino acid, 291 optionally wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or V CVSSCCKPQCCGAGX1GX2, wherein X1 and X2 are independently any amino acid, 292 optionally wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or V PITCRRTCYHGAGX1GX2, wherein X1 and X2 are independently any amino acid, 293 optionally wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or V DCKLPCNPCAGAGX1GX2, wherein X1 and X2 are independently any amino acid, 294 optionally wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or V CLPCLPAASCGAGX1GX2, wherein X1 and X2 are independently any amino acid, 295 optionally wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or V CEPAICEPSCGAGX1GX2, wherein X1 and X2 are independently any amino acid, 296 optionally wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or V CQCSCCKPYCSGAGX1GX2, wherein X1 and X2 are independently any amino acid, 297 optionally wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or V FCGFPSCSTSCGAGX1GX2, wherein X1 and X2 are independently any amino acid, 298 optionally wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or V CTPPSCCQLHHAGAGX1GX2, wherein X1 and X2 are independently any amino acid, 299 optionally wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or VSCCAPVYCCKGAGX1GX2, wherein X1 and X2 are independently any amino acid, 300 optionally wherein X1 is A, S, Y, or V, optionally wherein X2 is S, A, Y, or V GGVCGPSPPCITT(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more 301 thereof GGVCGPSPPC(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more 302 thereof CGPSPPCITT(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more 303 thereof YGGSSGGG(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more 304 thereof FGGGS(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, 305 GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more thereof CCQSSCCKPSC(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more 306 thereof CVSSCCKPQCC(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more 307 thereof PITCRRTCYH(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more 308 thereof DCKLPCNPCA(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more 309 thereof CLPCLPAASC(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more 310 thereof CEPAICEPSC(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more 311 thereof CQCSCCKPYCS(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more 312 thereof FCGFPSCSTSC(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more 313 thereof CTPPSCCQLHHA(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more 314 thereof SCCAPVYCCK(X), wherein X comprises GAGAGS, GAGSGA, GAGAGY, GAGYGA, GAGAGA, GAGAGV, GAGVGA, or GAGAGVGY, or a combination of two or more 315 thereof Collagen / CLP and Keratin Fusion Proteins 5 GGVCGPSPPCITTGPTGPTGPAGPRGLQGLQGLQGERGEQGPTGGVCGPSPPCGPTGPTGPAGPRGLQGLQGLQGERGEQGPT CGPSPPCITTGPTGPTGPAGPRGLQGLQGLQGERGEQGPT YGGSSGGGGPTGPTGPAGPRGLQGLQGLQGERGEQGPT FGGGSGPTGPTGPAGPRGLQGLQGLQGERGEQGPT CCQSSCCKPSCGPTGPTGPAGPRGLQGLQGLQGERGEQGPT CVSSCCKPQCCGPTGPTGPAGPRGLQGLQGLQGERGEQGPT PITCRRTCYHGPTGPTGPAGPRGLQGLQGLQGERGEQGPT DCKLPCNPCAGPTGPTGPAGPRGLQGLQGLQGERGEQGPT CLPCLPAASCGPTGPTGPAGPRGLQGLQGLQGERGEQGPT CEPAICEPSCGPTGPTGPAGPRGLQGLQGLQGERGEQGPT CQCSCCKPYCSGPTGPTGPAGPRGLQGLQGLQGERGEQGPT FCGFPSCSTSCGPTGPTGPAGPRGLQGLQGLQGERGEQGPT CTPPSCCQLHHAGPTGPTGPAGPRGLQGLQGLQGERGEQGPT SCCAPVYCCKGPTGPTGPAGPRGLQGLQGLQGERGEQGPT GGVCGPSPPCITTGPTGPT GGVCGPSPPCGPTGPT CGPSPPCITTGPTGPT YGGSSGGGGPTGPT FGGGSGPTGPT CCQSSCCKPSCGPTGPT CVSSCCKPQCCGPTGPT PITCRRTCYHGPTGPT DCKLPCNPCAGPTGPT CLPCLPAASCGPTGPT CEPAICEPSCGPTGPT CQCSCCKPYCSGPTGPT FCGFPSCSTSCGPTGPT CTPPSCCQLHHAGPTGPT SCCAPVYCCKGPTGPT GGVCGPSPPCITTGLQGLQ GGVCGPSPPCGLQGLQ CGPSPPCITTGLQGLQ YGGSSGGGGLQGLQ FGGGSGLQGLQ CCQSSCCKPSCGLQGLQ CVSSCCKPQCCGLQGLQ PITCRRTCYHGLQGLQ DCKLPCNPCAGLQGLQ CLPCLPAASCGLQGLQ CEPAICEPSCGLQGLQ CQCSCCKPYCSGLQGLQ FCGFPSCSTSCGLQGLQ CTPPSCCQLHHAGLQGLQ SCCAPVYCCKGLQGLQ GGVCGPSPPCITT(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of two or more thereofGGVCGPSPPC(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of two or 361 more thereof CGPSPPCITT(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of two or 362 more thereof YGGSSGGG(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of two or 363 more thereof FGGGS(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of two or more 364 thereof CCQSSCCKPSC(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of two or 365 more thereof CVSSCCKPQCC(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of two or 366 more thereof PITCRRTCYH(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of two or 367 more thereof DCKLPCNPCA(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of two or 368 more thereof CLPCLPAASC(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of two or 369 more thereof CEPAICEPSC(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of two or 370 more thereof CQCSCCKPYCS(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of two or 371 more thereof FCGFPSCSTSC(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of two or 372 more thereof CTPPSCCQLHHA(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of 373 two or more thereof SCCAPVYCCK(X), wherein X comprises GXPGXP (each X is independently any amino acid), GZPGZP (each Z is 4-hydroxyproline), or GPAGPA, or a combination of two or 374 more thereof Resilin / RLP and Keratin Fusion Proteins 4 GGVCGPSPPCITTGGRPSDSYGAPGGGN 375 GGVCGPSPPCGGRPSDSYGAPGGGN 376 CGPSPPCITTGGRPSDSYGAPGGGN 377 YGGSSGGGGGRPSDSYGAPGGGN 378 FGGGSGGRPSDSYGAPGGGN379 CCQSSCCKPSCGGRPSDSYGAPGGGN 380 CVSSCCKPQCCGGRPSDSYGAPGGGN 381 PITCRRTCYHGGRPSDSYGAPGGGN 382 DCKLPCNPCAGGRPSDSYGAPGGGN 383 CLPCLPAASCGGRPSDSYGAPGGGN 384 CEPAICEPSCGGRPSDSYGAPGGGN 385 CQCSCCKPYCSGGRPSDSYGAPGGGN 386 FCGFPSCSTSCGGRPSDSYGAPGGGN 387 CTPPSCCQLHHAGGRPSDSYGAPGGGN 388 SCCAPVYCCKGGRPSDSYGAPGGGN 389 GGVCGPSPPCITTGAPAQTPSSQY 390 GGVCGPSPPCGAPAQTPSSQY 391 CGPSPPCITTGAPAQTPSSQY 392 YGGSSGGGGAPAQTPSSQY 393 FGGGSGAPAQTPSSQY 394 CCQSSCCKPSCGAPAQTPSSQY 395 CVSSCCKPQCCGAPAQTPSSQY 396 PITCRRTCYHGAPAQTPSSQY 397 DCKLPCNPCAGAPAQTPSSQY 398 CLPCLPAASCGAPAQTPSSQY 399 CEPAICEPSCGAPAQTPSSQY 400 CQCSCCKPYCSGAPAQTPSSQY 401 FCGFPSCSTSCGAPAQTPSSQY 402 CTPPSCCQLHHAGAPAQTPSSQY 403 SCCAPVYCCKGAPAQTPSSQY 404 GGVCGPSPPCITTAQTPSSQYGAP 405 GGVCGPSPPCAQTPSSQYGAP 406 CGPSPPCITTAQTPSSQYGAP 407 YGGSSGGGAQTPSSQYGAP 408 FGGGSAQTPSSQYGAP 409 CCQSSCCKPSCAQTPSSQYGAP 410 CVSSCCKPQCCAQTPSSQYGAP 411 PITCRRTCYHAQTPSSQYGAP 412 DCKLPCNPCAAQTPSSQYGAP 413 CLPCLPAASCAQTPSSQYGAP 414 CEPAICEPSCAQTPSSQYGAP 415 CQCSCCKPYCSAQTPSSQYGAP 416 FCGFPSCSTSCAQTPSSQYGAP 417 CTPPSCCQLHHAAQTPSSQYGAP 418 SCCAPVYCCKAQTPSSQYGAP Abductin / ALP and Keratin Fusion Proteins 6 GGVCGPSPPCITTGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS 419 GGVCGPSPPCGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS 420 CGPSPPCITTGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS 421 YGGSSGGGGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS 422 FGGGSGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS 423 CCQSSCCKPSCGGFGGMGGGSGGFGGMGGGSGGFGGMGGGSCVSSCCKPQCCGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS PITCRRTCYHGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS DCKLPCNPCAGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS CLPCLPAASCGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS CEPAICEPSCGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS CQCSCCKPYCSGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS FCGFPSCSTSCGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS CTPPSCCQLHHAGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS SCCAPVYCCKGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS GGVCGPSPPCITTMGGG GGVCGPSPPCMGGG CGPSPPCITTMGGG YGGSSGGGMGGG FGGGSMGGG CCQSSCCKPSCMGGG CVSSCCKPQCCMGGG PITCRRTCYHMGGG DCKLPCNPCAMGGG CLPCLPAASCMGGG CEPAICEPSCMGGG CQCSCCKPYCSMGGG FCGFPSCSTSCMGGG CTPPSCCQLHHAMGGG SCCAPVYCCKMGGG GGVCGPSPPCITTFGGMG GGVCGPSPPCFGGMG CGPSPPCITTFGGMG YGGSSGGGFGGMG FGGGSFGGMG CCQSSCCKPSCFGGMG CVSSCCKPQCCFGGMG PITCRRTCYHFGGMG DCKLPCNPCAFGGMG CLPCLPAASCFGGMG CEPAICEPSCFGGMG CQCSCCKPYCSFGGMG FCGFPSCSTSCFGGMG CTPPSCCQLHHAFGGMG SCCAPVYCCKFGGMG GGVCGPSPPCITT(X), wherein X comprises GGFGGMGGGS, FGGMGGG, GGFGGMGGG, or FGGMGGGNAG, or a combination of two or more thereof GGVCGPSPPC(X), wherein X comprises GGFGGMGGGS, FGGMGGG, GGFGGMGGG, or FGGMGGGNAG, or a combination of two or more thereof CGPSPPCITT(X), wherein X comprises GGFGGMGGGS, FGGMGGG, GGFGGMGGG, or FGGMGGGNAG, or a combination of two or more thereof YGGSSGGG(X), wherein X comprises GGFGGMGGGS, FGGMGGG, GGFGGMGGG, or FGGMGGGNAG, or a combination of two or more thereofFGGGS(X), wherein X comprises GGFGGMGGGS, FGGMGGG, GGFGGMGGG, or 467 FGGMGGGNAG, or a combination of two or more thereof CCQSSCCKPSC(X), wherein X comprises GGFGGMGGGS, FGGMGGG, GGFGGMGGG, 468 or FGGMGGGNAG, or a combination of two or more thereof CVSSCCKPQCC(X), wherein X comprises GGFGGMGGGS, FGGMGGG, GGFGGMGGG, 469 or FGGMGGGNAG, or a combination of two or more thereof PITCRRTCYH(X), wherein X comprises GGFGGMGGGS, FGGMGGG, GGFGGMGGG, or 470 FGGMGGGNAG, or a combination of two or more thereof DCKLPCNPCA(X), wherein X comprises GGFGGMGGGS, FGGMGGG, GGFGGMGGG, 471 or FGGMGGGNAG, or a combination of two or more thereof CLPCLPAASC(X), wherein X comprises GGFGGMGGGS, FGGMGGG, GGFGGMGGG, or 472 FGGMGGGNAG, or a combination of two or more thereof CEPAICEPSC(X), wherein X comprises GGFGGMGGGS, FGGMGGG, GGFGGMGGG, or 473 FGGMGGGNAG, or a combination of two or more thereof CQCSCCKPYCS(X), wherein X comprises GGFGGMGGGS, FGGMGGG, GGFGGMGGG, 474 or FGGMGGGNAG, or a combination of two or more thereof FCGFPSCSTSC(X), wherein X comprises GGFGGMGGGS, FGGMGGG, GGFGGMGGG, 475 or FGGMGGGNAG, or a combination of two or more thereof CTPPSCCQLHHA(X), wherein X comprises GGFGGMGGGS, FGGMGGG, 476 GGFGGMGGG, or FGGMGGGNAG, or a combination of two or more thereof SCCAPVYCCK(X), wherein X comprises GGFGGMGGGS, FGGMGGG, GGFGGMGGG, or 477 FGGMGGGNAG, or a combination of two or more thereof Linker / Spacer-like and Keratin Fusion Proteins 44 GGVCGPSPPCITTGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 45 GGVCGPSPPCITTAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK 46 GGVCGPSPPCITTLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK 47 GGVCGPSPPCITTGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA 478 GGVCGPSPPCGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 479 CGPSPPCITTGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 480 YGGSSGGGGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 481 FGGGSGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 482 CCQSSCCKPSCGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 483 CVSSCCKPQCCGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 484 PITCRRTCYHGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 485 DCKLPCNPCAGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 486 CLPCLPAASCGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 487 CEPAICEPSCGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 488 CQCSCCKPYCSGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 489 FCGFPSCSTSCGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 490 CTPPSCCQLHHAGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 491 SCCAPVYCCKGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQ 492 GGVCGPSPPCAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK 493 CGPSPPCITTAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK 494 YGGSSGGGAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK 495 FGGGSAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK 496 CCQSSCCKPSCAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK 497 CVSSCCKPQCCAKAKAKAKAKAKAKAKAKAKAKAKAKAKAKPITCRRTCYHAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK DCKLPCNPCAAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK CLPCLPAASCAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK CEPAICEPSCAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK CQCSCCKPYCSAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK FCGFPSCSTSCAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK CTPPSCCQLHHAAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK SCCAPVYCCKAKAKAKAKAKAKAKAKAKAKAKAKAKAKAK GGVCGPSPPCLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK CGPSPPCITTLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK YGGSSGGGLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK FGGGSLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK CCQSSCCKPSCLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK CVSSCCKPQCCLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK PITCRRTCYHLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK DCKLPCNPCALKLKLKLKLKLKLKLKLKLKLKLKLKLKLK CLPCLPAASCLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK CEPAICEPSCLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK CQCSCCKPYCSLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK FCGFPSCSTSCLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK CTPPSCCQLHHALKLKLKLKLKLKLKLKLKLKLKLKLKLKLK SCCAPVYCCKLKLKLKLKLKLKLKLKLKLKLKLKLKLKLK GGVCGPSPPCGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA CGPSPPCITTGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA YGGSSGGGGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA FGGGSGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA CCQSSCCKPSCGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA CVSSCCKPQCCGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA PITCRRTCYHGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA DCKLPCNPCAGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA CLPCLPAASCGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA CEPAICEPSCGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA CQCSCCKPYCSGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA FCGFPSCSTSCGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA CTPPSCCQLHHAGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA SCCAPVYCCKGAGAGAGAGAGAGAGAGAGAGAGAGAGAGA GGVCGPSPPCITT(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1-20; (LK)n, where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or more thereof GGVCGPSPPC(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1- 20; (LK)n, where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or more thereof CGPSPPCITT(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1-20; (LK)n, where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or more thereofYGGSSGGG(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1-20; (LK)n, where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or more 537 thereof FGGGS(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1-20; (LK)n, 538 where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or more thereof CCQSSCCKPSC(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1- 20; (LK)n, where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or more 539 thereof CVSSCCKPQCC(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1- 20; (LK)n, where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or more 540 thereof PITCRRTCYH(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1-20; (LK)n, where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or more 541 thereof DCKLPCNPCA(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1- 20; (LK)n, where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or more 542 thereof CLPCLPAASC(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1-20; (LK)n, where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or more 543 thereof CEPAICEPSC(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1-20; (LK)n, where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or more 544 thereof CQCSCCKPYCS(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1- 20; (LK)n, where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or more 545 thereof FCGFPSCSTSC(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1- 20; (LK)n, where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or more 546 thereof CTPPSCCQLHHA(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1-20; (LK)n, where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or 547 more thereof SCCAPVYCCK(X), wherein X comprises (GQ)n, where n is 1-20; (AK)n, where n is 1- 20; (LK)n, where n is 1-20; or (GA)n, where n is 1-20; or a combination of two or more 548 thereof Additional Fusion Proteins 549 GGVCGPSPPCITTGAGAGSGAGAGSVPAVGVPAVGVPAVG GGVCGPSPPCITTRGAGAGSGAGAGSGAGAGSVPAVGVPAVGVPAVGVPAVGVPAVGVPA 550 VGVPAVGVPAVGVPAVGVPAVG GGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGG NGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGG GNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGQGQGQGQGQGQGQGQGQGQGGVC GPSPPCITTGQGQGQGQGQGQGQGQGQGQVPAVGVPAVGVPAVGVPAVGVPAVGVPA VGVPAVGVPAVGVPAVGVPAVGGQGQGQGQGQGQGQGQGQGQGGVCGPSPPCITTGQ GQGQGQGQGQGQGQGQGQGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYG APGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSY 551 GAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGN

[0205] Table 2 provides example embodiments of keratin and keratin associated fusion proteins.

[0206] In some embodiments, the keratin or keratin associated fusion proteins / peptides comprise or are selected from the following list of sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO:7; SEQ ID NO:44; SEQ ID NO:45; SEQ ID NO:46; SEQ ID NO:47. In some embodiments, the keratin or keratin associated fusion proteins comprise or are selected from any one of SEQ ID NOS: 200-551.

[0207] In some embodiments, the keratin or keratin associated fusion protein / peptide is SEQ ID NO: 1.

[0208] In some embodiments, the keratin or keratin associated fusion protein / peptide is SEQ ID NO: 2.

[0209] In some embodiments, the keratin or keratin associated fusion protein / peptide is SEQ ID NO: 3.

[0210] In some embodiments, the keratin or keratin associated fusion protein / peptide is SEQ ID NO: 4.

[0211] In some embodiments, the keratin or keratin associated fusion protein / peptide is SEQ ID NO: 5.

[0212] In some embodiments, the keratin or keratin associated fusion protein / peptide is SEQ ID NO: 6.

[0213] In some embodiments, the keratin or keratin associated fusion protein / peptide is SEQ ID NO: 7.

[0214] In some embodiments, the keratin or keratin associated fusion protein / peptide is SEQ ID NO: 44.

[0215] In some embodiments, the keratin or keratin associated fusion protein / peptide is SEQ ID NO: 45.

[0216] In some embodiments, the keratin or keratin associated fusion protein / peptide is SEQ ID NO: 46. some embodiments, the keratin or keratin associated fusion protein / peptide is SEQ ID

[0218] In some embodiments, the keratin or keratin associated fusion proteins / peptides comprise a protein having at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 99% or more sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551.

[0219] In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 50% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551.

[0220] In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 55% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551.

[0221] In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 60% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551.

[0222] In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 65% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551.

[0223] In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 70% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551.

[0224] In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 75% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551.

[0225] In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 80% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551.

[0226] In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 85% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551.

[0227] In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 90% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551. In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 91% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551. In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 92% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551. In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 93% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551. In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 94% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551.

[0228] In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 95% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551. In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least96% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551. In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 97% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551. In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 98% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551.

[0229] In some embodiments, the keratin or keratin associated fusion proteins comprise a protein having at least 99% sequence identity with any one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, or SEQ ID NO: 7, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46; SEQ ID NO: 47, or SEQ ID NOS: 200-551.

[0230] In some embodiments, the keratin or keratin associated fusion protein comprises a keratin or keratin associated peptide, connected to an elastin or ELP. The connection may be via a covalent bond. The connection may be via a linker. The linker may be a peptide linker. The peptide linker may comprise about 1 to about 10 amino acids. The fusion protein may comprise GGVCGPSPPCITTVPGVG (SEQ ID NO: 62). The fusion protein may comprise any one of SEQ ID NOS: 1, 2, 7, or 200-271.

[0231] In some embodiments, the keratin or keratin associated fusion protein comprises a keratin or keratin associated peptide, connected to a silk or SLP. The connection may be via a covalent bond. The connection may be via a linker. The linker may be a peptide linker. The peptide linker may comprise about 1 to about 10 amino acids. The fusion protein may comprise GGVCGPSPPCITTGAGAGS (SEQ ID NO: 63). The fusion protein may comprise any one of SEQ ID NOS: 3 or 272-315.

[0232] In some embodiments, the keratin or keratin associated fusion protein comprises a keratin or keratin associated peptide, connected to a resilin or RLP. The connection may be via a covalent bond. The connection may be via a linker. The linker may be a peptide linker. The peptide linker may comprise about 1 to about 10 amino acids. The fusion protein may compriseGGVCGPSPPCITTGGRPSDSYGAPGGGN (SEQ ID NO: 4). The fusion protein may comprise any one of SEQ ID NOS: 4 of 375-418.

[0233] In some embodiments, the keratin or keratin associated fusion protein comprises a keratin or keratin associated peptide, connected to a collagen or CLP. The connection may be via a covalent bond. The connection may be via a linker. The linker may be a peptide linker. The peptide linker may comprise about 1 to about 10 amino acids. The fusion protein may comprise GGVCGPSPPCITTGPT (SEQ ID NO: 64). The fusion protein may comprise any one of SEQ ID NOS: 5 or 316-374.

[0234] In some embodiments, the keratin or keratin associated fusion protein comprises a keratin or keratin associated peptide, connected to an abductin or ALP. The connection may be via a covalent bond. The connection may be via a linker. The linker may be a peptide linker. The peptide linker may comprise about 1 to about 10 amino acids. The fusion protein may comprise GGVCGPSPPCITTGGFGGMGGGS (SEQ ID NO: 65). The fusion protein may comprise any one of SEQ ID NOS: 6 or 419-477. Keratin and Keratin-Associate Fusion Proteins / Peptides

[0235] In other or additional aspects, the present disclosure includes keratin and keratin associated fusion protein / peptide. The keratin and keratin associated fusion protein / peptide of the present disclosure comprise co-polymers comprising various blocks. Each block of the co- polymer comprises monomers of amino acid residues. For example, amino acids such as alanine, arginine, asparagine, aspartate, cysteine, glutamine, glutamate, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, proline, serine, threonine, tryptophan, tyrosine, and valine, and two or more thereof.

[0236] In some embodiments, the keratin and keratin associated fusion protein / peptide disclosed herein comprise amino acid sequences (the term “peptides” may be used interchangeably to refer to the amino acid sequences) that may be joined by a covalent bond or any other type of bond that leads to a structure which maintains the properties of the fusion proteins of the present disclosure. The bond may be selected from, but is not limited to, hydrogen bonds, ion pairing, hydrophobic association, or inclusion complex formation.

[0237] In some embodiments, the keratin and keratin associated fusion proteins have Formula (I) [Bn1 – Am – Bn – Co – B n2]p .

[0238] In some embodiments, the keratin and keratin associated fusion proteins have Formula (II) [Bn1– Co-Bn– Am– Bn2]p.

[0239] In some embodiments, the keratin and keratin associated fusion proteins have Formula (III) [Bn1– Bn– Co– Am– Bn2]p.

[0240] In some embodiments, the keratin and keratin associated fusion proteins have Formula (IV) [Bn1- Co-Am-Bn-Bn2]p.

[0241] In some embodiments, “A” comprises a peptide sequence comprising a keratin or keratin associated peptide block. In an example embodiment, the keratin or keratin associated peptide block is a keratin or keratin associated peptide component as described elsewhere herein. In some embodiments, a keratin, keratin peptide, or keratin associated peptide includes a wild-type keratin peptide, a functional fragment of a wild-type keratin peptide, or a peptide having at least 90% identity to a wild-type keratin peptide or a functional fragment of a wild-type keratin peptide. The wild-type keratin peptide may be keratin 85 having SEQ ID NO: 48. The wild-type peptide keratin peptide may comprise SEQ ID NO: 8, 9, 10, 66, or 67, or a combination of two or more thereof. In some embodiments, the keratin, keratin peptide, or keratin associated peptide forms one or more disulfide bonds with hair, skin, or nails, or a combination of two or more thereof.

[0242] In a non-limiting example embodiment, a functional fragment of a wild-type keratin peptide comprises at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 contiguous amino acids of a wild- type keratin peptide. In a non-limiting example embodiment, a functional fragment of a wild- type keratin peptide comprises at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids having at least 90% identity to a wild-type keratin peptide. In a non-limiting example embodiment, a functional fragment of a wild-type keratin peptide comprises at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids, where the at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids comprise one or more cysteine amino acids. For instance, the one or more cysteine amino acids is 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26 or 27 cysteine amino acids. In a non-limiting example embodiment, a functional fragment of a wild- type keratin peptide comprises at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids, where at least 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20%, 30%, 40%, or 50% of the at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids are cysteine amino acids. A non-limiting example embodiment of a keratin or keratin peptide is provided in SEQ ID NO: 48.

[0243] In some embodiments, a keratin associated peptide (sometimes referred to as a keratin associated protein) includes a peptide that forms a disulfide bond with wild-type keratin. In some embodiments, a keratin associated peptide comprises at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids, and the at least 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 amino acids are at least 90% identical to a wild-type keratin peptide sequence. The wild-type keratin peptide may be keratin 85 having SEQ ID NO: 48. The wild-type peptide keratin peptide may comprise SEQ ID NO: 8, 9, 10, 66, or 67, or a combination of two or more thereof.

[0244] In some embodiments, the number of amino acids in the keratin or keratin associated peptide block of the fusion protein / peptide is from about 6 residues to about 16 residues.

[0245] In some embodiments, the number of amino acids in the keratin or keratin associated peptide block of the fusion protein / peptide is about 6 residues.

[0246] In some embodiments, the number of amino acids in the keratin or keratin associated peptide block of the fusion protein / peptide is about 7 residues.

[0247] In some embodiments, the number of amino acids in the keratin or keratin associated peptide block of the fusion protein / peptide is about 8 residues.

[0248] In some embodiments, the number of amino acids in the keratin or keratin associated peptide block of the fusion protein / peptide is about 9 residues.

[0249] In some embodiments, the number of amino acids in the keratin or keratin associated peptide block of the fusion protein / peptide is about 10 residues.

[0250] In some embodiments, the number of amino acids in the keratin or keratin associated peptide block of the fusion protein / peptide is about 11 residues.

[0251] In some embodiments, the number of amino acids in the keratin or keratin associated peptide block of the fusion protein / peptide is about 12 residues.

[0252] In some embodiments, the number of amino acids in the keratin or keratin associated peptide block of the fusion protein / peptide is about 13 residues.

[0253] In some embodiments, the number of amino acids in the keratin or keratin associated peptide block of the fusion protein / peptide is about 14 residues.

[0254] In some embodiments, the number of amino acids in the keratin or keratin associated peptide block of the fusion protein / peptide is about 15 residues.

[0255] In some embodiments, the number of amino acids in the keratin or keratin associated peptide block of the fusion protein / peptide is about 16 residues.

[0256] In some embodiments, the keratin or keratin associated peptide block of the fusion protein / peptide possesses a relatively high cysteine content to enrich certain properties of the keratin or keratin associated peptide block, such as, for example, to enhance formation of intermolecular cross-linking. The total cysteine content ranges from 10% to 50% of the total number of amino acids in the keratin or keratin associated peptide block. In some embodiments, the total cysteine content is at least 15% of the total number of amino acids in the keratin or keratin associated peptide block.

[0257] In some embodiments, the keratin or keratin associated peptide block of the fusion protein comprises 2 cysteine residues.

[0258] In some embodiments, the keratin or keratin associated peptide block of the fusion protein comprises 3 cysteine residues.

[0259] In some embodiments, the keratin or keratin associated peptide block of the fusion protein comprises 4 cysteine residues.

[0260] In some embodiments, the keratin or keratin associated peptide block of the fusion protein comprises 5 cysteine residues.

[0261] In some embodiments, the keratin or keratin associated peptide block of the fusion protein has the peptide sequence (X3)kC(X3)5C(X3)k.

[0262] In some embodiments, each “X3” is independently glycine, alanine, valine, isoleucine, leucine, phenylalanine, proline, serine, threonine, asparagine, glutamine, cysteine, methionine, phenylalanine, tyrosine, tryptophan, aspartate, glutamate, histidine, lysine, or arginine.

[0263] In some embodiments, each “k” is independently an integer ranging from 0 to 3. If k is 2, then (X3)k has a first X3and a second X3, where each X3is independently glycine, alanine, valine, isoleucine, leucine, phenylalanine, proline, serine, threonine, asparagine, glutamine, cysteine, methionine, phenylalanine, tyrosine, tryptophan, aspartate, glutamate, histidine, lysine, or arginine. If k is 3, then (X3)k has a first X3, a second X3, and a third X3, where each X3is independently glycine, alanine, valine, isoleucine, leucine, phenylalanine, proline, serine, threonine, asparagine, glutamine, cysteine, methionine, phenylalanine, tyrosine, tryptophan, aspartate, glutamate, histidine, lysine, or arginine. (X3)5 has a first X3, a second X3, a third X3, afourth X3, and a fifth X3, where each X3is independently glycine, alanine, valine, isoleucine, leucine, phenylalanine, proline, serine, threonine, asparagine, glutamine, cysteine, methionine, phenylalanine, tyrosine, tryptophan, aspartate, glutamate, histidine, lysine, or arginine.

[0264] In some embodiments, the keratin or keratin associate peptide block of the fusion protein / peptide comprises GGVCGPSPPCITT (SEQ ID NO: 8), GGVCGPSPPC (SEQ ID NO: 9), CGPSPPCITT (SEQ ID NO: 10), CGPSPPC (SEQ ID NO: 66), GVCGPSPPC (SEQ ID NO: 67), CLPCLPAASC (SEQ ID NO: 68), CLPAASC (SEQ ID NO: 69), YGGSSGGG (SEQ ID NO: 70), FGGGS (SEQ ID NO: 71), CCQSSCCKPSC (SEQ ID NO: 72), CVSSCCKPQCC (SEQ ID NO: 73), PITCRRTCYH (SEQ ID NO: 74), DCKLPCNPCA (SEQ ID NO: 75), CLPCLPAASC (SEQ ID NO: 76), CEPAICEPSC (SEQ ID NO: 77), CQCSCCKPYCS (SEQ ID NO: 78), FCGFPSCSTSC (SEQ ID NO: 79), CTPPSCCQLHHA (SEQ ID NO: 80), SCCAPVYCCK (SEQ ID NO: 81), or a combination or two or more thereof.

[0265] In some embodiments, the keratin or keratin associated peptide block of the fusion protein / peptide comprises GGVCGPSPPCITT (SEQ ID NO: 8), GGVCGPSPPC (SEQ ID NO: 9), CGPSPPCITT (SEQ ID NO: 10), CGPSPPC (SEQ ID NO: 66), or GVCGPSPPC (SEQ ID NO: 67),or a combination or two or more thereof.

[0266] In some embodiments, the keratin or keratin associated peptide block is GGVCGPSPPCITT (SEQ ID NO: 8) or CGPSPPCITT (SEQ ID NO: 10).

[0267] In some embodiments, the keratin or keratin associated peptide block of the fusion protein / peptide comprises YGGSSGGG (SEQ ID NO: 70), FGGGS (SEQ ID NO: 71), or a combination or two or more thereof.

[0268] In some embodiments, the keratin or keratin associated peptide block of the fusion protein / peptide comprises CCQSSCCKPSC (SEQ ID NO: 72), CVSSCCKPQCC (SEQ ID NO: 73), or a combination or two or more thereof.

[0269] In some embodiments, the keratin or keratin associated peptide block of the fusion protein / peptide comprises PITCRRTCYH (SEQ ID NO: 74).

[0270] In some embodiments, the keratin or keratin associated peptide block of the fusion protein comprises DCKLPCNPCA (SEQ ID NO: 75).

[0271] In some embodiments, the keratin or keratin associated peptide block of the fusion protein comprises CLPCLPAASC (SEQ ID NO: 76).

[0272] In some embodiments, the keratin or keratin associated peptide block of the fusion protein comprises CEPAICEPSC (SEQ ID NO: 77).

[0273] In some embodiments, the keratin or keratin associated peptide block of the fusion protein comprises CQCSCCKPYCS (SEQ ID NO: 78).

[0274] In some embodiments, the keratin or keratin associated peptide block of the fusion protein comprises FCGFPSCSTSC (SEQ ID NO: 79).

[0275] In some embodiments, the keratin or keratin associated peptide block of the fusion protein comprises CTPPSCCQLHHA (SEQ ID NO: 80).

[0276] In some embodiments, the keratin or keratin associated peptide block of the fusion protein comprises SCCAPVYCCK (SEQ ID NO: 81).

[0277] In some embodiments, “m” is an integer from 1 to 10.

[0278] In some embodiments, “m” is about 1.

[0279] In some embodiments, “m” is about 2.

[0280] In some embodiments, “m” is about 3.

[0281] In some embodiments, “m” is about 4.

[0282] In some embodiments, “m” is about 5.

[0283] In some embodiments, “m” is about 6.

[0284] In some embodiments, “m” is about 7.

[0285] In some embodiments, “m” is about 8.

[0286] In some embodiments, “m” is about 9.

[0287] In some embodiments, “m” is about 10.

[0288] In some embodiments, “B” comprises a linker or a termination. Linkers aid fusion protein design by providing appropriate spacing between domains and support correct protein folding in the case that N or C termini interactions are crucial to folding. Commonly, linkers permit important domain interactions, reinforce stability, mobility and reduce steric hindrance, making them suitable for use in protein / peptide design even when N and C termini can be fused. The three major types of linkers are flexible, rigid, and in vivo cleavable. Termination (N- or C- terminal) peptides aid in binding processes, synthesis stability and correct folding.

[0289] In some embodiments, “B” comprises a peptide sequence comprising or having one to three amino acids. In some embodiments, “B” comprises a peptide sequence comprising or having one to three amino acids repeated 0 to about 25 times. In some embodiments, “B” comprises a peptide sequence comprising one or two amino acids repeated about 10 to about 25 times. In some embodiments, each of the amino acids in the peptide sequence is independently arginine, histidine, lysine, aspartic acid, glutamic acid, serine, threonine, asparagine, glutamine, cysteine, selenocysteine, glycine, proline, alanine, valine, isoleucine, leucine, methionine, phenylalanine, tyrosine, or tryptophan. In some embodiments, B has 1 to 40 amino acids.

[0290] In some embodiments, each “n,” n1”, and “n2” are independently an integer from 0 to 25.

[0291] In some embodiments, “n, n1, and n2”is 0.

[0292] In some embodiments, “n, n1, and n2” is about 1.

[0293] In some embodiments, “n, n1, and n2” is about 2.

[0294] In some embodiments, “n, n1, and n2” is about 3.

[0295] In some embodiments, “n, n1, and n2” is about 4.

[0296] In some embodiments, “n, n1, and n2” is about 5.

[0297] In some embodiments, “n, n1, and n2” is about 6.

[0298] In some embodiments, “n, n1, and n2” is about 7.

[0299] In some embodiments, “n, n1, and n2” is about 8.

[0300] In some embodiments, “n, n1, and n2” is about 9.

[0301] In some embodiments, “n, n1, and n2” is about 10.

[0302] In some embodiments, “n, n1, and n2” is about 11.

[0303] In some embodiments, “n, n1, and n2” is about 12.

[0304] In some embodiments, “n, n1, and n2” is about 13.

[0305] In some embodiments, “n, n1, and n2” is about 14.

[0306] In some embodiments, “n, n1, and n2” is about 15.

[0307] In some embodiments, “n, n1, and n2” is about 16.

[0308] In some embodiments, “n, n1, and n2” is about 17.

[0309] In some embodiments, “n, n1, and n2” is about 18.

[0310] In some embodiments, “n, n1, and n2” is about 19.

[0311] In some embodiments, “n, n1, and n2” is about 20.

[0312] In some embodiments, “n, n1, and n2” is about 21.

[0313] In some embodiments, “n, n1, and n2” is about 22.

[0314] In some embodiments, “n, n1, and n2” is about 23.

[0315] In some embodiments, “n, n1, and n2” is about 24.

[0316] In some embodiments, “n, n1, and n2” is about 25.

[0317] In some embodiments, “C” comprises a peptide sequence having the structure Dq-Er-Fs- Gt-Hu.

[0318] In some embodiments, blocks “D,” “E,” “F,” “G,” and “H” may be provided in any order.

[0319] In some embodiments, “D” comprises a silk or a silk-like peptide (SLP) block.

[0320] In some embodiments, “E” comprises a collagen or collagen-like peptide (CLP) block.

[0321] In some embodiments, “F” comprises an elastin or elastin-like peptide (ELP) block.

[0322] In some embodiments, “G” comprises a resilin or resilin-like peptide (RLP) block.

[0323] In some embodiments, “H” comprises an abductin or abductin-like peptide (ALP) block.

[0324] In some embodiments, the keratin or keratin associated fusion proteins disclosed herein comprise an elastin or elastin-like polypeptide (ELP) block (“F”). In some embodiments, elastin- like polypeptide (ELP) refers to a peptide, including a synthetic peptide, comprising an amino acid sequence having a similar secondary structure, tertiary structure, or amino acid sequence, or a combination of two or more thereof, to a wild-type elastin protein (e.g., SEQ ID NO: 55), or a fragment of a wild-type elastin protein. In some embodiments, a fragment includes a sequence having at least 4, 5, 6, 7, 8, 9, or 10 amino acids 100% identical to a sequence of wild-type elastin protein. Non-limiting example elastin and ELPs include SEQ ID NOS: 11-23, 49-55, 82-91, and 104.

[0325] ELPs may comprise polymeric or oligomeric repeating peptide sequences of an elastin protein. In an example embodiment, an elastin or ELP comprises SEQ ID NO: 49 ((VPGXG)n, where n is 1 to 10 and each X is independently any amino acid), or a sequence having no more than 1amino acid substitution as compared to SEQ ID NO: 49. In some embodiments, each X is independently valine or leucine. In some embodiments, n is 5. In some embodiments, n is 6.

[0326] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 50 (VPGVG), or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 50. The elastin or ELP may comprise 1 to 10 sequences having SEQ ID NO: 50, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 50. The 1 to 10 sequences may be connected, e.g., VPGVGVPGVGVPGVGVPGVGVPGVGVPGVG (SEQ ID NO: 23), or may be separated by one or more amino acids, e.g., by another ELP as in VPGVGVPGVGVPGLGVPGVGVPGVG (SEQ ID NO: 54).

[0327] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 51 (VPGLG), or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 51. The elastin or ELP may comprise 1 to 10 sequences having SEQ ID NO: 51, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 51. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids.

[0328] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 52 (VPGVGVPGL), or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 52. The elastin or ELP may comprise 1 to 10 sequences having SEQ ID NO: 52, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 52. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids.

[0329] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 53 (VPGVGVPGVGVPGLGVPGVGVPGVGR) or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 53. The elastin or ELP may comprise 1 to 10 sequences having SEQ ID NO: 53, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 53. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids.

[0330] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 23 (VPGVGVPGVGVPGVGVPGVGVPGVGVPGVG), or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 23. The elastin or ELP may comprise 1 to 10 sequences having SEQ ID NO: 23, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 23. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids.

[0331] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 54 (VPGVGVPGVGVPGLGVPGVGVPGVG), or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 54. The elastin or ELP may comprise 1 to 10 sequences having SEQ ID NO: 54, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 54. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids.

[0332] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 22 (GVGVPGVGVPGLGVPGVGVPGVG), or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 22. The elastin or ELP may comprise 1 to 10 sequences having SEQ ID NO: 22, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 22. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids.

[0333] In an example embodiment, an elastin or ELP comprises SEQ ID NO: 82 (IPGLG), or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 82. The elastin or ELP may comprise 1 to 10 sequences having SEQ ID NO: 82, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 82. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids. In some embodiments, the elastin or ELP comprises SEQ ID NO: 85 (IPGVGIPGLG), SEQ ID NO: 89 (VPGVGIPGLG), or a combination thereof.

[0334] In some embodiments, an elastin or ELP comprises a polymeric or oligomeric repeating peptide sequence of an elastin peptide. In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 4 amino acid residues.

[0335] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 5 amino acid residues. As a non-limiting example, SEQ ID NOS: 49, 50 or 51.

[0336] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 6 amino acid residues.

[0337] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 7 amino acid residues.

[0338] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 8 amino acid residues.

[0339] Non-limiting example repeating peptide sequences include polytetra-, polypenta-, polyhexa-, polyhepta-, polyocta-, and polynonapeptides, including but not limited to, VPGG (SEQ ID NO: 11), IPGG (SEQ ID NO: 12) VPAVG (SEQ ID NO: 13), AVGVP (SEQ ID NO: 14), IPGVG (SEQ ID NO: 15), LPGVG (SEQ ID NO: 16), VAPGVG (SEQ ID NO: 17), GVGVPGVG (SEQ ID NO: 18), VPGFGVGAG (SEQ ID NO: 19), VPGVGVPGG (SEQ ID NO: 20), VPGX2G (SEQ ID NO: 21), SEQ ID NO: 49 ((VPGXG)n, where n is 1 to 10 and each X is independently any amino acid), SEQ ID NO: 50 (VPGVG), SEQ ID NO: 51 (VPGLG), and SEQ ID NO: 52 (VPGVGVPGL), and combinations of two or more thereof.

[0340] In some embodiments, “X2” comprises a naturally occurring or a non-naturally occurring amino acid.

[0341] In some embodiments, elastin or ELPs are polymeric or oligomeric repeats of the pentapeptide VPAVG.

[0342] In some embodiments, elastin or ELPs are polymeric or oligomeric repeats of the pentapeptide VPGX2G, wherein “X2” is an amino acid selected from the group consisting of arginine, histidine, lysine, aspartic acid, glutamic acid, serine, threonine, asparagine, glutamine, cysteine, glycine, alanine, valine, isoleucine, leucine, methionine, phenylalanine, tyrosine, or tryptophan. In some embodiments, “X2” is leucine. In some embodiments, “X2” is asparagine.

[0343] In some embodiments, “X2” is valine.

[0344] In some embodiments, the elastin or ELP is defined by the peptide sequence GVGVPGVGVPGLGVPGVGVPGVG (SEQ ID NO: 22).

[0345] In some embodiments, the elastin or ELP is defined by the sequence VPGVGVPGVGVPGVGVPGVGVPGVGVPGVG (SEQ ID NO: 23).

[0346] In some embodiments, the elastin or elastin-like polypeptide (ELP) block forms β-sheet- rich domains.

[0347] In some embodiments, the elastin or ELP block comprises amorphous domains. In some embodiments, the elastin or ELP block comprises crystalline domains. In some embodiments, the elastin or ELP block comprises both crystalline and amorphous domains.

[0348] In some embodiments, the elastin or ELP blocks are stimuli-responsive. In some embodiments, the ELP blocks are thermoresponsive. In some embodiments, the ELP component may be responsive to changes in pH. In some embodiments, the ELP component may beresponsive over a range of temperatures. In some embodiments, the ELP component may be response to salts.

[0349] In some embodiments, “s” is an integer from 0 to about 220.

[0350] In some embodiments, “s” is 0.

[0351] In some embodiments, “s” is about 1.

[0352] In some embodiments, “s” is about 2.

[0353] In some embodiments, “s” is about 3.

[0354] In some embodiments, “s” is about 4.

[0355] In some embodiments, “s” is about 5.

[0356] In some embodiments, “s” is about 6.

[0357] In some embodiments, “s” is about 7.

[0358] In some embodiments, “s” is about 8.

[0359] In some embodiments, “s” is about 9.

[0360] In some embodiments, “s” is about 10.

[0361] In some embodiments, “s” is about 20.

[0362] In some embodiments, “s” is about 30.

[0363] In some embodiments, “s” is about 40.

[0364] In some embodiments, “s” is about 50.

[0365] In some embodiments, “s” is about 100.

[0366] In some embodiments, the keratin or keratin associated fusion protein / peptide disclosed herein comprise a silk or silk-like polypeptide (SLP) block (“D”). In some embodiments, silk-like polypeptide (SLP) refers to a peptide, including a synthetic peptide having a similar secondary structure, tertiary structure, or amino acid sequence, or a combination of two or more thereof, to a wild-type silk protein (e.g., SEQ ID NO: 56), or a fragment of a wild-type silk protein. In some embodiments, a fragment includes a sequence having at least 4, 5, 6, 7, 8, 9, or 10 amino acids 100% identical to a sequence of wild-type silk protein. The wild-type silk protein may be fibroin. Non-limiting example silk and SLPs include SEQ ID NOS: 24-32, 92, and 56.

[0367] SLPs may comprise polymeric or oligomeric repeating peptide sequences of a silk protein. In an example embodiment, a silk or SLP comprises SEQ ID NO: 24 GAGAGS, or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 24. In an example embodiment, a silk or SLP comprises SEQ ID NO: 24, or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 24. The silk or SLP may comprise 1 to 10 sequences having SEQ ID NO: 24, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 24. The 1 to 10 sequences may be connected, or may be separated by one or more amino acids.

[0368] In some embodiments, a silk or SLP comprises a polymeric or oligomeric repeating peptide sequence of a silk peptide, where each polymeric or oligomeric repeating peptide sequence comprises or has 6 amino acid residues.

[0369] In some embodiments, a silk or SLP comprises a polymeric or oligomeric repeating peptide sequence of a silk peptide, where each polymeric or oligomeric repeating peptide sequence comprises or has 7 amino acid residues.

[0370] In some embodiments, a silk or SLP comprises a polymeric or oligomeric repeating peptide sequence of a silk peptide, where each polymeric or oligomeric repeating peptide sequence comprises or has 8 amino acid residues.

[0371] Non-limiting example repeating peptide sequences include polytetra-, polypenta-, polyhexa-, polyhepta-, polyocta, and polynonapeptides, including but not limited to, GAGAGS (SEQ ID NO: 24), GAGSGA (SEQ ID NO: 25), GAGAGY (SEQ ID NO: 26), GAGYGA (SEQ ID NO: 27), GAGAGA (SEQ ID NO: 28), GAGAGV (SEQ ID NO: 29), GAGVGA (SEQ ID NO: 30), and GAGAGVGY (SEQ ID NO: 31), and combinations of two or more thereof.

[0372] In some embodiments, the silk or SLP are polymeric or oligomeric repeats of the pentapeptide GAGAGS (SEQ ID NO: 24).

[0373] In some embodiments, the silk or SLP is defined by the peptide sequence GAGAGSGAGAGSGAGAGSGAGAGSGAGAGS (SEQ ID NO: 32).

[0374] In some embodiments, the silk or silk-like (SLP) block forms β-sheet-rich domains.

[0375] In some embodiments, the silk or SLP block comprises crystalline domains. In some embodiments, the silk or SLP block comprises amorphous domains. In some embodiments, the silk or SLP block comprises both amorphous and crystalline domains.

[0376] In some embodiments, “q” is an integer from 0 to 100.

[0377] In some embodiments, “q” is 0.

[0378] In some embodiments, “q” is about 1.

[0379] In some embodiments, “q” is about 2.

[0380] In some embodiments, “q” is about 3.

[0381] In some embodiments, “q” is about 4.

[0382] In some embodiments, “q” is about 5.

[0383] In some embodiments, “q” is about 6.

[0384] In some embodiments, “q” is about 7.

[0385] In some embodiments, “q” is about 8.

[0386] In some embodiments, “q” is about 9.

[0387] In some embodiments, “q” is about 10.

[0388] In some embodiments, “q” is about 20.

[0389] In some embodiments, “q” is about 30.

[0390] In some embodiments, “q” is about 40.

[0391] In some embodiments, “q” is about 50.

[0392] In some embodiments, “q” is about 100.

[0393] In some embodiments, the keratin or keratin associated fusion protein / peptide disclosed herein comprise a collagen or collagen-like polypeptide (CLP) block (“E”). In some embodiments, collagen-like polypeptide (CLP) refers to a peptide, including a synthetic peptide having a similar secondary structure, tertiary structure, or amino acid sequence, or a combination of two or more thereof, to a wild-type collagen protein (e.g., SEQ ID NO: 59), or a fragment of a wild-type collagen protein. In some embodiments, a fragment includes a sequence having at least 3, 4, 5, 6, 7, 8, 9, or 10 amino acids 100% identical to a sequence of wild-type collagen protein. Non-limiting example collagen and CLPs include SEQ ID NOS: 33, 58, 59, 93, 94, 95, and 57, as well as fragments having amino acids “GTP” and / or “GLQ”.

[0394] CLPs may comprise polymeric or oligomeric repeating peptide sequence of a collagen peptide. In an example embodiment, a collagen or CLP comprises the sequence GTP. The collagen or CLP may comprise 1 to 10 sequences comprising the sequence GTP. The 1 to 10 sequences may be connected or may be separated by one or more amino acids. The 1 to 10 sequences may be, for example, 2 or 3. For example, collagen or CLP may comprise GPTGPT (SEQ ID NO: 57) or GPTGPTGPAGPRGLQGLQGLQGERGEQGPT (SEQ ID NO: 33). In an example embodiment, collagen or CLP comprises the sequence GLQ. The collagen or CLP may comprise 1 to 10 sequences comprising the sequence GLQ. The 1 to 10 sequences may be, for example, 2 or 3. The 1 to 10 sequences may be connected or may be separated by one or more amino acids. For example, collagen or CLP may comprise GLQGLQ (SEQ ID NO: 58) or GPTGPTGPAGPRGLQGLQGLQGERGEQGPT (SEQ ID NO: 33).

[0395] In some embodiments, each polymeric or oligomeric repeating peptide sequences of the collagen or collagen-like polypeptide (CLP) block comprise or have 3 amino acid residues. As non- limiting examples, the 3 amino acid residues may include GTP, GLQ, and GX1H.

[0396] In some embodiments, the repeating peptide sequence includes polytetra-, polypenta-, polyhexa-, polyhepta-, polyocta-, and polynonapeptides, including but not limited to, GX1H.

[0397] In some embodiments, “X1” comprises proline, leucine, isoleucine, glutamic acid, aspartic acid, glutamine, lysine, alanine, arginine and threonine; and where “H” comprises an amino acid selected from the group consisting of glycine, alanine, lysine, proline, methionine, glutamine, arginine, threonine, valine, glutamic acid, aspartic acid, or asparagine.

[0398] In some embodiments, the collagen or CLP is defined by the peptide sequence GPTGPTGPAGPRGLQGLQGLQGERGEQGPT (SEQ ID NO: 33).

[0399] In some embodiments, “r” is an integer from 0 to about 200.

[0400] In some embodiments, “r” is 0.

[0401] In some embodiments, “r” is about 1.

[0402] In some embodiments, “r” is about 2.

[0403] In some embodiments, “r” is about 3.

[0404] In some embodiments, “r” is about 4.

[0405] In some embodiments, “r” is about 4.

[0406] In some embodiments, “r” is about 5.

[0407] In some embodiments, “r” is about 6.

[0408] In some embodiments, “r” is about 7.

[0409] In some embodiments, “r” is about 8.

[0410] In some embodiments, “r” is about 9.

[0411] In some embodiments, “r” is about 10.

[0412] In some embodiments, “r” is about 20.

[0413] In some embodiments, “r” is about 30.

[0414] In some embodiments, “r” is about 40.

[0415] In some embodiments, “r” is about 50.

[0416] In some embodiments, “r” is about 100.

[0417] In some embodiments, the keratin or keratin associated fusion protein / peptide disclosed herein comprise a resilin or resilin-like polypeptide (RLP) block (“G”). In some embodiments, resilin-like polypeptide (RLP) refers to a peptide, including a synthetic peptide having a similar secondary structure, tertiary structure, or amino acid sequence, or a combination of two or more thereof, to a wild-type resilin protein (e.g., SEQ ID NO: 60), or a fragment of a wild-type resilin protein. In some embodiments, a fragment includes a sequence having at least 4, 5, 6, 7, 8, 9, or 10 amino acids 100% identical to a sequence of wild-type silk protein. Non-limiting example resilin and RLPs include SEQ ID NOS: 34-35, 96, and 60.

[0418] RLPs comprise polymeric or oligomeric repeating peptide sequence of a resilin protein. In example embodiments, the polymeric or oligomeric repeating peptide sequence is a fragment of a wild-type resilin peptide having about 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 amino acids.

[0419] In some embodiments, each polymeric or oligomeric repeating peptide sequences of the resilin or resilin-like polypeptide (RLP) components comprise or have 11 amino acid residues.

[0420] In some embodiments, each polymeric or oligomeric repeating peptide sequences of the resilin or resilin-like polypeptide (RLP) components comprise or have 12 amino acid residues.

[0421] In some embodiments, each polymeric or oligomeric repeating peptide sequences of the resilin or resilin-like polypeptide (RLP) components comprise or have 13 amino acid residues.

[0422] In some embodiments, each polymeric or oligomeric repeating peptide sequences of the resilin or resilin-like polypeptide (RLP) components comprise or have 14 amino acid residues.

[0423] In some embodiments, each polymeric or oligomeric repeating peptide sequences of the resilin or resilin-like polypeptide (RLP) components comprise or have 15 amino acid residues.

[0424] In some embodiments, the repeating peptide sequence includes polytetra-, polypenta-, polyhexa-, polyhepta-, polyocta, and polynonapeptides, including but not limited to, GGRPSDSYGAPGGGN (SEQ ID NO: 34), GAPAQTPSSQY (SEQ ID NO: 35), AQTPSSQYGAP (SEQ ID NO: 96), and combinations thereof.

[0425] In some embodiments, the resilin or RLP is defined by the peptide sequence GGRPSDSYGAPGGGN (SEQ ID NO: 34).

[0426] In some embodiments, “t” is an integer from 0 to about 80.

[0427] In some embodiments, “t” is 0.

[0428] In some embodiments, “t” is about 1.

[0429] In some embodiments, “t” is about 2.

[0430] In some embodiments, “t” is about 3.

[0431] In some embodiments, “t” is about 4.

[0432] In some embodiments, “t” is about 5.

[0433] In some embodiments, “t” is about 6.

[0434] In some embodiments, “t” is about 7.

[0435] In some embodiments, “t” is about 8.

[0436] In some embodiments, “t” is about 9.

[0437] In some embodiments, “t” is about 10.

[0438] In some embodiments, “t” is about 20.

[0439] In some embodiments, “t” is about 30.

[0440] In some embodiments, “t” is about 40.

[0441] In some embodiments, “t” is about 50.

[0442] In some embodiments, “t” is about 80.

[0443] In some embodiments,”"t” is about 100.

[0444] In some embodiments, the keratin or keratin associated component disclosed herein comprise an abductin or abductin-like polypeptide (ALP) block (“H”). In some embodiments, abductin-like polypeptide (ALP) refers to a peptide, including a synthetic peptide comprising an amino acid sequence having a similar secondary structure, tertiary structure, or amino acid sequence, or a combination of two or more thereof, to a wild-type abductin protein (e.g., SEQ ID NO: 61), or a fragment of a wild-type abductin protein. In some embodiments, a fragment includes a sequence having at least 4, 5, 6, 7, 8, 9, or 10 amino acids 100% identical to a sequence of wild-type abductin protein. Non-limiting example abductin and ALPs include SEQ ID NOS: 36- 42, 61, and 108. ALPs comprise polymeric or oligomeric repeating peptide sequence of an abductin protein.

[0445] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 4 amino acid residues of an abductin protein.

[0446] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 5 amino acid residues of an abductin protein.

[0447] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 6 amino acid residues of an abductin protein.

[0448] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 7 amino acid residues of an abductin protein.

[0449] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 8 amino acid residues of an abductin protein.

[0450] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 9 amino acid residues of an abductin protein.

[0451] In some embodiments, each polymeric or oligomeric repeating peptide sequence comprises or has 10 amino acid residues of an abductin protein.

[0452] In some embodiments, the repeating peptide sequence includes polytetra-, polypenta-, polyhexa-, polyhepta-, polyocta, and polynonapeptides, including but not limited to,GGFGGMGGGS (SEQ ID NO: 36), MGGG (SEQ ID NO: 37), FGGMG (SEQ ID NO: 38), FGGMGGG (SEQ ID NO: 39), GGFGGMGGG (SEQ ID NO: 40), FGGMGGGNAG (SEQ ID NO: 41), MNAYICLAACLIAAVSAAGYGGGAGSMGGTGGMGGGMNAGGFGGMGGMGGGKGGFGGIGGFGGGM GGGPGGFGGMGGFGGMAAKGGFGGMGSGMGGFGGMGGGNAGFGGMGGGNAGFGGMGGQGGFG GKGY (SEQ ID NO: 61), GGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSY GAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGN GGRPSDSYGAPGGGNGQGQGQGQGQGQGQGQGQGQGGVCGPSPPCITTGQGQGQGQGQGQGQGQ GQGQVPAVGVPAVGVPAVGVPAVGVPAVGVPAVGVPAVGVPAVGVPAVGVPAVGGQGQGQGQGQG QGQGQGQGQGGVCGPSPPCITTGQGQGQGQGQGQGQGQGQGQGGRPSDSYGAPGGGNGGRPSDSY GAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGN GGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGNGGRPSDSYGAPGGGN (SEQ ID NO: 108), and combinations thereof.

[0453] In some embodiments, the abductin or ALP is defined by the peptide sequence GGFGGMGGGSGGFGGMGGGSGGFGGMGGGS (SEQ ID NO: 42). In an example embodiment, abductin or ALP comprises SEQ ID NO: 36, or a sequence having no more than 1 amino acid substitution as compared to SEQ ID NO: 36. The abductin or ALP may comprise 1 to 10 sequences having SEQ ID NO: 36, or 1 to 10 sequences each independently having no more than 1 amino acid substitution as compared to SEQ ID NO: 36. The 1 to 10 sequences may be connected, e.g., SEQ ID NO: 42, or may be separated by one or more amino acids.

[0454] In some embodiments, “u” is an integer from 0 to about 100.

[0455] In some embodiments, “u” is from 0 to about 70.

[0456] In some embodiments, “u” is 0.

[0457] In some embodiments, “u” is about 1.

[0458] In some embodiments, “u” is about 2.

[0459] In some embodiments, “u” is about 3.

[0460] In some embodiments, “u” is about 4.

[0461] In some embodiments, “u” is about 5.

[0462] In some embodiments, “u” is about 6.

[0463] In some embodiments, “u” is about 7.

[0464] In some embodiments, “u” is about 8.

[0465] In some embodiments, “u” is about 9.

[0466] In some embodiments, “u” is about 10.

[0467] In some embodiments, “u” is about 20.

[0468] In some embodiments, “u” is about 30.

[0469] In some embodiments, “u” is about 40.

[0470] In some embodiments, “u” is about 50.

[0471] In some embodiments, “u” is about 70.

[0472] In some embodiments, “o” is an integer from 0 to 30.

[0473] In some embodiments, “o” is 0.

[0474] In some embodiments, “o” is about 1.

[0475] In some embodiments, “o” is about 2.

[0476] In some embodiments, “o” is about 3.

[0477] In some embodiments, “o” is about 4.

[0478] In some embodiments, “o” is about 5.

[0479] In some embodiments, “o” is about 6.

[0480] In some embodiments, “o” is about 7.

[0481] In some embodiments, “o” is about 8.

[0482] In some embodiments, “o” is about 9.

[0483] In some embodiments, “o” is about 10.

[0484] In some embodiments, “o” is about 15.

[0485] In some embodiments, “o” is about 20.

[0486] In some embodiments, “o” is about 25.

[0487] In some embodiments, “o” is about 30.

[0488] In some embodiments, “p” is an integer from 1 to 30.

[0489] In some embodiments, “p” is about 1.

[0490] In some embodiments, “p” is about 2.

[0491] In some embodiments, “p” is about 3.

[0492] In some embodiments, “p” is about 4.

[0493] In some embodiments, “p” is about 5.

[0494] In some embodiments, “p” is about 6.

[0495] In some embodiments, “p” is about 7.

[0496] In some embodiments, “p” is about 8.

[0497] In some embodiments, “p” is about 9.

[0498] In some embodiments, “p” is about 10.

[0499] In some embodiments, “p” is about 15.

[0500] In some embodiments, “p” is about 20.

[0501] In some embodiments, “p” is about 25.

[0502] In some embodiments, “p” is about 30.

[0503] some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 1 kDa to about 144 kDa.

[0504] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 1 kDa to about 5 kDa.

[0505] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 5 kDa to about 10 kDa.

[0506] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 6 kDa to about 17 kDa.

[0507] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 10 kDa to about 15 kDa.

[0508] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 14 kDa to about 30 kDa.

[0509] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from between about 15 kDa to about 20 kDa.

[0510] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 17 kDa to about 39 kDa.

[0511] In some embodiments, the keratin or keratin associated fusion protein / peptide may have an average molecular weight from about 20 kDa to about 25 kDa.

[0512] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 25 kDa to about 30 kDa.

[0513] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 30 kDa to about 35 kDa.

[0514] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 35 kDa to about 40 kDa.

[0515] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 39 kDa to about 54 kDa.

[0516] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 39 kDa to about 80 kDa.

[0517] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 40 kDa to about 45 kDa.

[0518] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 45 kDa to about 50 kDa.

[0519] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 50 kDa to about 55 kDa.

[0520] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 55 kDa to about 60 kDa.

[0521] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 60 kDa to about 100 kDa.

[0522] In some embodiments, the keratin or keratin associated fusion protein / peptide has an average molecular weight ranging from about 80 kDa to about 144 kDa.

[0523] In another or additional aspect, the present disclosure relates to compositions comprising the fusion proteins / peptides disclosed herein.

[0524] In some embodiments, the composition is used for improving one or more properties of the hair, nails, or skin, or a combination thereof. For example, the composition improves the elasticity, hydration, or texture of skin, or provides UV protection to skin, or a combination of two or more thereof.

[0525] In some embodiments, the composition improves the mechanical properties, color, texture, shape, or hydration of hair, or provides better thermal protection to hair, or a combination of two or more thereof.

[0526] In some embodiments, the composition improves the mechanical properties or antimicrobial properties of nails or provides better UV protection to nails, or a combination of two or more thereof.

[0527] In some embodiments, the composition disclosed herein further comprise at least one additive selected from the list: water, preservatives, antioxidants, chelating agents, sunscreen agents, vitamins, dyes, hair coloring agents, surfactants, detergents, emulsifiers, opacifying agents, volatiles, propellants, liquid vehicles, carriers, salts, pH adjusting agents, neutralizing agents, buffers, hair conditioning agents, anti-static agents, anti-frizz agents, anti-dandruff agents, natural extracts, humectants, fragrances, perfumes, oils, emollients, lubricants, butters, penetrants, thickeners, viscosity modifiers, polymers, resins, hair fixatives, film formers, absorbents, and combinations thereof, in order to achieve a close approximation to commercially available product forms.

[0528] In some embodiments, the composition disclosed herein is formulated as a soap, shampoo, conditioner, spray, gel, liquid with low to moderate viscosity, lotion, milk, mousse, or cream, comprising a fusion protein / peptide of the present disclosure.

[0529] In some embodiments, the additives are included or excluded from the composition depending on the form of use.

[0530] A further or additional aspect of the present disclosure relates to method of obtaining the fusion protein / peptide disclosed herein.

[0531] In some embodiments, the method of obtaining the fusion proteins of the present disclosure comprises the steps of:a) inoculating a liquid medium with a microorganism containing a gene for the expression of the desired fusion protein / peptide; b) allowing the microorganism to multiply during a certain incubation period and inducing the expression of the desired fusion protein / peptide under influence of a promoter; c) retrieving the desired fusion protein / peptide from the obtained microorganisms by purifying the protein from endogenous contaminants.

[0532] In some embodiments, the method of obtaining the fusion protein / peptide comprises the step of inoculating a liquid medium with a microorganism, in particular Escherichia coli strains, containing a gene for the expression of the desired fusion protein / peptide.

[0533] In some embodiments, the method of obtaining the fusion protein comprises the step of retrieving the desired fusion protein / peptide from microorganisms by purifying the fusion protein / peptide from endogenous contaminants.

[0534] In some aspects, provided herein is a method of providing a fusion peptide as described elsewhere. Definit ions

[0535] Unless defined otherwise, all terms of art, notations and other technical and scientific terms or terminology used herein are intended to have the same meaning as is commonly understood by one of ordinary skill in the art to which the claimed subject matter pertains. In some cases, terms with commonly understood meanings are defined herein for clarity and / or for ready reference, and the inclusion of such definitions herein should not necessarily be construed to represent a substantial difference over what is generally understood in the art.

[0536] Throughout this disclosure, various embodiments may be presented in a range format. It should be understood that the description in range format is merely for convenience and brevity and should not be construed as an inflexible limitation on the scope of the disclosure. Accordingly, the description of a range should be considered to have specifically disclosed all the possible subranges as well as individual numerical values within that range. For example, description of a range such as from 1 to 6 should be considered to have specifically disclosed subranges such as from 1 to 3, from 1 to 4, from 1 to 5, from 2 to 4, from 2 to 6, from 3 to 6 etc.,as well as individual numbers within that range, for example, 1, 2, 3, 4, 5, and 6. This applies regardless of the breadth of the range.

[0537] As used in the specification and claims, the singular forms “a”, “an” and “the” include plural references unless the context clearly dictates otherwise. For example, the term “a sample” includes a plurality of samples, including mixtures thereof.

[0538] Whenever the term “at least,” “greater than,” or “greater than or equal to” precedes the first numerical value in a series of two or more numerical values, the term “at least,” “greater than” or “greater than or equal to” applies to each of the numerical values in that series of numerical values. For example, greater than or equal to 1, 2, or 3 is equivalent to greater than or equal to 1, greater than or equal to 2, or greater than or equal to 3.

[0539] The terms “determining,” “measuring,” “evaluating,” “assessing,” “assaying,” and “analyzing” are often used interchangeably herein to refer to forms of measurement. The terms include determining if an element is present or not (for example, detection). These terms can include quantitative, qualitative or quantitative and qualitative determinations. Assessing can be relative or absolute. “Detecting the presence of” can include determining the amount of something present in addition to determining whether it is present or absent depending on the context.

[0540] As used herein, the term “about” a number refers to that number plus or minus 10% of that number. The term “about” a range refers to that range minus 10% of its lowest value and plus 10% of its greatest value.

[0541] As used herein, the terms “pharmaceutically acceptable” and “cosmetically acceptable” are used interchangeably and refer to those compounds, materials, compositions, and / or dosage forms which are, within the scope of sound medical judgment, suitable for use in contact with the tissues of human beings and animals without excessive toxicity, irritation, allergic response, or other problems or complications commensurate with a reasonable benefit / risk ratio. More specifically, pharmaceutically acceptable refers to a material, compound, or composition which is suitable for use in contact with the skin, scalp, or hair. Pharmaceutically acceptable materials are known to those of ordinary skill in the art.

[0542] As used herein, the terms “treatment” or “treating” are used in reference to a pharmaceutical or other intervention regimen for obtaining beneficial or desired results in the recipient. Beneficial or desired results include but are not limited to a therapeutic benefit and / ora prophylactic benefit. A therapeutic benefit may refer to eradication or amelioration of symptoms or of an underlying disorder being treated. Also, a therapeutic benefit can be achieved with the eradication or amelioration of one or more of the physiological symptoms associated with the underlying disorder such that an improvement is observed in the subject, notwithstanding that the subject may still be afflicted with the underlying disorder. A prophylactic effect includes delaying, preventing, or eliminating the appearance of a disease or condition, delaying or eliminating the onset of symptoms of a disease or condition, slowing, halting, or reversing the progression of a disease or condition, or any combination thereof. For prophylactic benefit, a subject at risk of developing a particular disease, or to a subject reporting one or more of the physiological symptoms of a disease may undergo treatment, even though a diagnosis of this disease may not have been made.

[0543] As used herein, the terms “hair care” or “hair treatment” are used in reference to a composition for improving a characteristic of hair. The characteristic includes, but is not limited to, strength, elasticity, shine, smoothness, volume, or a combination thereof. “Hair care” or “hair treatment” may be used to describe a process of providing a composition to hair previously treated or damaged, such as with bleach or heat.

[0544] Whenever the term “at least,” “greater than,” or “greater than or equal to” precedes the first numerical value in a series of two or more numerical values, the term “at least,” “greater than” or “greater than or equal to” applies to each of the numerical values in that series of numerical values. For example, greater than or equal to 1, 2, or 3 is equivalent to greater than or equal to 1, greater than or equal to 2, or greater than or equal to 3.

[0545] Whenever the term “no more than,” “less than,” or “less than or equal to” precedes the first numerical value in a series of two or more numerical values, the term “no more than,” “less than,” or “less than or equal to” applies to each of the numerical values in that series of numerical values. For example, less than or equal to 3, 2, or 1 is equivalent to less than or equal to 3, less than or equal to 2, or less than or equal to 1.

[0546] The expressions “at least one of A and B” and “at least one of A or B” may be construed to mean at least A, at least B, or at least A and B (i.e., a set comprising A and B, which set may include one or more additional elements). The term “A and / or B” may be construed to mean only A, only B, or both A and B.

[0547] The expressions “at least about A, B, and C” and “at least about A, B, or C” may be construed to mean at least about A, at least about B, or at least about C. The expressions “at most about A, B, and C” and “at most about A, B, or C” may be construed to mean at most about A, at most about B, or at most about C.

[0548] The expression “between about A and B, C and D, and E and F” may be construed to mean between about A and about B, between about C and about D, and between about E and about F. The expression “between about A and B, C and D, or E and F” may be construed to mean between about A and about B, between about C and about D, or between about E and about F.

[0549] The expression “about A to B and C to D” may be construed to mean between about A and about B and between about C and about D. The expression “about A to B or C to D” may be construed to mean between about A and about B or between about C and about D.

[0550] The term “comprising” whenever used in this document is intended to indicate the presence of stated features, integers, steps, components, but not to preclude the presence or addition of one or more other features, integers, steps, components or groups thereof. Examples

[0551] This disclosure may be further understood by reference to the following examples. This disclosure is not limited in scope by the embodiments in the examples, which are intended as illustrations of single aspects of this disclosure only. Any methods that are functionally equivalent are within the scope of this disclosure. Various modifications of this disclosure in addition to those described herein will become apparent to those skilled in the art from the foregoing description and accompanying figures. Such modifications fall within the scope of the appended claims. Vector Construction

[0552] A target nucleic acid sequence encoding for the fusion protein is inserted into an appropriate expression vector, phage or directly integrated in the microorganism genome or derivatives thereof, to yield a polynucleotide composition. The target nucleic acid sequence encodes for the fusion protein / peptide of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NOS: 44-47, or 200-552, or any combination thereof, or any nucleic acid sequence encoding for a fusion protein comprising at least 60%homology to any one of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NOS: 44-47, or 200-552. The target nucleic acid sequence comprises at least one keratin or keratin associated peptide component of SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 66, or SEQ ID NO: 67, or SEQ ID NOS: 70-81, and at least one of a ELP component (SEQ ID NO: 11–23, 49-55, 82-91), a SLP component (SEQ ID NO: 24–32, 56, 92), a CLP component (SEQ ID NO: 33, 57-59, 93-95), a RLP component (SEQ ID NO: 34–35, 60, 96), an ALP component (SEQ ID NO: 36–42, 61), or any combination thereof.

[0553] The expression vector comprises a promoter and the target nucleic acid sequence encoding for the target fusion protein / peptide. The vector optionally comprises polynucleotides encoding for: an antibiotic resistance (e.g., ampR gene, camR gene, kmR gene, tetR gene, and the like), an affinity tag (e.g., a C-terminal tag or an N-terminal tag), an expression reporter, cleavable linker, a terminator (e.g., a T7 terminator, and the like), a ribozyme, or any combination thereof.

[0554] A promoter is included in the vector backbone and is upstream of the start codon. The promoter is a T7 promoter, lac, T7lac, araBAD, Sp6, trp, or any combination thereof. The promoter is an inducible or constitutive promoter that induces overexpression continuously or in the presence of an inducer, respectively. For example, and not by limitation, a lac promoter is incorporated into the vector, and overexpression is induced in the presence of ispropyl-β-D- thiogalactoside (IPTG).

[0555] The vector comprises an affinity tag, which is either a C-terminal or an N-terminal affinity tag. The affinity tag comprises a poly-His tag (3xHis, 4xHis, 5xHis, 6xHis, 7xHis, 8xHis, or 9xHis), a GST tag, a FLAG tag, a MBP tag, a streptavidin (Strep) tag or a derivative of a streptavidin tag (e.g., Strep-tag II, Twin-Strep), a calmodulin tag, a chitin-binding tag, or any combination or derivative thereof. If using an N-terminal affinity tag, a linker sequence is placed between the polynucleotide encoding for the target fusion protein and the N-terminal affinity tag. If using a C-terminal affinity tag, a cleavable linker sequence is placed between the 3’ end of the nucleic acid sequence encoding for the C-terminal tag and the 5’ start codon of the polynucleotide encoding for the target fusion protein. The linker sequence codes for a cleavable linker motif that is a recognized substrate of a protease that selectively cleaves the cleavable linker and not the target fusion protein. For example, a cleavable linker sequence comprising the sequence IEGR is a known substrate of Factor Xa. The nucleic acid sequence encoding for IEGR-(His)6 is introduced to allow for expression of the affinity tag, 6xHis, and a cleavable linker sequence IEGRto enable removal of the affinity tag post-purification. A spacer sequence is optionally placed between the cleavable linker sequence and the affinity tag sequence.

[0556] Exemplary vector maps of expression vectors used are presented in FIGS.1 and 2. In FIG. 1, the promoter is upstream of an N-terminal affinity tag sequence, followed by the linker sequence, and the target nucleic acid sequence. The expression vector contains an antibiotic resistance gene like ampicillin resistance to the host bacterium via the AmpR gene and AmpR promoter. In FIG. 2, a promoter is upstream of the target nucleic acid sequence, the linker sequence, and the C-terminal affinity tag sequence. The expression vector contains an antibiotic resistance like ampicillin resistance to the host bacterium via the AmpR gene and AmpR promoter.

[0557] The target nucleic acid sequence encoding for fusion protein is inserted into the vector backbone using traditional assembly or Gibson Assembly via PCR. For traditional assembly (TA), primers are designed to include the restriction sites and the target nucleic acid sequence to be inserted into the vector backbone. For Gibson Assembly of nucleic acid fragments, Gibson primers are designed to exhibit complementarity to (1) a region of the vector backbone and the nucleic acid sequence encoding for the target fusion protein / peptide, or (2) two different regions of the target nucleic acid sequence. For Gibson Assembly cloning, the Gibson Assembly® cloning kit (New England Biolabs, Inc.) is used. Transformation

[0558] After the target nucleic acid sequences are cloned into the vector, insertion of the target nucleic acid sequences is verified by a DNA gel (e.g., an agarose gel). Once confirmed, the vector is transformed into microorganism cells via heat shock transformation or electroporation. In an example, E. coli strain is chosen from the group comprising K-12, B, or derivatives thereof. In another example, the vector with the target sequence is inserted into Komagataella phaffii by electroporation and the gene is integrated into the genome by homologous recombination. An K. phaffii strain is chosen from the group comprising GS115, X-33 or derivatives thereof.

[0559] Heat Shock Transformation. A stock solution of competent cells is thawed on ice, are mixed with a ligation mixture (e.g., a T4 ligase), and further mixed with an appropriate volume of the vector having the polynucleotide sequence encoding for the target fusion protein / peptide. The mixture is gently mixed then transferred to a hot water bath or a preheated block at a temperature of about 42 °C for about 30 seconds. The heated mixture is immediately cooled inice and allowed to rest for about 2 minutes. The cooled mixture is mixed with LB medium. The cooled mixture is incubated at 37 °C for about 30 to about 60 minutes before plating. An aliquot of the mixture is plated and incubated at 37 °C overnight.

[0560] Electroporation. Round-bottom culture tubes are allowed to reach room temperature. Recovery media is preheated in a 37 °C water bath. Electroporation cuvettes are cooled over ice. A source of competent E. coli cells is chilled over ice and mixed with the expression vector comprising the target nucleic acid sequence. A solution comprising a 25:1 ratio of competent cells:vector is pipetted into a microcentrifuge tube and gently mixed. The microcentrifuge tube containing the cell / DNA mixture is electroporated on an electroporator (Gene-Pulser, Bio-Rad) at 2.1 kV, 100 Ω, and 25 μF with a time constant of 2.6 milliseconds. Warmed recovery media at is added to the electroporated cell / DNA mixture and shaken vigorously for about 1 hour at 37 °C. Cells are diluted, plated, and incubated overnight at 37 °C.

[0561] Transformation Success. Transformation success was determined by obtaining aliquots of the bacterial cultures (as described below), lysing the cultures, and extracting the plasmids (e.g., using a DNA Extraction Kit (QIAamp DNA kit, QIAGEN®)), and comparing the relative weights of the plasmids from the cultures and empty vector on a DNA gel (e.g., an agarose gel). The extracted DNA from the cultures exhibit a larger weight than the empty vector. If traditional assembly is used to insert the target nucleic acid sequence, a digest using the corresponding restriction enzymes is performed prior to running the DNA gel. Cell Culturing

[0562] Colonies of are inoculated into growth media (e.g., LB). The inoculated media is mixed with / without a selective marker. The culture is grown at 37 °C for about several hours on a shaker. An aliquot is obtained to check for growth stage by measuring the absorbance (or optical density) of the culture at 600 nm. When the optical density at 600 nm (OD600) of the culture corresponds to exponential phase or log phases, the culture is removed from the shaker.

[0563] Small Scale. About 25 mL to about 100 mL of the culture is added to several sterilized baffled flasks with media, and the cultures are allowed to grow overnight at 37 °C on the shaker. When the OD600 corresponds to the lag phase, IPTG (or other promoter inducer) is added to the culture, which is allowed to shake at 37 °C until OD600 corresponds to exponential phase or log- phase. Afterwards, the cells are pelleted by centrifuging at about 1,800 x g at 4 °C for about 30 minutes. The supernatant is discarded, and the pellet is stored at -20 °C for later use.

[0564] Large Scale. A bioreactor (e.g., BioFlo®, Eppendorf) is equipped with a stirring apparatus (e.g., baffled stirrer), sterilized, and filled at least half-way with fresh medium. The medium optionally includes anti-foam. The medium is agitated from about 300 rpm to about 1200 rpm. The bioreactor is maintained at an internal temperature of about 37 °C. The agitation rate may be automatically adjusted based on other parameters, e.g., carbon dioxide (CO2) content. A quorum of transformed cells is slowly introduced (e.g., via a peristaltic pump) into the bioreactor. The air composition within the bioreactor is monitored. The air composition in the headspace within the bioreactor is monitored, such as monitoring for the amount of CO2. The amount of dissolved oxygen (DO) is monitored and maintained at about 35% DO. The pH of the culture is also monitored. A pH maintenance feed is in fluid communication with the bioreactor, and the pH maintenance feed comprises an acidic buffer feed and a basic buffer feed. The pH of the culture in the bioreactor is maintained between about 7.2 and about 7.6. A food feed is in fluid communication with the bioreactor and comprises glucose (e.g., 20 g / L). The food feed is slowly introduced into the bioreactor. An automated program is used to introduce glucose when the DO content grows above a predetermined threshold. Aliquots of the culture are obtained, and OD600is measured to monitor the growth-phase of the culture. When OD600corresponds to the lag phase or late-lag phase, an appropriate amount of IPTG or other inducer is added to induce expression. A reporter protein, such as green fluorescent protein (GFP), may be expressed, and a green fluorescence tint of the culture is used to approximate expression of the target fusion protein. When OD600corresponds to the exponential phase or log phase, the culture is pumped out of the bioreactor and centrifuged at about 1,800 x g at 4 °C for about 20 to about 30 minutes to pellet the cultures. The supernatant is discarded, and the pellets are stored at -30 °C. Protein Purification

[0565] The cell pellets are reconstituted in buffer (e.g., PBS buffer, pH 7.4). An appropriate amount of buffer is added to the pellets to yield a suspension. The pellets and buffer are mixed until homogenous. A vortexer or homogenizer is used. Once homogenous, the suspension is lysed by passing through a French press, ultrasonicating, high pressure homogenization, mixing with glass beads, or through several freeze / thaw cycles. A protease inhibitor is added to the suspension of lysed cells. The lysed cells are centrifuged at least at 2,000 x g at 4 °C for about 5 to about 30 minutes. The supernatant is collected, and the pellet is discarded. The supernatant is dialyzed purified via size exclusion chromatography, affinity chromatography, or directly to drying. The pure fractions are dialyzed against buffer or water or diafiltrated.Chromatography

[0566] Size Exclusion. The concentrated supernatant is passed through a size exclusion column, which is chosen based on the desired molecular weight resolution. For example, and not by limitation, when the fusion protein exhibits a molecular weight of about 35 kDa, a size exclusion resin with a resolution for proteins between 5 kDa and 250 kDa is used (e.g., HiPrep Sephacryl S- 200 HR, Cytiva LifeSciences).

[0567] Affinity Chromatography. The affinity chromatography medium is chosen based on the incorporated affinity tag in the expressed fusion protein. When a 6xHis tag is incorporated into the expression vector, the expressed 6xHis tag is suited for affinity chromatography over a Ni(II)- NTA resin. A HPLC apparatus (ÄKTA Pure Protein Purification System, Cytiva LifeSciences) equipped with buffer A and buffer B is used. Buffer A and buffer B are in fluid communication with the affinity chromatography media, such as a Ni(II)-NTA column. Buffer A comprises 0 mM imidazole. Buffer B comprises about 200 mM imidazole. The column is primed with several column volumes of Buffer A, followed by several volumes of a diluted Buffer B in Buffer A. The concentrated supernatant is flowed through the column and is allowed to incubate for several minutes. A ramp of 0 mM imidazole to about 150 mM imidazole is used to elute undesired components. A final wash of several column volumes of 100% buffer B (200 mM imidazole) is used to elute the purified target fusion protein. The purified target fusion protein / peptide is collected for further processing. Further Purification – Cleaving Affinity Tag

[0568] The purified His-tagged target fusion protein / peptide is further treated with a protease that selectively cleaves the cleavable linker, yielding the purified, un-tagged target fusion protein / peptide. The un-tagged target fusion protein / peptide is run through a spin column with the appropriate molecular weight cut-off to yield a concentrated target fusion protein / peptide using a table-top centrifuge. Characterization

[0569] The purified and concentrated fusion protein / peptide may be characterized by SDS-PAGE, circular dichroism (CD) spectroscopy, nuclear magnetic resonance (NMR), mass spectrometry (MS), and the like.

[0570] SDS-PAGE. A protein gel (e.g., SDS-PAGE) is run with serial dilutions of the concentrated target fusion protein / peptide against a ladder. The protein gel reveals bands corresponding to the desired molecular weight of the target fusion protein / peptide without the cleavable linker motif and affinity tag. The concentrated target fusion protein / peptide is pre-digested with an enzyme to yield a digested product, and the digested product is assessed by SDS-PAGE.

[0571] Circular Dichroism spectroscopy. The concentrated target fusion protein / peptide is analyzed by circular dichroism spectroscopy (CD; J-1000 Series Circular Dichroism Spectropolarimeter, Jasco) to analyze secondary structure(s). A maximum peak at 195 nm and minimal peak at 208 nm and 222 nm are observed corresponding to the alpha helices of the target fusion protein / peptide. A maximum peak at 195 nm and a minimum peak at 218 nm are observed corresponding to the beta sheet, of the target fusion protein. A minimum peak at 198 nm is observed corresponding to the random coil of the target fusion protein.

[0572] Mass Spectrometry. The concentrated target fusion protein / peptide is analyzed via mass spectrometry (MS), such as liquid chromatograph-mass spectrometry (LC-MS2). The concentrated target fusion protein / peptide is pre-treated with DTT and optionally digested in the presence of a protease, such as chymotrypsin, trypsin, LysC, or AspN. The concentrated target fusion protein / peptide is mixed with 1.0 vol% trifluoroacetic acid (TFA) prior to fragmentation by ESI-MS (Orbitrap, ThermoFisher). Data is collected and processed using Proteome Discoverer (ThermoFisher). Predicted fragment sizes for the various fragmentation and charge states are estimated using Proteome Discoverer or ExPasy.

[0573] Fusion proteins / peptides (0.01%) solution in ethanolic formulation were applied on Asian bleached hair tresses (300 mg). Several properties were evaluated: emulsifier properties, antibacterial properties, fiber integrity, elasticity, Young’s Module, hydrophobicity, among others.

[0574] Emulsifier properties. The emulsifier property of peptides was evaluated by the addiction of each peptide at a concentration of 0.1% (m / v) to a mixture containing 15% of cooking oil and water. The pH of the samples was adjusted to 7. To promote emulsification, the samples were sonicated for 20 seconds. The samples were examined immediately and 7 days after sonication process. The evaluation was classified as ‘Yes’ if the peptide demonstrated emulsifier property or as ‘No’ if the peptide did not demonstrate emulsifier property. The results of the study are presented in Table 3.

[0575] Table 3. Emulsifier property of the peptides of the present disclosure SEQ ID NO: Emulsifiers proprieties Control No 2 No 3 No 4 Yes 5 Yes 6 No 44 No 45 No 46 No 47 No

[0576] Antibacterial agent - medicine or cosmetic. Peptide antibacterial susceptibility testing were performed following CLSI and EUCAST recommendations. Assays were prepared in Lysogeny Broth. Pre-cultures of Pseudomonas aeruginosa and Staphylococcus aureus were prepared beforehand and adjusted with previously made calibration curves to a final number of 1x106 CFUs / mL. A minimal inhibitory concentration assay in 96-well plate was prepared with concentrations ranging from 0.78 to 400 µM. The evaluation was classified as ‘Yes’, if the peptide demonstrated antibacterial activity for both bacteria or as ‘No’ if the peptide did not shown any antibacterial activity. The results of the study are presented in Table 4.

[0577] Table 4. Antibacterial properties of the peptides of the present disclosure SEQ ID NO: Antibacterial properties Control No 2 No 3 No4 No 5 No 6 No 44 No 45 Yes 46 Yes 47 No

[0578] Fiber integrity - Fiber integrity of hair samples with peptides (2 ± 0.1 mg) were analyzed by Differential Scanning Calorimetry (DSC) with a DSC 3500 Sirius from Netzsch. Thermal studies of selected peptides’ effect on hair were conducted using a power compensated differential scanning calorimetry instrument and aluminum pans (max. pressure: 1 bar), at a temperature range from 25 °C to 150 °C (heating rate: 10 °C / min), then an isometric stage at 150 °C for 5 min followed by increase of temperature until 300 °C (heating rate: 10 °C / min). Data are show as a mean of duplicates ± standard error and the value in percentage of hair integrity compared with hair treated with water (enthalpy = 16.4 ± 0.6). The results of the study are presented in Table 5.

[0579] Table 5. Fiber integrity of hair samples with the peptides of the present disclosure SEQ ID NO: Fiber integrity Hair integrity (%) Enthalpy sum for peaks ~190 °C and 230 °C Control 16.4 ± 0.8 - 2 39.1 ±2.3 +139 3 37.2 ± 0.9 +127 4 43.2 ± 0.9 +164 5 36.0 ± 1.9 +120 6 45.4 ± 2.1 +17744 35.3 ± 4.1 +115 45 42.0 ± 3.1 +157 46 37.2 ± 0.2 +127 47 40.4 ± 4.1 +146

[0580] Young’s Module. Hair fibers’ mechanical properties (Young’s modulus) were assessed using a texture analyzer machine (TA.XTplusC, Stable Micro Systems) to study the effect after treatment with the selected peptides. The differences in hairs’ mechanical properties were determined for 30 single hair fibers with low variability in diameter. The fibers were individually attached to a tensile jig (paper template with a fixed gauge length of 55 mm). Test samples were maintained in an excicator to avoid excessive humidity until testing. The stretching measurements were performed at a rate of 0.03 mm / s. This parameter is evaluated in percentage of hair recovery when hair is treated with peptides compared with damaged bleached hair (without any treatment). Data are shown as a mean ± standard error. The results of the study are presented in Table 6.

[0581] Table 6. Hair fibers’ mechanical properties (Young’s modulus) with the peptides of the present disclosure SEQ ID NO: Hair recovery Control 0 2 +18 ± 4% 3 +18 ± 5% 4 -1 ± 3% 5 +23 ± 6% 6 +13 ± 5% 44 +4 ± 4% 45 +13 ± 5% 46 -5 ± 4%47 -11 ± 4%

[0582] Hydrophobicity property. The advancing contact angles were measured using a Force Tensiometer K100C (KRUSS). The contact angles in water were calculated using the force and the estimated fiber diameter. During the measurement, 10 individual hair fibers were submerged to a depth with a rate of 5 mm / min. The results of the study are presented in Table 7.

[0583] Table 7. Hydrophobicity property of the peptides of the present disclosure SEQ ID NO: Hydrophobicity property Control 32.8 ± 16.9 2 30.7 ± 16.6 3 39.6 ± 10.0 4 37.9 ± 9.4 5 28.2 ± 10.7 6 26.0 ± 23.7 44 21.2 ± 23.6 45 34.2 ± 16.8 46 43.5 ± 6.7 47 38.8 ± 12.2

[0584] The penetration / location of peptides in hair fiber is observed labeling the peptides with FITC (fluorescence probe) and observation in fluorescence microscopy (FIG.3).

[0585] Computational Simulation of Fusion Protein Interactions with Model Keratin. Free energies of complexation of fusion peptides and a model keratin were modeled. The free energies were calculated and the number of hydrogen bonds are provided in Table 8. [[more experimental details here?]]

[0586] Table 8. Affinity ΔG (kcal / mol) and hydrogen bond (HB) of the peptides of the present disclosure SEQ ID NO: ΔG (kcal / mol) Total nº HB – 1stpose2 -6.2 10 3 -4.8 9 4 -4.7 4 5 -4.0 10 6 -4.7 11 7 -6.2 9 8 -7.0 7 22 -6.6 5 32 -5.6 5 33 -5.1 3 34 -6.8 6 36 -5.0 4 44 -5.1 11 45 -4.0 4 46 -3.8 7 47 -6.1 12 98 -4.8 12 99 -4.3 9

[0587] A more negative ΔG corresponds a better interaction of the peptide with the keratin model. The calculated number of hydrogens between the peptide and the keratin model is a also a direct measure between the peptide and keratin model. Those parameters give an account on how the fusion peptides interact with keratin.

[0588] Methods for the alignment of sequences for comparison are well known in the art, such methods include GAP, BESTFIT, BLAST, FASTA and TFASTA. GAP uses the algorithm of Needleman and Wunsch ((1970) J Mol Biol, 48: 443-453) to find the global (over the whole the sequence)alignment of two sequences that maximizes the number of matches and minimizes the number of gaps. The BLAST algorithm (Altschul et al. (1990) J Mol Biol 215: 403-10) calculates percent sequence identity and performs a statistical analysis of the similarity between the two sequences. The software for performing BLAST analysis is publicly available through the National Centre for Biotechnology Information (NCBI). Global percentages of similarity and identity may also be determined using one of the methods available in the MatGAT software package (Campanella et al., BMC Bioinformatics, 2003 Jul 10; 4:29. MatGAT: an application that generates similarity / identity matrices using protein or DNA sequences). Minor manual editing may be performed to optimize alignment between conserved motifs, as would be apparent to a person skilled in the art. The sequence identity values, which are indicated in the present subject matter as a percentage were determined over the entire amino acid sequence, using BLAST with the default parameters.

[0589] Where singular forms of elements or features are used in the specification of the claims, the plural form is also included, and vice versa, if not specifically excluded. For example, the term “a peptide” or “the peptide” also includes the plural forms “peptides” or “the peptides,” and vice versa. In the claims articles such as “a,” “an,” and “the” may mean one or more than one unless indicated to the contrary or otherwise evident from the context. Claims or descriptions that include “or” between one or more members of a group are considered satisfied if one, more than one, or all of the group members are present in, employed in, or otherwise relevant to a given product or process unless indicated to the contrary or otherwise evident from the context. The disclosure includes embodiments in which exactly one member of the group is present in, employed in, or otherwise relevant to a given product or process. The disclosure also includes embodiments in which more than one, or all of the group members are present in, employed in, or otherwise relevant to a given product or process.

[0590] Furthermore, it is to be understood that the disclosure encompasses all variations, combinations, and permutations in which one or more limitations, elements, clauses, descriptive terms, etc., from one or more of the claims or from relevant portions of the description is introduced into another claim. For example, any claim that is dependent on another claim can be modified to include one or more limitations found in any other claim that is dependent on the same base claim.

[0591] Furthermore, where the claims recite a composition, it is to be understood that methods of using the composition for any of the purposes disclosed herein are included, and methods ofmaking the composition according to any of the methods of making disclosed herein or other methods known in the art are included, unless otherwise indicated or unless it would be evident to one of ordinary skill in the art that a contradiction or inconsistency would arise.

[0592] Where ranges are given, endpoints are included. Furthermore, it is to be understood that unless otherwise indicated or otherwise evident from the context and / or the understanding of one of ordinary skill in the art, values that are expressed as ranges can assume any specific value within the stated ranges in different embodiments of the disclosure, to the tenth of the unit of the lower limit of the range, unless the context clearly dictates otherwise. It is also to be understood that unless otherwise indicated or otherwise evident from the context and / or the understanding of one of ordinary skill in the art, values expressed as ranges can assume any subrange within the given range, wherein the endpoints of the subrange are expressed to the same degree of accuracy as the tenth of the unit of the lower limit of the range.

[0593] The disclosure should not be seen in any way restricted to the embodiments described and a person with ordinary skill in the art will foresee many possibilities to modifications thereof.

[0594] The above described embodiments are combinable.

[0595] The following claims further set out particular embodiments of the disclosure.

Claims

C L A I M S 1. A fusion protein / peptide comprising: (a) a keratin or keratin associated peptide block; and (b) at least a polypeptide block selected from a list consisting of : (i) an elastin or elastin- like polypeptide (ELP) block, (ii) a silk or silk-like polypeptide (SLP) block, (iii) a collagen or collagen-like polypeptide (CLP) block, (iv) a resilin or resilin-like polypeptide (RLP) block, (v) an abductin or abductin-like polypeptide (ALP) block, or (vi) a combination of two or more blocks selected from (i) to (v).

2. The fusion protein / peptide according to claim 1, wherein the polypeptide block comprises the elastin or elastin like polypeptide block.

3. The fusion protein / peptide according to any one of the previous claims, wherein elastin or elastin like polypeptide (ELP) block has a length of 3 to 30 amino acids; preferably 5 to 20 amino acids, more preferably 15 to 30 amino acids.

4. The fusion protein / peptide according to any one of the claims 1 or claim 2, comprising a linker block as a spacer-like.

5. The fusion protein / peptide according to the previous claims, wherein the linker block has repeat sequence has a length of 2 to 8 amino acids.

6. The fusion protein / peptide according to any one of the previous claims 4-5, wherein the linker block has repeat sequence hasa length of 2 to 40 amino acids, preferably a length of 8 to 30 amino acids.

7. The fusion protein / peptide according to any one of the previous claims 4-6, wherein the linker block comprises a hydrophilic block has a length of 1 to 75 amino acids.

8. The fusion protein / peptide according to the previous claim, wherein the hydrophilic block comprises a length of 10 to 50 amino acids.

9. The fusion protein / peptide according to any one of the previous claims, wherein the linker block adopts an alpha-helix conformation.

10. The fusion protein / peptide according to any one of the previous claims, wherein the linker has a length of 1 to 3 amino acids repeated 0 to 25 times, preferably a length of 1 to 20 times.

11. The fusion protein / peptide according to the previous claim, wherein the linker block comprises 1 or 2 amino acids repeated 10 to 25 times.

12. The fusion protein / peptide according to any of the previous claims, wherein the keratin or keratin associated peptide block comprises SEQ ID NO: 8: GGVCGPSPPCITT, or a sequence having at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO:

8.

13. The fusion protein / peptide according to any of the previous claims, wherein the keratin or keratin associated peptide block comprises SEQ ID NO: 8: GGVCGPSPPCITT, or a sequence having at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO:

8.

14. The fusion protein / peptide according to any of the previous claims, wherein the keratin or keratin associated peptide block comprises SEQ ID NO: 9: GGVCGPSPPC, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO:

9.

15. The fusion protein / peptide according to any of the previous claims, wherein the keratin or keratin associated peptide block comprises SEQ ID NO: 10: CGPSPPCITT, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO:

10.

16. The fusion protein / peptide according to any of the previous claims, wherein the keratin or keratin associated peptide block comprises SEQ ID NO: 68: CLPCLPAASC, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO: 68.

17. The fusion protein / peptide according to any of the previous claims, wherein the keratin or keratin associated peptide block comprises SEQ ID NO: 73: CVSSCCKPQCC, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO:

73.

18. The fusion protein / peptide according to any of the previous claims, wherein the keratin or keratin associated peptide block comprises SEQ ID NO: 74: PITCRRTCYH, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO:

74.

19. The fusion protein / peptide according to any of the previous claims, wherein the keratin or keratin associated peptide block comprises SEQ ID NO: 75: DCKLPCNPCA, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO:

75.

20. The fusion protein / peptide according to any of the previous claims, wherein the keratin or keratin associated peptide block comprises SEQ ID NO: 76: CLPCLPAASC, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO:

76.

21. The fusion protein / peptide according to any of the previous claims, wherein the keratin or keratin associated peptide block comprises SEQ ID NO: 77: CEPAICEPSC, or a sequence comprising at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO:

77.

22. The fusion protein / peptide according to any one of the previous claims, wherein the fusion protein / peptide comprises SEQ ID NO.1: GGVCGPSPPCITTVPGVGVPGVGVPGLGVPGVGVPGVGR, or a sequence at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO:

1.

23. The fusion protein / peptide according to any one of the previous claims, wherein the fusion protein / peptide comprises SEQ ID NO. 2:GGVCGPSPPCITTVPGVGVPGVGVPGVGVPGVGVPGVGVPGVG, or a sequence at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO:

2.

24. The fusion protein / peptide according to any one of the previous claims, wherein the fusion protein / peptide comprises SEQ ID NO. 7: GGVCGPSPPCITTVPGVGVPGVGVPGLGVPGVGVPGVG, or a sequence at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO:

7.

25. The fusion protein / peptide according to any one of the previous claims, wherein the polypeptide block comprises a silk or silk like polypeptide (SLP) block.

26. The fusion protein / peptide according to any one of the previous claims, wherein the fusion protein / peptide comprises SEQ ID NO: 3: GGVCGPSPPCITTGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS, or a sequence at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO:

3.

27. The fusion protein / peptide according to any one of the previous claims, wherein the polypeptide block comprises a collagen or collagen-like polypeptide (CLP) block.

28. The fusion protein / peptide according to any one of the previous claims, wherein the fusion protein comprises SEQ ID NO: 5: GGVCGPSPPCITTGPTGPTGPAGPRGLQGLQGLQGERGEQGPT, or a sequence at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO:

5.

29. The fusion protein / peptide according to any one of the previous claims, wherein the polypeptide component comprises the resilin or resilin-like polypeptide (RLP) component.

30. The fusion protein / peptide according to any of the previous claims, wherein the fusion protein comprises SEQ ID NO: 4: GGVCGPSPPCITTGGRPSDSYGAPGGGN, or a sequence at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO:

4.

31. The fusion protein / peptide according to any one of previous claims, wherein the polypeptide component comprises the abductin or abductin polypeptide (ALP) component.

32. The fusion protein / peptide according to any one of the previous claims, wherein the fusion protein comprises SEQ ID NO.6: GGVCGPSPPCITTGGFGGMGGGSGGFGGMGGGSGGFGGMGGGS, or a sequence at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to SEQ ID NO:

6.

33. The fusion protein / peptide according to any one of previous claims, wherein the keratin or keratin associated peptide component has a length of from 6 to 16 amino acids, and / or the silk or “SLP” has a repeat sequence with a length of 6 to 8 amino acids, and / or the silk or SLP has a length of 10 to 30 amino acids, preferably has a length of 15 to 20 amino acids; and / or the collagen or “CLP” has a repeat sequence with a length of 3 amino acids, and / or the collagen or CLP has a length of 10 to 32 amino acids, preferably has a length of 15 to 30 amino acids; and / or the elastin or “ELP” has a repeat sequence with a length of 5 amino acids, and / or the elastin or ELP has a length of 3 to 30 amino acids; preferably has a length of 8 to 32 , more preferably 15-30; and / or the resilin or “RLP” has a repeat sequence with a length of 11 to 15 amino acids, and / or the resilin or RLP has a length of 10 to 30 amino acids, preferably has a length of 15 to 20 amino acids; and / or the abductin or “ALP” has a repeat sequence with a length of 4 to 10 amino acids, and / or the abductin or ALP has a length of 15 to 32 , more preferably 20-30;.

34. The fusion protein / peptide according to any one of previous claims, wherein the fusion protein has an average molecular weight from about 1 kDa to about 144 kDa, from about 10 kDa to about 144 kDa, or from about 35 kDa to about 130 kDa.

35. The fusion protein / peptide according to any one of previous claims, wherein the fusion protein has an average molecular weight ranging from about 1 kDa to about 5 kDa, from about 5 kDa to about 10 kDa, from about 6 kDa to about 17 kDa, from about 10 kDa to about 15 kDa, from about 14 kDa to about 30 kDa, from between about 15 kDa to about 20 kDa, from about 17 kDa to about 39 kDa, from about 20 kDa to about 25 kDa, from about 25 kDa to about 30 kDa, from about 30 kDa to about 35 kDa, from about 35 kDa to about 40 kDa,from about 39 kDa to about 54 kDa, from about 39 kDa to about 80 kDa, from about 40 kDa to about 45 kDa, from about 45 kDa to about 50 kDa, from about 50 kDa to about 55 kDa, from about 55 kDa to about 60 kDa, from about 60 kDa to about 100 kDa, and from about 80 kDa to about 144 kDa.

36. The fusion protein / peptide according to any one of the previous claims, wherein the fusion protein / peptide comprises a sequence having at least 80% sequence identity to any one of SEQ ID NOS: 1-7, 43-47, or 200-552.

37. The fusion protein / peptide according to any of the previous claims, wherein the fusion protein / peptide comprises a sequence having at least 90%, 95%, 96%, 97%, 98% or 99% sequence identity to any one of SEQ ID NOS: 1-7, 43-47, or 200-552.

38. The fusion protein / peptide according to any of the previous claims, wherein the fusion protein / peptide comprises a sequence identical to any one of SEQ ID NOS: 1-7, 43-47, or 200- 552.

39. The fusion protein / peptide or composition according to any one of the previous claims, wherein the cosmetic product is suitable for hair care or hair treatment.

40. The fusion protein / peptide according to claim 1, wherein the fusion protein / peptide is represented by Formulas (I) to (IV): [Bn1– Am– Bn– Co- Bn2]pFormula (I); or [Bn1– Co– Bn– Am– Bn2]pFormula (II); or [Bn1 – Bn – Co – Am -Bn2]p Formula (III); or [Bn1 – Co – Am – Bn – Bn2]p Formula (IV)wherein, “A” comprises a peptide sequence comprising the keratin or keratin associated peptide block, wherein “m” is an integer from 1 to about 10; “B” comprises a peptide sequence comprising from 1 to 3 amino acids, wherein each “n”, n1”, and “n2” is independently an integer from 0 to 25; “C” comprises a peptide sequence having the structure Dq-Er-Fs-Gt-Hu; wherein “D” comprises the silk or silk-like polypeptide (SLP) block; wherein “E” comprises the collagen or collagen-like polypeptide (CLP) block; wherein “F” comprises the elastin or elastin-like polypeptide (ELP) block; wherein “G” comprises the resilin or resilin-like polypeptide (RLP) block; wherein “H” comprises the abductin or abductin-like polypeptide (ALP) block; wherein “q” is an integer from 0 to about 100, “r” is an integer from 0 to about 200, “s” is an integer from 0 to about 220, “t” is an integer from 0 to about 80, and “u” is an integer from 0 to about 70; wherein “o” is an integer from 0 to about 30; and “p” is an integer from about 1 to about 40; wherein at least one of “n”, n1”, and “n2” or “o” is not 0.The fusion protein / peptide according to claim 33, wherein each of “n”, n1”, and “n2” is independently an integer from 0 to about 25.

41. The fusion protein / peptide according to claim 33 or 34, wherein “o” is an integer from about 1 to about 30.

42. The fusion protein / peptide according to any one of claims 33-35, wherein each “n”, n1”, and “n2” is an integer from 0 to 25 and “o” is an integer from 1 to 30.

43. The fusion protein / peptide according to any one of claims 33-36, wherein “p” is an integer from 3 to 37, from 8 to 15, or from 10 to 12.

44. The fusion protein / peptide according to any one of claims 33-37, wherein “B” comprises a peptide sequence comprising from 1 to 40 amino acids, from 2 to 25, or from 4 to 25. The fusion protein / peptide according to any one of claims 33-38, wherein “B” comprises a peptide sequence having XnZc and / or ZcXn; wherein “Xn” is proline, leucine, isoleucine,glutamic acid, aspartic acid, glutamine, lysine, alanine, arginine or threonine; and wherein “Zc” comprises glycine, alanine, lysine, proline, methionine, glutamine, arginine, threonine, valine, glutamic acid, aspartic acid, or asparagine. The fusion protein / peptide according to any of any one of claims 32-38, wherein the at least one keratin or keratin associated peptide block has a length of from 6 to 16 amino acids, “D” comprises a polypeptide sequence comprising SEQ ID NO: 24: GAGAGS, SEQ ID NO: 25: GAGSGA, SEQ ID NO: 26: GAGAGY, SEQ ID NO: 27: GAGYGA, SEQ ID NO: 28: GAGAGA, SEQ ID NO: 29: GAGAGV, SEQ ID NO: 30: GAGVGA, or SEQ ID NO: 31: GAGAGVGY, or a combination of two or more thereof; “E” comprises a polypeptide sequence GX1Z, wherein “X1” is proline, leucine, isoleucine, glutamic acid, aspartic acid, glutamine, lysine, alanine, arginine or threonine; and wherein Z is glycine, alanine, lysine, proline, methionine, glutamine, arginine, threonine, valine, glutamic acid, aspartic acid, or asparagine; “F” comprises a polypeptide sequence comprising SEQ ID NO: 21: VPGX2G and / or SEQ ID NO: 13: VPAVG, wherein “X2” is arginine, histidine, lysine, aspartic acid, glutamic acid, serine, threonine, asparagine, glutamine, cysteine, glycine, alanine, valine, isoleucine, leucine, methionine, phenylalanine, tyrosine, or tryptophan; “G” comprises a polypeptide sequence comprising SEQ ID NO: 34: GGRPSDSYGAPGGGN and / or SEQ ID NO: 35: GAPAQTPSSQY; “H” comprises a polypeptide sequence comprising SEQ ID NO: 36: GGFGGMGGGS, SEQ ID NO: 37: MGGG, SEQ ID NO: 38: FGGMG, SEQ ID NO: 39: FGGMGGG, SEQ ID NO: 40: GGFGGMGGG, or SEQ ID NO: 41: FGGMGGGNAG, or a combination of two or more thereof.

45. The fusion protein / peptide according to any of any one of claims 32-39, wherein, “A” comprises a peptide sequence X3kCX35CX3k, wherein “X3” is glycine, alanine, valine, isoleucine, leucine, phenylalanine, proline, serine, threonine, asparagine, glutamine, cysteine, methionine, phenylalanine, tyrosine, tryptophan, aspartate, glutamate, histidine, lysine, or arginine, and “k” is an integer from 0 to 3.

46. The fusion protein / peptide according to any of claims 32-40, wherein, “A” comprises SEQ ID NO: 8: GGVCGPSPPCITT, SEQ ID NO: 9: GGVCGPSPPC, SEQ ID NO: 10: CGPSPPCITT, CGPSPPC (SEQ ID NO: 66), or GVCGPSPPC (SEQ ID NO: 67).

47. The fusion protein / peptide according to any one of claims 32-41, wherein the fusion protein has an average molecular weight ranging from about 1 kDa to about 144 kDa, from about 10 kDa to about 144 kDa, or from about 35 kDa to about 130 kDa.

48. The fusion protein / peptide according to any one of claims 32-42, wherein the fusion protein has an average molecular weight ranging from about 1 kDa to about 5 kDa, from about 5 kDa to about 10 kDa, from about 6 kDa to about 17 kDa, from about 10 kDa to about 15 kDa, from about 14 kDa to about 30 kDa, from between about 15 kDa to about 20 kDa, from about 17 kDa to about 39 kDa, from about 20 kDa to about 25 kDa, from about 25 kDa to about 30 kDa, from about 30 kDa to about 35 kDa, from about 35 kDa to about 40 kDa, from about 39 kDa to about 54 kDa, from about 39 kDa to about 80 kDa, from about 40 kDa to about 45 kDa, from about 45 kDa to about 50 kDa, from about 50 kDa to about 55 kDa, from about 55 kDa to about 60 kDa, from about 60 kDa to about 100 kDa, and from about 80 kDa to about 144 kDa.

49. The fusion protein / peptide according to any one of claims 32-43, wherein the silk or silk like peptide (SLP) block forms a β-sheet-rich structure.

50. The fusion protein / peptide according to any one of claims 32-44, wherein the elastin or elastin-like peptide (ELP) block form a β-turn-rich structure.

51. The fusion protein / peptide according to any one of claims 32-45, wherein the elastin-like peptide (ELP) block is thermoresponsive.

52. A composition comprising the fusion protein / peptide according to any one of claims 1-43 for improving elasticity, recovery, hydration, integrity, hydrophobicity, texture, antibacterial, emulsifier properties, mechanical properties, thermal protection, or UV protection, or a combination of two or more thereof, of hair, nails or skin.

53. The composition according to the previous claim, wherein the composition improves the elasticity, recovery, hydration, integrity, texture, antibacterial protections, or UV protection, or a combination of two or more thereof, of the skin.

54. The composition according to any of the previous claims 44-45, wherein the amount of fusion protein / peptide ranges from 0.0001 % – 20 %(w / w); preferably the amount of fusion protein / peptide ranges from 0.001% – 5 % (w / w); or 0.1% to about 1% (w / w).

55. The composition according to any of the previous claims 43-46wherein the composition improves the mechanical properties, color, texture, shape, hydration, integrity, recovery, hydrophobicity, or thermal protection, or a combination of two or more thereof, of the hair.

56. The composition according to any of the previous claims 44-47, wherein the composition improves the mechanical properties, integrity, antimicrobial properties, or UV protection, or a combination of two or more thereof, of the nails.

57. The composition according to any of the previous claims 44-48, wherein the at least one excipient suitable for dermatological use is selected is from the following list: surfactant, emulsifier, preservative, thickener, organic polymer, humectant, silicone, oil, fragrance, vitamin, buffer, antimicrobial agent, antibacterial agent, disinfectant, chelating agent or mixtures thereof.

58. The composition according to any of the previous claims 44-49, comprising at least one excipient suitable for dermatological use.

59. The composition according to the previous claim, wherein the at least one excipient suitable for dermatological use is selected is from the following list: ethanol, benzyl alcohol, diol molecule, urea, ammonium thioglycolate, thioanisole, tris(hydroxymethyl)aminomethane, phosphate buffer, sodium chloride, citrate buffer, or ethanol, or a combination of two or more thereof.

60. The composition according to any of the previous claim, wherein the diol molecule is selected from: ethylene glycol, propylene diol, butylene glycol, butylene diol, or mixtures thereof.

61. The composition according to any of the previous claims 44-52, comprising: 0-30 % (w / v) of ethanol, preferably 10-20%(w / v); 0-3 % (w / v) of benzyl alcohol; preferably 0.5-2%(w / v); 0-20% (w / v) of a diol molecule, preferably 10-15% (w / v).

62. The composition according to any one of the previous claims 44-53, further comprising a propellant, a fragrance, an oil, or mixture thereof.

63. The composition according to any of the claims 44-54, for use in hair treatment.

64. The fusion protein / peptide or composition according to any of previous claims, for use as a cosmetic; namely as a cosmetic of hair, nails or skin.

65. The fusion protein / peptide or composition according to any one of the previous claims 44- 56, wherein the cosmetic product is suitable for hair care or hair treatment.

66. A shampoo, lotion, serum, cream, conditioner, foam, elixir, oil, aerosol or mask comprising a composition / fusion protein / peptide described in any of the previous claims.

67. Use of a composition comprising the fusion protein / peptide according to any one of claims 1-43 as an enhancer agent of one or more properties of hair, nails or skin, or as an agent for enhancing elasticity, hydration, recovery, texture, antimicrobial and / or UV protections of hair, nails and skin.

68. A method of obtaining the fusion protein / peptide according to any one of claims 1-43, comprising the steps of: inoculating a liquid medium with microorganism containing a gene for the expression of the desired fusion protein; allowing the microorganism to multiply during a certain incubation period and inducing the expression under influence of a promoter; and retrieving the desired fusion protein / peptide from the obtained microorganisms by purifying the protein from endogenous contaminants.

69. The method according to the previous claim, wherein the microorganism Escherichia coli.

70. The method according to any one of claims 60-61, wherein the fusion protein / peptide is purified from endogenous contaminants.

71. A method for obtaining the fusion protein / peptide according to any one of claims 1-51 by solid-state synthesis comprising the steps of: initiating solid-state synthesis combining a keratin or keratin associated peptide block and at least a polypeptide block selected from a list consisting of: (i) an elastin or elastin-like polypeptide (ELP) block, (ii) a silk or silk-like polypeptide (SLP) block, (iii) a collagen or collagen-like polypeptide (CLP) block, (iv) a resilin or resilin-like polypeptide (RLP) block, (v) an abductin or abductin-like polypeptide (ALP) block, or (vi) a combination of two or more blocks selected from (i) to (v); executing a plurality of solid-phase reactions to obtain the fusion protein / peptide.

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