Peptides

Abstract

A peptide having three short peptide sequences (SP1-3) spaced apart by a linker having the sequence GSGS(A)nGSGS, wherein n is 6 to 20 residues. The peptide comprises a starter sequence. The peptide comprises at least one N-terminal sequence from the Major Ampullate Spidroin 2 protein derived from Latrodectus Hesperus (SEQ ID NO 1) and / or a C-terminal sequence from the Minor Ampullate Spidroin protein from Araneus ventricosus (SEQ ID NO 2), both spider silk proteins. A further aspect is a composition comprising the peptide and a pharmaceutically acceptable carrier or excipient. The composition can be for cosmetic use. The composition can be a topical preparation for application to skin or hair. The composition can be an emulsion, lotion, spray, aerosol, powder, ointment cream, foam or patch. The composition can comprise at least 0.5% by weight of the peptide. The composition can be formulated to form a film after application. The film can be a breathable barrier. The peptide can be used for the treatment of hair or skin. A further aspect is a film comprising the peptide. Further aspects are polynucleotides encoding the peptide, and vectors and host cells comprising the polynucleotide.

Description

Technical Field The present invention relates to peptides and compositions comprising the peptides. The peptides and their compositions demonstrate a high degree of solubility and film forming ability. The peptides therefore find particular utility in products for the treatment of skin and / or hair and for cosmetic products. The present invention further relates to a genetic construct for expression of the peptides. Background to the Invention The solubility of proteins oftens limits their utility. The solubility of collagen, for example, is 70 mg / ml. It would be beneficial to have proteins with a higher degree of solubility, for example a solubility ay 20°C in an aqueous buffer of at least 100 mg / ml. EP1064010 describes the formation of small peptides by digestion of elastin and suggests that these peptides can improve skin appearance when delivered to the skin in the form of a therapeutic or cosmetic composition. Most preferably the peptides have a molecular weight in the range of about 188-585 kDa. There is a need for further and improved peptides having a high degree of solubility. There is a need for further and improved peptides having an ability to form a film. The film may be able to act as a barrier, for example in skin and haircare products. There is a need for further and improved peptides having anti-oxidant properties. The present invention seeks to address one or more of the above objectives. Summary of the Invention The present invention relates to peptides which are useful in one or more of the above fields. The peptides of the present invention comprise up to 3 short peptide (SP) sequences which are spaced apart by a defined linker sequence. Each short peptide sequence can be the same or different. The short peptide (SP) sequences are selected to deliver a pre-determined functionality, such as cell binding, binding to the surface of hair, colour, binding to the surface of the skin, antioxidant properties, UV absorbing, increasing skin firmness, or skin elasticity and may be derived from collagen, spider silk, keratin or other proteins that have desirable properties. The peptides of the present invention also include either a specific N-terminal or C-terminal sequence. Optionally, a starter sequence can also be present. The present inventors have found that use of a linker which has the sequence: GSGS(A)nGSGS, (wherein n is an integer of 6 to 20, for example is 8 to 16, for example is 8 to 12, for example is 10), provides a consistent spacing between the short peptide sequences and structural integrity and surprisingly improves solubility and film forming ability. A preferred linker has the sequence GSGSAAAAAAAAAAGSGS (SEQ ID No: 20) Additionally, the combination of this linker together with a specific N terminal sequence (SEQ ID No: 1) or C terminal sequence (SEQ ID No: 2) leads to the creation of a stable and soluble peptide. The present invention relates to peptides which are useful for skin care, hair care and cosmetic compositions. The present invention provides therapeutically effective compositions comprising a therapeutically effective concentration of such peptides. The therapeutically effective compositions can function to enhance the appearance of skin, for example by improving the tone, turgor and / or elasticity of the tissue. The present invention is further directed to a composition for improving tissue texture, wherein the composition comprises a peptide as described herein. Preferably the composition includes one or more excipients or carriers in combination with the peptide. Optionally, the composition is a cosmetic preparation. Optionally, the cosmetic preparation is formulated as a topical preparation to be applied to a patient's skin or hair. For example, the topical preparation can be an emulsion, lotion, spray, aerosol, powder, ointment, cream, or foam. In some embodiments the peptide is soluble in an aqueous solution at ambient temperatures. For example, the peptide has a solubility at 20eC in an aqueous buffer of at least 100 mg / ml, for example at least 120 mg / ml, for example at least 140 mg / ml. The peptide may have a solubility at 20eC in 20 mM HEPES buffer, pH 7.5 of from 100 to 180 mg / ml, for example of around 150 mg / ml. Optionally, the aqueous buffer includes one or more of the following: Tris-HCI (10-50 mM), HEPES (10-50 mM), CAPS (10-50 mM), carbonate buffer (10-50 mM), or phosphate buffers such as sodium and potassium phosphate (10- 50 mM). Optionally, the pH is from 6.0 to 10.0. Optionally, the peptide has a molecular weight of less than 42,000 Da, for example less than 40,000 Da, for example less than 30,000 Da. The peptide can have a molecular weight of at least 14,000 Da, for example 14,000 to 42,000 Da, for example 15,000 to 40,000 Da. Optionally, the peptide includes up to 400 amino acid residues and a minimum of 120 amino acid residues, for example has from 150 to 400 amino acid residues. Brief Description of the Figures Figure 1 shows an 4-20% SDS-PAGE showing the production and purification of the expressed proteins for peptides of SEQ ID Nos 31,38 and 40 next to standards. Figure 2 shows an 4-20% SDS-PAGE showing the production and purification of the expressed proteins for peptides of SEQ ID Nos 31,32, 33 and 34 next to standards. Figure 3 shows an 4-20% SDS-PAGE showing the production and purification of the expressed proteins for peptides of SEQ ID Nos 35, 36 and 37 next to standards. Figure 4 shows examples of films formed using the peptides of the invention of SEQ ID Nos: 31, 14, 15 and 36. The water penetration times of these films are given in Example 4. Figure 5 shows exemplary films formed with PEG 20,000 and using peptides according to SEQ ID No: 31 (3% protein, 1% PEG), SEQ ID No: 35 (3% protein, 1% PEG) and SEQ ID No: 36 (3% protein, 3% PEG). Figure 6 shows exemplary films formulated with glycerol and using peptides according to SEQ ID No: 31 (3% protein, 1% glycerol), SEQ ID No: 34 (3% protein, 3% glycerol) and SEQ ID No: 35 (3% protein, 3% glycerol). Figure 7 shows an exemplary film formulated with SEQ ID No: 31 (3 % w / v) with palmitic acid (1% w / v) and glycerol (1 % w / v). Figure 8 shows the hair binding activity of the peptide of SEQ ID No: 31 at 2% (w / v). The results are shown at two different magnifications. Control A, B (B is high magnification of the boxed section shown in A); Test sample (no rinse) C, D (D is a high magnification of the boxed section shown in C). Figure 9 shows the hair binding activity of the peptide of SEQ ID No: 31 at 2% (w / v). The results are shown at two different magnifications. Test sample (dunk rinse) A, B (B is high magnification of the boxed section shown in A); Test sample (soak rinse) C, D (D is a high magnification of the boxed section shown in C). Figure 10 is a bar chart showing results of the antioxidant assay using the peptide of SEQ ID No: 31. Figure 11 shows an image of porous hydrogel formation of the peptide according to SEQ ID No:31. A. protein hydrogel. B. hydrogel loaded with nutrient media. C. hydrogel passed through a syringe needle to print gel letters. Detailed Description of the Invention The peptide, polynucleotides and vectors encoding the peptide, compositions comprising the peptide, expression system and methods of the present invention are now described in further detail. As used herein, the term "and / or" is to be taken as specific disclosure of each of the two specified features or components with or without the other. As used herein, the term "comprising" is to be construed as encompassing both "including" and "consisting of, both meanings being specifically intended, and hence individually disclosed embodiments in accordance with the present invention. As used herein the term “peptide” refers to a polymer composed of amino acids joined by peptide bonds and does not refer to a specific length of the polymer. A "peptide bond" is a covalent bond between two amino acids in which the a-amino group of one amino acid is bonded to the a-carboxyl group of the other amino acid. The peptide can be modified, for example by glycosylation, amidation, carboxylation, phosphorylation, or the like. The modification can be in vitro or in vivo. Amino acid chains with a length of less than approximately 100 amino acids are generally considered within the art to be "peptides", but both "polypeptides", and "proteins" are included within the definition of "peptides" as used herein. The terms “amino acid sequence” and “peptide sequence” are used interchangeably. All amino acid or peptide sequences, unless otherwise designated, are written from the amino terminus (N-terminus) to the carboxy terminus (C-terminus). For convenience of nomenclature, this application refers to a “peptide”. However, the designation of “peptide” in the term “peptide” is not intended to suggest any information regarding the size or relative size of the polymer concerned. As used herein, when applied to an amino acid sequence, “conservative substitution” refers to the substitution of one amino acid residue with another amino acid residue having a side chain with similar physical and chemical properties. For example, conservative substitution may be conducted among amino acid residues having a hydrophobic side chain (e.g., Met, Ala, VaL, Leu, and lie), amino acid residues having a neutral hydrophilic side chain (e.g., Cys, Ser, Thr, Asn, and Gin), amino acid residues having an acidic side chain (e.g., Asp and Glu), amino acid residues having a basic side chain (e.g., His, Lys, and Arg), or amino acid residues having an aromatic side chain (e.g., Trp, Tyr and Phe). It is known in the art that a conservative substitution generally does not cause a significant change in the conformational structure of a protein, and thus can retain the biological activity of the protein. The term "polynucleotide" refers to a polymer of nucleic acid, for example, DNA, cDNA, RNA or synthetically produced DNA or RNA or a recombinantly produced chimeric polynucleotide molecule comprising one of these polynucleotides alone or in combination. The term “nucleic acid” is used interchangeably with the term “polynucleotide”. The term "vector" as used herein refers to a genetic construct to facilitate the handling of a target polynucleotide. The vector may comprise further genes such as marker genes, which allow for the selection of the vector in a suitable host cell and under suitable conditions. Expression of said polynucleotide or vector comprises transcription of the polynucleotide into a translatable mRNA. Usually, a vector comprises regulatory sequences ensuring initiation of transcription. Other elements which are responsible for the initiation of transcription, such as regulatory elements, may also be present. The vector may also comprise transcription termination signals downstream of the target polynucleotide. When applied to an amino acid sequence (or a nucleic acid sequence), “percent sequence identity” refers to a percentage of amino acid (or nucleic acid) residues in a candidate sequence that are identical to those of a reference sequence, relative to the amino acid (or nucleic acid) residues in the candidate sequence during sequence alignment, and if necessary, after introducing gaps to maximize the number of identical amino acids (or nucleic acids). A conservative substitution of amino acid residue may or may not be considered as an identical residue. Percent sequence identity of amino acid (or nucleic acid) sequences can be determined by aligning sequences through tools disclosed in the art. A person skilled in the art may use the default parameters of the tools or adjust the parameters appropriately according to the needs of the alignment, for example by choosing an appropriate algorithm. The percentage identity between two polypeptide sequences may be readily determined by programs such as BLASTp which is freely available at http: / / blast.ncbi.nlm.nih.gov. An “isolated” material has been artificially altered from its natural state. If an “isolated” substance or component occurs in nature, it has been altered or removed from its original state, or both. For example, a polynucleotide or polypeptide naturally occurring in a living animal is not isolated but may be considered “isolated” if the polynucleotide or peptide is sufficiently isolated from the materials with which it coexists in its native state and exists in a sufficiently pure state. In some embodiments, the polynucleotide or peptide are at least 90%, 93%, 95%, 96%, 97%, 98%, 99% pure as determined by electrophoresis (e.g., SDS-PAGE, isoelectric focusing, capillary electrophoresis), or chromatography (e.g., ionexchange chromatography or reverse phase HPLC). The terms “variant”, “homologue” or “derivative” in relation to a nucleotide sequence include any substitution of, variation of, modification of, replacement of, deletion of or addition of one (or more) nucleic acid(s) from or to the sequence. In a first aspect, the present invention provides a peptide having the following formula I or which has 95% sequence identity thereto: [M]x-[Starter Sequence]-[SEQ ID No: 1]a-[SP1]-GSGS(A)nGSGS-[SP2]-GSGS(A)nGSGS)-[SP3]-[SEQ ID No: 2]b wherein: x is 0 or 1; a and b are each independently 0 or 1, but at least one of a or b must be 1; each n is an integer from 6 to 20, for example is 8 to 16; wherein each of SP1, SP2, and SP3 are each independently selected from SEQ ID Nos: 3 to 19; and wherein the Starter Sequence has the sequence: [Motif 1 ]-[Motif2] wherein Motif 1 is selected from SEQ ID Nos: 21 to 26; and wherein Motif 2 is selected from: SEQ ID Nos: 27 to 30. SEQ ID No: 1 has the following sequence: ALGQANTPWSSKENADAFIGAFMNAASQSGAFSSDQIDDMSVISNTLMAAMDNM GGRITQSKLQALDMAFASSVAEIAVADGQNVGAATNAISDALRSAFYQTTGVVNN QFITGISSLIGMFAQVSGNEV SEQ ID No: 2 has the following sequence: SVTSGGYGYGTSAAAGAGVAAGSYAGAVNRLSSAEAASRVSSNIAAIASGGASA LPSVISNIYSGVVASGVSSNEALIQALLELLSALVHVLSSASIGNVSSVGVDSTLNV VQDSVGQYVG At least one of SEQ ID Nos 1 and 2 must be present. Optionally, both SEQ ID Nos: 1 and 2 are present in the peptide. When integer x is 0, this indicates that the N-terminal Methionine residue has been cleaved post-translationally. However, depending upon the expression system used, this post-translational cleavage of methionine may not occu^ and the present invention extends to such peptide constructs, in which integer x is 1 and the N-terminal residue is methionine (see, for example, SEQ ID Nos: 53 to 63). Optionally, n is an integer of 6 to 16, for example is 8 to 12. Thus, (A)n can be a chain of 6, 7, 8, 9, 10, 11, 12,13,14, 15 or 16 alanine residues. Optionally (A)n can be a chain of 10 alanine residues so that the linker sequence has the sequence of SEQ ID No: 20. For the avoidance of any doubt, the reference to “M” is to a methionine residue, “A” is to an alanine residue, “G” is to a glycine residue, and “S” is to a serine residue. SP1, SP2, SP3 can be the same or different to each other. Optionally SP1 and SP2 have a first sequence and SP3 has a second sequence. Optionally SP1 has a first sequence and SP2 and SP3 are each a second sequence. Optionally SP2 has a first sequence and SP1 and SP3 are each a second sequence. Optionally SP3 has a first sequence and SP1 and SP2 are each a second sequence. Optionally, each of SP1, SP2, and SP3 have a different sequence to each other. Optionally each of SP1, SP2, and SP3 have an identical sequence. SP1, SP2, and SP3 each consist of one of the following sequences shown in Table 1 below. Table 1: SEQ ID No: Sequence 3 GGRPSDSYGAPGGGN 4 GGRPCDSYGAPGGGN 5 GGRPSDSYGPPGNPGPP 6 GGRPCDSYGPPGPPSGGN 7 GSCGIGGGIGAGSS 8 SGGACGLGGGYGGGF 9 GGDVEKRGDREE 10 SIKVAVSADRDCIR 11 GVLPGVGGAGVLPGVGGA 12 GLVPGGPGFGGLVPGGPGFG 13 GLGPERGLGPER SEQ ID No: Sequence 14 RGDGGRPSDSYGAPGGGN 15 GRGDSPGGRPSDSYGAPGGGN 16 IKVAVGGRPSDSYGAPGGGN 17 CTGRGDSPACGGRPSDSYGAPGGGN 18 YGISRGGRPSDSYGAPGGGN 19 VGVAPGVGVAPGVGVAPG Optionally, at least one SP1, SP2, and SP3 is SEQ ID No: 3, for example SP1 and / or SP2 can be SEQ ID No: 3. Optionally both SP1 and SP2 can be SEQ ID No: 3. Optionally each of SP1, SP2 and SP3 are SEQ ID No: 3. Optionally, at least one SP1, SP2, and SP3 is SEQ ID No: 4, for example at least one of SP2 and / or SP3 can be SEQ ID No: 4. Optionally both SP2 and SP3 can be SEQ ID No: 4. Optionally each of SP1, SP2 and SP3 are SEQ ID No: 4. Optionally, at least one SP1, SP2, and SP3 is SEQ ID No: 5, for example SP1 and / or SP2 can be SEQ ID No: 5. Optionally both SP1 and SP2 can be SEQ ID No: 5. Optionally each of SP1, SP2 and SP3 are SEQ ID No: 5. Optionally, at least one SP1, SP2, and SP3 is SEQ ID No: 7, for example SP1 and / or SP2 can be SEQ ID No:7. Optionally both SP1 and SP2 can be SEQ ID No: 7. Optionally each of SP1, SP2 and SP3 are SEQ ID No: 7. Optionally, at least one SP1, SP2, and SP3 is SEQ ID No: 9, for example SP1 and / or SP2 can be SEQ ID No: 9. Optionally both SP1 and SP2 can be SEQ ID No: 9. Optionally each of SP1, SP2 and SP3 are SEQ ID No: 9. Optionally, at least one SP1, SP2, and SP3 is SEQ ID No: 11, for example SP1 and / or SP2 can be SEQ ID No: 11. Optionally both SP1 and SP2 can be SEQ ID No: 11. Optionally each of SP1, SP2 and SP3 are SEQ ID No: 11. Optionally, at least one SP1, SP2, and SP3 is SEQ ID No: 19, for example SP1 and / or SP2 can be SEQ ID No: 19. Optionally both SP1 and SP2 can be SEQ ID No: 19. Optionally each of SP1, SP2 and SP3 are SEQ ID No: 19. Optionally, the Starter Sequence may comprise SEQ ID No: 51 formed from the combination of SEQ ID Nos: 21 and 27, namely: GSSHHHHHHSSGVDLGTENLYFQSM Optionally, the Starter Sequence may comprise SEQ ID No: 52 formed from the combination of SEQ ID Nos: 25 and 27, namely: HHHHHHSSGVDLGTENLYFQSM Optionally, the present invention provides a peptide having the following formula la: [M]x -[Starter Sequence]-[SEQ ID No: 1]-[SP1]-GSGS(A)nGSGS-[SP2]-GSGS(A)nGSGS-[SP3]-[SEQ ID No: 2] wherein: x is 0 or 1; each n is an integer from 6 to 20, for example is 8 to 16; wherein each of SP1, SP2, and SP3 is independently selected from SEQ ID Nos: 3 to 19; and wherein the Starter Sequence has the sequence: [Motif 1 ]-[Motif2] wherein Motif 1 is selected from SEQ ID Nos: 21 to 26; and wherein Motif 2 is selected from: SEQ ID Nos: 27 to 30. Optionally, the present invention provides a peptide having the following formula lb: [M]x -[Starter Sequence]-[SEQ ID No: 1]-[SP1]-GSGS(A)nGSGS-[SP2]-GSGS(A)nGSGS-[SP3] wherein: x is 0 or 1; each n is an integer from 6 to 20, for example is 8 to 16; wherein each of SP1, SP2, and SP3 is independently selected from SEQ ID Nos: 3 to 19; and wherein the Starter Sequence has the sequence: [Motif 1 ]-[Motif2] wherein Motif 1 is selected from SEQ ID Nos: 21 to 26; and wherein Motif 2 is selected from: SEQ ID Nos: 27 to 30. Optionally, the present invention provides a peptide having the following formula Ic: [M]x -[Starter Sequence]-[SP1]-GSGS(A)nGSGS-[SP2]-GSGS(A)nGSGS-[SP3]-[SEQ ID No: 2] wherein: x is 0 or 1; each n is an integer from 6 to 20, for example is 8 to 16; wherein each of SP1, SP2, and SP3 is independently selected from SEQ ID Nos: 3 to 19; and wherein the Starter Sequence has the sequence: [Motif 1 ]-[Motif2] wherein Motif 1 is selected from SEQ ID Nos: 21 to 26; and wherein Motif 2 is selected from: SEQ ID Nos: 27 to 30. An exemplary peptide according to formula 1a is shown in SEQ ID No: 31 below in which Motif 1 is SEQ ID No: 21, Motif 2 is SEQ ID No: 27, and SP1, SP2 and SP3 are each SEQ ID No: 3 (the sequence motifs SP1, SP2 and SP3 are shown underlined): GSSHHHHHHSSGVDLGTENLYFQSMALGQANTPWSSKENADAFIGAFMN AASQSGAFSSDQIDDMSVISNTLMAAMDNMGGRITQSKLQALDMAFASSV AEIAVADGQNVGAATNAISDALRSAFYQTTGVVNNQFITGISSLIGMFAQVS GNEVGGRPSDSYGAPGGGNGSGSAAAAAAAAAAGSGSGGRPSDSYGA PGGGNGSGSAAAAAAAAAAGSGSGGRPSDSYGAPGGGNSVTSGGYGY GTSAAAGAGVAAGSYAGAVNRLSSAEAASRVSSNIAAIASGGASALPSVIS NIYSGVVASGVSSNEALIQALLELLSALVHVLSSASIGNVSSVGVDSTLNVV QDSVGQYVG The equivalent sequence in which the initial Met residue is not cleaved post-translationally is SEQ ID No: 53. An alternative exemplary peptide according to formula 1a is shown in SEQ ID No: 32 below in which Motif 1 is SEQ ID No: 21, Motif 2 is SEQ ID No: 27, SP1 and SP3 are each SEQ ID No: 3 and SP2 is SEQ ID No: 7 (the sequence motifs SP1, SP2 and SP3 are shown underlined): GSSHHHHHHSSGVDLGTENLYFQSMALGQANTPWSSKENADAFIGAFMN AASQSGAFSSDQIDDMSVISNTLMAAMDNMGGRITQSKLQALDMAFASSV AEIAVADGQNVGAATNAISDALRSAFYQTTGVVNNQFITGISSLIGMFAQVS GNEVGGRPSDSYGAPGGGNGSGSAAAAAAAAAAGSGSGSCGIGGGIGA GSSGSGSAAAAAAAAAAGSGSGGRPSDSYGAPGGGNSVTSGGYGYGTS AAAGAGVAAGSYAGAVNRLSSAEAASRVSSNIAAIASGGASALPSVISNIYS GVVASGVSSNEALIQALLELLSALVHVLSSASIGNVSSVGVDSTLNVVQDS VGQYVG The equivalent sequence in which the initial Met residue is not cleaved post-translationally is SEQ ID No: 54. An alternative exemplary peptide according to formula 1a is shown in SEQ ID No: 33 below in which Motif 1 is SEQ ID No: 21, Motif 2 is SEQ ID No: 27, SP2 is SEQ ID No: 3, and SP1 and SP3 are each SEQ ID No: 7 (the sequence motifs SP1, SP2 and SP3 are shown underlined): GSSHHHHHHSSGVDLGTENLYFQSMALGQANTPWSSKENADAFIGAFMN AASQSGAFSSDQIDDMSVISNTLMAAMDNMGGRITQSKLQALDMAFASSV AEIAVADGQNVGAATNAISDALRSAFYQTTGVVNNQFITGISSLIGMFAQVS GNEVGSCGIGGGIGAGSSGSGSAAAAAAAAAAGSGSGGRPSDSYGAPG GGNGSGSAAAAAAAAAAGSGSGSCGIGGGIGAGSSSVTSGGYGYGTSAA AGAGVAAGSYAGAVNRLSSAEAASRVSSNIAAIASGGASALPSVISNIYSG VVASGVSSNEALIQALLELLSALVHVLSSASIGNVSSVGVDSTLNVVQDSV GQYVG The equivalent sequence in which the initial Met residue is not cleaved post-translationally is SEQ ID No: 55. An alternative exemplary peptide according to formula 1a is shown in SEQ ID No: 34 below in which Motif 1 is SEQ ID No: 21, Motif 2 is SEQ ID No: 27, and SP1, SP2 and SP3 are each SEQ ID No: 7 (the sequence motifs SP1, SP2 and SP3 are shown underlined): GSSHHHHHHSSGVDLGTENLYFQSMALGQANTPWSSKENADAFIGAFMN AASQSGAFSSDQIDDMSVISNTLMAAMDNMGGRITQSKLQALDMAFASSV AEIAVADGQNVGAATNAISDALRSAFYQTTGVVNNQFITGISSLIGMFAQVS GNEVGSCGIGGGIGAGSSGSGSAAAAAAAAAAGSGSGSCGIGGGIGAGS SGSGSAAAAAAAAAAGSGSGSCGIGGGIGAGSSSVTSGGYGYGTSAAAG AGVAAGSYAGAVNRLSSAEAASRVSSNIAAIASGGASALPSVISNIYSGVVA SGVSSNEALIQALLELLSALVHVLSSASIGNVSSVGVDSTLNVVQDSVGQY VG The equivalent sequence in which the initial Met residue is not cleaved posttranslation is SEQ ID No: 56. An alternative exemplary peptide according to formula 1a is shown in SEQ ID No: 35 below in which Motif 1 is SEQ ID No: 21, Motif 2 is SEQ ID No: 27, and SP1, SP2 and SP3 are each SEQ ID No: 9 (the sequence motifs SP1, SP2 and SP3 are shown underlined): GSSHHHHHHSSGVDLGTENLYFQSMALGQANTPWSSKENADAFIGAFMN AASQSGAFSSDQIDDMSVISNTLMAAMDNMGGRITQSKLQALDMAFASSV AEIAVADGQNVGAATNAISDALRSAFYQTTGVVNNQFITGISSLIGMFAQVS GNEVGGDVEKRGDREEGSGSAAAAAAAAAAGSGSGGDVEKRGDREEGS GSAAAAAAAAAAGSGSGGDVEKRGDREESVTSGGYGYGTSAAAGAGVA AGSYAGAVNRLSSAEAASRVSSNIAAIASGGASALPSVISNIYSGVVASGVS SNEALIQALLELLSALVHVLSSASIGNVSSVGVDSTLNVVQDSVGQYVG The equivalent sequence in which the initial Met residue is not cleaved posttranslation is SEQ ID No: 57. An alternative exemplary peptide according to formula 1a is shown in SEQ ID No: 36 below in which Motif 1 is SEQ ID No: 21, Motif 2 is SEQ ID No: 27, and SP1, SP2 and SP3 are each SEQ ID No: 11 (the sequence motifs SP1, SP2 and SP3 are shown underlined): GSSHHHHHHSSGVDLGTENLYFQSMALGQANTPWSSKENADAFIGAFMN AASQSGAFSSDQIDDMSVISNTLMAAMDNMGGRITQSKLQALDMAFASSV AEIAVADGQNVGAATNAISDALRSAFYQTTGVVNNQFITGISSLIGMFAQVS GNEVGVLPGVGGAGVLPGVGGAGSGSAAAAAAAAAAGSGSGVLPGVGG AGVLPGVGGAGSGSAAAAAAAAAAGSGSGVLPGVGGAGVLPGVGGASV TSGGYGYGTSAAAGAGVAAGSYAGAVNRLSSAEAASRVSSNIAAIASGGA SALPSVISNIYSGVVASGVSSNEALIQALLELLSALVHVLSSASIGNVSSVGV DSTLNVVQDSVGQYVG The equivalent sequence in which the initial Met residue is not cleaved post-translationally is SEQ ID No: 58. An alternative exemplary peptide according to formula 1a is shown in SEQ ID No: 37 below in which Motif 1 is SEQ ID No: 21, Motif 2 is SEQ ID No: 27, and SP1, SP2 and SP3 are each SEQ ID No: 19 (the sequence motifs SP1, SP2 and SP3 are shown underlined): GSSHHHHHHSSGVDLGTENLYFQSMALGQANTPWSSKENADAFIGAFMN AASQSGAFSSDQIDDMSVISNTLMAAMDNMGGRITQSKLQALDMAFASSV AEIAVADGQNVGAATNAISDALRSAFYQTTGVVNNQFITGISSLIGMFAQVS GNEVVGVAPGVGVAPGVGVAPGGSGSAAAAAAAAAAGSGSVGVAPGVG VAPGVGVAPGGSGSAAAAAAAAAAGSGSVGVAPGVGVAPGVGVAPGSV TSGGYGYGTSAAAGAGVAAGSYAGAVNRLSSAEAASRVSSNIAAIASGGA SALPSVISNIYSGVVASGVSSNEALIQALLELLSALVHVLSSASIGNVSSVGV DSTLNVVQDSVGQYVG The equivalent sequence in which the initial Met residue is not cleaved post-translationally is SEQ ID No: 59. An exemplary peptide according to formula 1b is shown in SEQ ID No: 38 in which in which Motif 1 is SEQ ID No: 21, Motif 2 is SEQ ID No: 27, and SP1, SP2 and SP3 are each SEQ ID No: 3 (the sequence motifs SP1, SP2 and SP3 are shown underlined): GSSHHHHHHSSGVDLGTENLYFQSMALGQANTPWSSKENADAFIGAFMN AASQSGAFSSDQIDDMSVISNTLMAAMDNMGGRITQSKLQALDMAFASSV AEIAVADGQNVGAATNAISDALRSAFYQTTGVVNNQFITGISSLIGMFAQVS GNEVGGRPSDSYGAPGGGNGSGSAAAAAAAAAAGSGSGGRPSDSYGA PGGGNGSGSAAAAAAAAAAGSGSGGRPSDSYGAPGGGN The equivalent sequence in which the initial Met residue is not cleaved post-translationally is SEQ ID No: 60. An alternative exemplary peptide according to formula 1b is shown in SEQ ID No: 39 in which in which Motif 1 is SEQ ID No: 21, Motif 2 is SEQ ID No: 27, SP1 is SEQ ID No: 3, SP2 is SEQ ID No: 4 and SP3 is SEQ ID No: 5 (the sequence motifs SP1, SP2 and SP3 are shown underlined): GSSHHHHHHSSGVDLGTENLYFQSMALGQANTPWSSKENADAFIGAFMN AASQSGAFSSDQIDDMSVISNTLMAAMDNMGGRITQSKLQALDMAFASSV AEIAVADGQNVGAATNAISDALRSAFYQTTGVVNNQFITGISSLIGMFAQVS GNEVGGRPSDSYGAPGGGNGSGSAAAAAAAAAAGSGSGGRPCDSYGA PGGGNGSGSAAAAAAAAAAGSGSGGRPSDSYGPPGNPGPP The equivalent sequence in which the initial Met residue is not cleaved post-translationally is SEQ ID No: 61. An exemplary peptide according to formula 1c is shown in SEQ ID No: 40 in which Motif 1 is SEQ ID No: 21, Motif 2 is SEQ ID No: 27, and SP1, SP2 and SP3 are each SEQ ID No: 3 (the sequence motifs SP1, SP2 and SP3 are shown underlined): GSSHHHHHHSSGVDLGTENLYFQSMGGRPSDSYGAPGGGNGSGSAAAA AAAAAAGSGSGGRPSDSYGAPGGGNGSGSAAAAAAAAAAGSGSGGRPS DSYGAPGGGNSVTSGGYGYGTSAAAGAGVAAGSYAGAVNRLSSAEAAS RVSSNIAAIASGGASALPSVISNIYSGVVASGVSSNEALIQALLELLSALVHV LSSASIGNVSSVGVDSTLNVVQDSVGQYVG The equivalent sequence in which the initial Met residue is not cleaved post-translationally is SEQ ID No: 62. An alternative exemplary peptide according to formula 1c is shown in SEQ ID No: 41 in which in which Motif 1 is SEQ ID No: 25, Motif 2 is SEQ ID No: 27, SP1 and SP2 are each SEQ ID No: 3, and SP3 is SEQ ID No: 4 (the sequence motifs SP1, SP2 and SP3 are shown underlined): HHHHHHSSGVDLGTENLYFQSMGGRPSDSYGAPGGGNGSGSAAAAAAA AAAGSGSGGRPSDSYGAPGGGNGSGSAAAAAAAAAAGSGSGGRPCDS YGAPGGGNSVTSGGYGYGTSAAAGAGVAAGSYAGAVNRLSSAEAASRV SSNIAAIASGGASALPSVISNIYSGVVASGVSSNEALIQALLELLSALVHVLS SASIGNVSSVGVDSTLNVVQDSVGQYVG The equivalent sequence in which the initial Met residue is not cleaved post-translationally is SEQ ID No: 63. Thus, in one aspect, the present invention provides a peptide of SEQ ID Nos: 31 to 41 or which has at least 80% sequence identity thereto, optionally which has at least 90% sequence identity thereto, optionally which has at least 95% sequence identity thereto, optionally which has at least 98% sequence identity thereto. The present invention further provides a composition comprising a peptide as described above together with a pharmaceutically acceptable carrier or excipient. Optionally, the composition is suitable for topical application to skin or hair. In a second aspect of the invention, the invention provides a polynucleotide which encodes the peptide described above. Thus, the isolated polynucleotide according to the present invention can be used to encode a peptide which is in accordance with formula 1. In addition, the invention also encompasses a polynucleotide which specifically hybridizes under stringent conditions to the polynucleotide encoding the peptide. For the purposes of the present specification, hybridisation under stringent hybridisation conditions means remaining hybridised after washing with 0.1 xSSC, 0.5% SDS at a temperature of at least 68° C, as described by Sambrook et al (Molecular Cloning. A Laboratory Manual. Cold Spring Harbor Press). It will be understood by a skilled person that numerous different polynucleotides and nucleic acids can encode the same peptide as a result of the degeneracy of the genetic code. In addition, it is to be understood that skilled persons may, using routine techniques, make nucleotide substitutions that do not affect the polypeptide sequence encoded by the polynucleotides described herein to reflect the codon usage of any particular host organism in which the peptides are to be expressed. The polynucleotide of the invention may consist of DNA or RNA. The polynucleotide may be single-stranded or double-stranded. The polynucleotide may include synthetic or modified nucleotides. Several different types of modification to polynucleotides are known in the art. These include methylphosphonate and phosphorothioate backbones, addition of acridine or polylysine chains at the 3' and / or 5' ends of the molecule. For the purposes of the invention as described herein, it is to be understood that the polynucleotides may be modified by any method available in the art. Such modifications may be carried out to enhance the in vivo activity or life span of polynucleotides of interest. Optionally, the polynucleotide of the invention has a nucleotide sequence which expresses a peptide with at least 85% sequence identity to one of SEQ ID Nos: 31 to 41. Optionally, the polynucleotide of the invention encodes a peptide having a sequence identity to SEQ ID Nos: 31 to 41 which is more than 85%, for example which is 90%, 95%, 98% or even more. Optionally, the polynucleotide of the invention has a nucleotide sequence which expresses a peptide with at least 80% sequence identity to one of SEQ ID Nos: 31 to 41. Optionally, the polynucleotide of the invention encodes a polypeptide having a sequence identity to SEQ ID Nos: 31 to 41 which is more than 80%, for example which is 85%, 90%. 95%, 98% or even more. In a third aspect, the present invention provides a vector comprising such a polynucleotide according to the invention as described above, in particular an expression vector expressing, or overexpressing, said polynucleotide. The present invention provides a polynucleotide of any of SEQ ID Nos: 42 to 50. The present invention also encompasses a polynucleotide which specifically hybridizes under stringent conditions to a polynucleotide of any of SEQ ID Nos: 42 to 50. For the purposes of the present specification, hybridisation under stringent hybridisation conditions means remaining hybridised after washing with 0.1 xSSC, 0.5% SDS at a temperature of at least 68° C, as described by Sambrook et al (Molecular Cloning. A Laboratory Manual. Cold Spring Harbor Press). In a fourth aspect, the present invention provides a vector comprising such a polynucleotide according to the invention as described above, in particular an expression vector expressing, or overexpressing, said polynucleotide. The vector can include a polynucleotide having at least 85% sequence identity to any one of SEQ ID Nos: 42 to 50, for example having a sequence identity which is 90%, 95%, 98% or even more identity to any one of SEQ ID Nos: 42 to 50. A “vector” in the present invention refers to a vehicle into which a polynucleotide encoding a peptide can be operably inserted for enabling the peptide to be expressed. The vector can be used to transform, transduce, or transfect (which terms are used interchangeably herein) a host cell, such that the genetic elements carried by the vector are expressed in the host cell. A variety of vectors are available. The vector may comprise a variety of elements that control expression, including a promoter sequence, a transcription initiation sequence, an enhancer sequence, a signal sequence, one or more marker genes, a selection element, a reporter gene, and a transcription termination sequence. Further, the vector may also comprise an origin of replication. The vector may also comprise a component that facilitates the vector to enter into cells, including, but not limited to, viral particle, liposome, or protein shell. For example, the vectors include plasmids, phagemids, cosmids, artificial chromosomes such as yeast artificial chromosome (YAC), bacterial artificial chromosome (BAC) or P1 -derived artificial chromosome (PAC), bacteriophages such as 2 bacteriophage or M13 bacteriophage, animal viruses, and the like. In some embodiments, the vector systems include mammalian, bacterial, and yeast systems, and will include plasmids such as, but not limited to, ‘pENDO-2’ and other vectors available from the laboratory or commercially available vectors. Suitable eukaryotic vectors include vectors having a 2 micron or centromeric origin of replication. Suitable vectors may include plasmid or viral vectors (e.g., replicationdefective retroviruses, adenoviruses, and adeno-associated viruses). Suitable vectors include pET28 and pET32, for example. The present invention thus provides an expression vector comprising the above polynucleotide according to the invention. The expression vector of the present invention can be prepared by subcloning the polynucleotide as described above into the expression vector by any conventionally known genetic engineering method. The type of expression vector that can be used in the present embodiment is not particularly limited, and examples thereof include any expression vector suitable for heterologous gene expression in eukaryotes and able to drive expression of the target peptide. For example, a eukaryotic vector having a 2 micron or centromeric origin of replication together with a constitutive promoter / terminator cassette can conveniently be used, for example the Tef1 promoter. A vector comprising a polynucleotide encoding the peptide may be introduced into a host cell for cloning (amplification of DNA) or gene expression using recombinant techniques well known in the art. In another embodiment, the peptide can be prepared by homologous recombination methods well known in the art. In a fifth aspect, the present invention provides a host cell comprising a vector or a polynucleotide according to the invention as described above. A “host cell” in the present invention refers to a cell into which an exogenous polynucleotide and / or a vector are introduced. Amino acid sequences of the fusion protein of the present application may be converted to corresponding DNA coding sequences using genetic engineering techniques well known in the art. Due to the degeneracy of genetic code, the transformed DNA sequences may not be completely identical, while the encoded protein sequences remain unchanged. Host cells suitable for cloning or expressing the DNA in the vectors of the present invention are prokaryotic, yeast or the above-mentioned advanced eukaryotic cells. Prokaryotic cells suitable for use in the present invention include E. coli (for example E. coli DH5a and BL21de3). In one embodiment, eukaryotic host cells are used for cloning or expressing vectors encoding the peptide according to the invention. Saccharomyces cerevisiae (S288C) or baker's yeast is the most used lower eukaryotic host microorganism. However, many other genera, species and strains are common and suitable for use in the present invention, such as other members of the Saccharomyces clade (including S. pastorianus. S. eubayanus and S. paradoxus), Komagataella (including K. pastoris), Kluyveromyces (including K. lactis) and Yarrowia (including Y. lipolytica). In another aspect of the present invention, the present invention provides a recombinant cell or recombinant microorganism which contains the polynucleotide or vector as described above. Thus, the recombinant cells or recombinant microorganisms according to the present invention can express the peptide of the present invention. The invention further relates to a recombinant host cell comprising the polynucleotide, or the vector as described above. The polynucleotide or vector of the present invention, which is present in the host cell, may either be integrated into the genome of the host cell, or it may be maintained extra-chromosomally. Once the polynucleotide or vector has been incorporated into the appropriate “host cell”, the host cell is maintained under conditions suitable for high level expression of the polynucleotide or vector. The transformed host cells can be grown according to methodology known in the art to achieve cell growth. Optionally, once expressed, the peptide can be purified according to standard procedures of the art. Mention may be made of affinity columns, column chromatography, such as size exclusion chromatography (SEC), gel electrophoresis, ammonium sulphate precipitation and the like. The peptide of the invention can then be isolated from the growth medium, cellular lysates, or cellular membrane fractions. The isolation and purification of the peptide may be by any conventional means such as, for example, preparative chromatographic separations. The host cell is transformed with the above-mentioned expression or cloning vector that can produce the peptide, and then cultured in a conventional nutrient medium, which is suitable for inducing promoters, selecting transformed cells, or amplifying genes encoding target sequences after being modified. The host cells used to produce the peptides in the present invention can be cultured in a variety of media known in the art. The media may also comprise any other necessary additives known in the art in a suitable concentration. The conditions of the media, such as temperature, pH and the like are those selected previously for expression of host cells, which are well known to those of ordinary skill. The present invention further provides a method for producing a peptide as described above, wherein the method comprises the following steps of suitably culturing a recombinant host cell comprising and expressing a polynucleotide encoding the peptide according to formula I or a vector encoding the peptide according to formula I. The polynucleotide can include a sequence according to any one of SEQ ID Nos: SEQ ID Nos: 42 to 50. The polynucleotide can express a peptide having a sequence of any one of SEQ ID Nos: 31 to 41. The peptide can improve the elasticity of the tissue to which the peptide is applied. Optionally, the administration step be comprised of a number of separate administration steps which are conveniently repeated twice daily over a predetermined time, for example where the predetermined time exceeds one week of daily administration of the peptide, for example where the predetermined time exceeds two weeks, or (in some embodiments) is at least a month of daily topical application (with twice daily of the peptide administration over the month being preferable). The peptide of the present invention is suitable for prophylactic or cosmetic use. The peptide can be provided to the relevant tissue, typically to skin or hair. As used herein, the term "providing", when used in conjunction with the peptide, can include, but is not limited to, providing the peptide into or onto the target tissue, for example topically. Mammalian skin consists of a number of overlapping layers of cells. The outer layer of skin is the “stratum corneum” and acts as a physical barrier against physical damage and damage due to the sun. The moisture content of the stratum corneum affects the texture and “softness” of this layer. In lower skin layers a lack of elasticity decreases the tone of the skin and can influence its overall appearance. Use of the inventive peptides within a topical formulation can ameliorate loss of moisture and / or help to maintain hydration of cells. As stated above, the present invention is directed to a peptide according to formula I which is useful as a therapeutic and / or cosmetic composition or agent for modifying tissue, especially skin or hair. The term "modify" is used to mean that the peptide of the present invention (or composition containing such peptide) changes either the appearance, form, characteristics and / or the physical attributes of the tissue to which it is being provided, applied or administered. The change in form can be reflected in any of the following alone or in combination: enhanced appearance of the skin or hair (shine or lustre); increased softness of the skin; increased smoothness of hair; decreased static within hair; reduction of split-ends within hair; increased turgor of the skin; increased texture of the skin; increased elasticity of the skin; decreased wrinkle formation and increased endogenous elastin production in the skin. Details on techniques for formulation and administration of pharmaceuticals may be found in the latest edition of Remington's Pharmaceutical Sciences (Mack Publishing Co, Easton Pa.). Although local topical delivery is desirable, there are other means of delivery, for example: oral, parenteral, aerosol, intramuscular, subcutaneous, transcutaneous, intamedullary, intrathecal, intraventricular, intravenous, intraperitoneal, or intranasal administration. The delivery system of the present invention is preferably a topical delivery system but can alternatively be a subcutaneous, transcutaneous, aerosol, or patch delivery system. The term "cosmetic," as used herein, refers to a beautifying substance or preparation which preserves, restores, bestows, simulates, or enhances the appearance of bodily beauty, specifically as it relates to the appearance of skin or hair. The present invention can be formulated in a number of carrier vehicles, for example, in a spray; an aerosol; a water and an oil-type emulsion; an oil and watertype emulsion; a face cream or body cream; a sun lotion or after-sun lotion; or other topical administration vehicle. The concentration of the peptide of the present invention in an end-use formulation would typically be 5% (by weight) or less, for example 4% (by weight) or less, for example 3% (by weight) or less, for example 2% (by weight) or less, for example 1 % (by weight) or less, such as 0.5% by weight. Typically, an end-use formulation may contain from 0.5% to 3% by weight of the peptide, for example around 0.8% to 2.5% by weight. Optionally, the composition can be a film-forming composition. The film may be able to act as a barrier. The barrier can be a breathable barrier and can be formulated for application to skin or hair. The present invention further provides the film formed using the peptides of the invention. The benefit of forming films in a formulation is that it will leave a protective barrier on the surface of the skin protecting against pollution and potentially sun damage and helping to prevent moisture loss. The film will also smoothen fine lines and wrinkles delivering antiaging effects. The composition can be an aqueous composition and can be formulated to include (i) an aqueous phase, that optionally contains glycerol and / or thickening agents (such as salts and / or gums), (ii) an oil phase that optionally contains fatty acids, ether lipids and triglycerides (e.g., as found in coconut milk and oil) and (iii) optionally one or more other excipients such as preservatives (such as phenoxyethanol or ethylhexylglycerin), colourants, aroma or fragrance compounds, or emulsifier compounds. Optionally, the composition includes more than one peptide of the invention, for example include two or more peptides of the invention, for example includes three or more peptides of the invention. It is preferable that the topical administration of the composition of the present invention occur repeatedly over a predetermined time period, preferably in the range of about one week to about one month. Optionally the peptide of the present invention or a composition comprising a peptide of the present invention can be for application to hair, for example human hair. Optionally the composition can be a shampoo, hair conditioner, hair colourant, hair setting or holding composition or hair spray. Thus, the peptide of the invention or the composition comprising the peptide is useful for treating hair, for example human hair. Optionally the peptide of the present invention or a composition comprising a peptide of the present invention can be for application to skin, for example human skin. Optionally the composition can be a skin emollient to the skin, for example can be a soap, cleanser, scrub, cream, lotion, or moisturiser. Optionally the composition can be for improving the appearance of skin, for example can improve the turgor of skin or can be for reduction of wrinkles. Optionally the composition can be a cosmetics (make-up) composition. Optionally the composition can be a face mask. Optionally the composition can be for treatment of scars. Optionally the composition can be a sunscreen. Optionally, the composition can be a deodorant. Thus, the peptide of the invention or the composition comprising the peptide is useful for treating skin, for example human skin. Preferred or alternative features of each aspect or embodiment of the invention apply mutatis mutandis to each other aspect or embodiment of the invention (unless the context demands otherwise). All documents referred to herein are incorporated by reference. Any modifications and / or variations to described embodiments that would be apparent to one of skill in art are hereby encompassed. Whilst the invention has been described herein with reference to certain specific embodiments and examples, it should be understood that the invention is not intended to be unduly limited to these specific embodiments or examples. The following examples are provided to further illustrate the invention but are not intended to limit the scope of the invention in any manner. Examples Example 1: Sequence creation DNA polynucleotide sequences encoding SEQ ID Nos: 42 to 50 (encoding the peptides of SEQ ID Nos: 31 to 38 and 40, respectively) were created synthetically. Each DNA sequence was then loaded into the T7-driven expression plasmid pET32. Example 2: Expression and Purification of Peptides A pET32 vector containing a relevant coding sequence for each peptide of interest was separately used to transform chemically competent BL21 E. coli, using a standard heat shock approach. Thus, ‘empty’ bacterial cells were caused to take up copies of the expression plasmid encoding the target sequence(s), facilitating downstream protein expression. Cell growth for purification was done in BL21 (DE3) and BL21 STAR (DE3) cells. LB Broth media was used for cell growth. Growth Conditions All cells were grown at 37SC until an OD of approximately 0.6 is reached and were then induced with 1 mM IPTG. The cells were then left to grow at 20sC overnight and spun down and stored dry in -20eC. Each test is run with cells grown with 1 litre of LB Broth. Purification of the Peptides The peptides were expressed using IPTG. The cells were harvested and lysed using a sonicator. After centrifugation to remove insoluble proteins and cell lysate, the soluble fraction was run through an immobilised metal affinity column to separate the polypeptide from the other contaminants. Each protein was then concentrated to (100 mg / mL) and a buffer exchange was performed to store the protein in its final storage buffer (20 mM HEPES pH 7.5). Fig. 1 shows an 4-20% SDS-PAGE showing the production and purification of the expressed proteins for peptides of SEQ ID Nos: 31,38 and 40 next to standards. Fig. 2 shows an 4-20% SDS-PAGE showing the production and purification of the expressed proteins for peptides of SEQ ID Nos: 31,32, 33 and 34 next to standards. Fig. 3 shows an 4-20% SDS-PAGE showing the production and purification of the expressed proteins for peptides of SEQ ID Nos: 35 to 37 next to standards. Example 3 - Characteristics of the Expressed Peptides Colour of Peptides Each of the peptides expressed (SEQ ID Nos: 31 to 38 and 40) were colourless. At higher concentrations, the protein solutions turn a slight yellow solution and are slightly viscous in consistency. Solubility of Peptides Each of the peptides expressed (SEQ ID Nos: 31 to 38 and 40) were soluble up to 150 mg / mL in 25 mM HEPES pH 7.5 at 239 C. Thermostability of Peptides Each of the peptides expressed (SEQ ID Nos: 31 to 38 and 40) were shown to be able to handle up to 3 freeze thaw cycles (-20°C to + 25°C) when stored in 20 mM HEPES pH 7.5. The peptides were also stable for 6 months at room temperature and 4°C. The peptides were also stable for 1 year at -20°C and -80°C. Each of the peptides were able to remain in aqueous solution at a temperature of up to 95°C for 30 minutes. pH Stability of Peptides Each of the peptides were soluble in aqueous solutions at pH above 6.4 at 23B C. Example 4 - Film Formation by Peptides - SEQ ID Nos: 31 to 38 and 40 2 mL of each peptide (1-3% w / v) was left to dry overnight at 50eC in silicone moulds. Higher concentrations formed more robust films. Water and oil penetration tests were performed to confirm the permeability of the films. This was done by the addition of these solutions on top of the film and the time taken for the solutes to penetrate through the film was measured. The films showed no penetration of oil. The films also showed that water penetrated through the films, but higher concentrations of proteins had a longer water penetration time. Water penetration times are given below in Table 2. Table 2 Peptide SEQ ID No: Protein Cone (% w / v) Time for water to penetrate (mins) 31 3 1 31 2 0.25 34 2 3 35 3 0.01 35 2 0.01 36 2 1 Figure 4 shows examples of films formed from peptides of SEQ ID No: 31 (2% w / v solution), SEQ ID No: 34 (3% w / v solution), SEQ ID No: 35 (3% w / v solution), and SEQ ID No: 36 (2% w / v solution). Example 5 - Formulations with PEG 20,000. PEG 20,000 and glycerol are well known plasticizers. Plasticizers are chemicals that are added than can make the films more flexible increasing its plasticity. Solutions of peptides according to the invention were mixed together with plasticizers and the solution was left to form films. A 2mL solution containing 1-3% (w / v) peptide and 1-3% (w / v) PEG 20,000 was made and left to form films. The films were then tested for transparency, flexibility, water and oil permeability. It was observed that the films became more stiffer, more opaque and more brittle as the concentration of PEG was increased. Higher concentration of PEG also showed a decrease in water permeability creating more hydrophobic films. Oil did not penetrate through any of the films. Water penetration tests were carried out to test the hydrophobicity of the films formed. The results are shown in the Table 3 below: Table 3 Peptide SEQ ID No: Protein Cone (% w / v) PEG Cone (% w / v) Time for water to penetrate (mins) 31 3 5 60 31 3 1 5 31 2 1 1 31 2 0 1 35 3 3 2 35 3 1 3 35 2 1 2 35 3 0 0 35 2 0 0 36 3 3 3 Peptide SEQ ID No: Protein Cone (% w / v) PEG Cone (% w / v) Time for water to penetrate (mins) 36 2 1 1 36 2 0 1 Figure 5 shows examples of the films formed with PEG 20,000 using peptides of the invention of SEQ ID No: 31 (3% protein, 1% PEG), SEQ ID No: 35 (3% protein, 1% PEG) and SEQ ID No: 36 (3% protein, 3% PEG). Example 6 - Formulations with Glycerol A 2mL solution containing 1-3% (w / v) protein and 1-3% (w / v) glycerol was made and left to form films. The films were then tested for transparency, flexibility, water and oil permeability. It was observed that the films became more flexible and transparent as the concentration of glycerol was increased. Water penetration tests were carried out to test the hydrophobicity of the films formed. The results of the water penetration tests are shown in Table 4 below: Table 4 Peptide SEQ ID No: Protein Cone (% w / v) Glycerol Cone (% w / v) Time for water to penetrate (mins) 31 3 3 60 31 3 1 1 31 2 1 1 31 2 0 1 34 3 3 6 34 3 3 1 34 3 0 3 35 3 3 3 35 3 1 0 35 3 0 0 36 3 1 1.5 Peptide SEQ ID No: Protein Cone (% w / v) Glycerol Cone (% w / v) Time for water to penetrate (mins) 36 2 1 0.5 36 2 0 1 Figure 6 shows exemplary films formulated with glycerol, using peptides of the invention having the following sequences: SEQ ID No: 31 (3% protein, 1% glycerol), SEQ ID No: 34 (3% protein, 3% glycerol) and SEQ ID No: 35 (3% protein, 3% glycerol). Example 7 - Formulations with Palmitate acid Palmitates have been used as an emollient in cosmetics. Palmitic acid at varying concentrations was successfully formulated with SEQ ID No: 31. These formulations were then used to form films with varying characteristics as highlighted in Table 5 below. Table 5 SEQ 31 Cone (% w / v) Palmitic Acid (% w / v) Glycerol (% w / v) Water Resistance Oil Resistance Film Structure 2 1 Yes No brittle, cloudy opaque film 2 0.5 - Yes Yes brittle, opaque film 2 1 1 No Yes flexible, cloudy opaque film 2 0.5 1 No No flexible, opaque film 3 1 Yes No brittle, extremely cloudy opaque film SEQ 31 Cone (% w / v) Palmitic Acid (% w / v) Glycerol (% w / v) Water Resistance Oil Resistance Film Structure 3 0.5 Yes Yes brittle, opaque film 3 1 1 Yes Yes flexible, cloudy opaque film 3 0.5 1 No Yes flexible, opaque film Figure 7 shows an exemplary film formulated with the peptide of SEQ ID No: 31 (3 % w / v) with palmitic acid (1% w / v) and glycerol (1% w / v). Example 8 - Hair Binding Activity All hair was washed with mild soap solution in water followed by a water rinse and left to dry overnight at room temperature. Dry clean hair was soaked for 5 minutes in a solution (20 mM HEPES pH 7.5) containing the peptide of SEQ ID No: 31 (2% w / v). The hair was then rinsed with water for 0 secs (No Rinse), was rinsed by a quick immersion of the soaked hair for 2-3 sec (Dunk Rinse) or was rinsed for a period of 5 mins (Soak Rinse). The rinsed hair was then left to air dry at room temperature overnight and was imaged using a scanning electron microscope. The Control hair was soaked for 5 mins in buffer (20 mM HEPES pH 7.5) and left to air dry overnight at room temperature. Control. This sample has a rough surface, with edges of “flakes” turned upward (see Fig. 8A). At higher magnification (see Fig. 8B) the jagged edge / surface of the hair strand can be seen. No Rinse. This sample has a noticeable smoother surface relative to the “Control” - see Fig. 8C. At higher magnification (see Fig. 8D) there is no jagged edge / surface to the hair strand, and the hair “flakes” are not turned upward as seen in the Control sample. Arrows in Fig. 8C show the presence of aggregates of the peptide on the surface of the hair which is evidence of the peptide bonding the hair strands together. Dunk Rinse. This sample has a noticeable smoother surface relative to the “Control” - see Fig. 9A. At higher magnification (see Fig. 9B) there is no jagged edge / surface to the hair strand, and the hair “flakes” are not turned upward as seen in the Control sample. Arrows in Fig. 9A show the presence of aggregates of the peptide on the surface of the hair but fewer aggregates than are present in the “No Rinse” sample seen in Fig. 8C. Soak Rinse, This sample has a noticeable smoother surface relative to the “Control” - see Fig. 9C. At higher magnification (see Fig. 9D) there is no jagged edge / surface to the hair strand, and the hair “flakes” are not turned upward as seen in the Control sample. Arrows in Fig. 9C show the presence of aggregates of the peptide on the surface of the hair but fewer aggregates than are present in the “No Rinse” sample seen in Fig. 8C. In conclusion, the peptides of the invention showed a clear ability to improve the integrity of the hair strand and the smoothness and overall appearance of the hair strand surface. The observed anti-static characteristics can also reduce or prevent “fly away” hair. Example 9 - Antioxidant Activity Antioxidant assay was carried out using the ABTS Antioxidant Assay Kit by Zen-Bio. The results are shown in Figure 10. Example 10 - Gel Formation The peptides according to the invention can form hydrogels when heated up or when formulated with chemicals such as ethanol and chloroform and plasticizers. Figure 11 shows an image of porous hydrogel formation of the peptide according to SEQ ID No: 31. A. SEQ ID No. 31 protein hydrogel. B. SEQ ID No. 31 hydrogel loaded with nutrient media. C. SEQ ID No: 31 hydrogel passed through a syringe needle to print gel letters.

Claims

1. A peptide having the following formula I:[M]x -[Starter Sequence]-[SEQ ID No: 1]a-[SP1]-GSGS(A)nGSGS-[SP2]-GSGS(A)nGSGS)-[SP3]-[SEQ ID No: 2]bwherein:x is 0 or 1;a and b are each independently 0 or 1, but at least one of a or b must be 1;each n is an integer from 6 to 20;wherein each of SP1, SP2, and SP3 are each independently selected fromSEQ ID Nos: 3 to 19;and wherein the Starter Sequence has the sequence:[Motif 1]-[Motif2]wherein Motif 1 is selected from SEQ ID Nos: 21 to 26; andwherein Motif 2 is selected from: SEQ ID Nos: 27 to 30.

2. The peptide as claimed in claim 1, wherein a and b are each 1.

3. The peptide as claimed in either one of claims 1 and 2, wherein each of SP1, SP2 and SP3 are independently comprise a different sequence to each other.

4. The peptide as claimed in either one of claims 1 and 2, wherein at least two of SP1, SP2 and SP3 have the same sequence.

5. The peptide as claimed in claim 4, wherein each of SP1, SP2 and SP3 have the same sequence.

6. The peptide as claimed in any one of claims 1 to 5 wherein the Starter Sequence has the sequence of SEQ ID No: 51.

7. The peptide as claimed in any one of claims 1 to 5 wherein n is an integer from 8 to 16.

8. The peptide as claimed in claim 7, wherein n is an integer selected from 9, 10, 11 or 12.

9. The peptide as claimed in any one of claims 1 to 8, wherein said peptide has a sequence which has at least 80% sequence identity to one of the sequences of SEQ ID Nos: 31 to 41.10.The peptide as claimed in claim 9 which has at least 90% sequence identity to one of the sequences of SEQ ID Nos: 31 to 41 or to SEQ ID Nos: 53 to 63.11 .The peptide as claimed in any of claims 1 to 9 which includes SEQ ID No: 1.12.The peptide as claimed in any of claims 1 to 9 which includes SEQ ID No: 2.

13. A composition comprising a peptide as claimed in any one of claims 1 to 12 in combination with a pharmaceutically acceptable carrier or excipient.

14. The composition as claimed in claim 13 which is for cosmetic use.15.The composition as claimed in claim 14 as a topical preparation for application to skin or hair.16.The composition as claimed in claim 15, wherein said topical preparation is an emulsion, lotion, spray, aerosol, powder, ointment cream, foam or patch.17.The composition as claimed in any one of claims 13 to 16 which comprises at least 0.5% by weight of the peptide of claims 1 to 12.18.The composition as claimed in any one of claims 13 to 17 which is formulated to form a film after application.19.The composition as claimed in claim 18 wherein said film is a breathable barrier.

20. A film comprising a peptide of any one of claims 1 to 12.21 .The peptide as claimed in any one of claims 1 to 12 for treatment of hair or skin.22.The composition as claimed in any one of claims 13 to 19 for the treatment of hair or skin.

23. A polynucleotide which encodes a peptide as claimed in any one of claims 1 to 12.

24. The polynucleotide as claimed in claim 23 which has the sequence of any one of SEQ ID Nos: 42 to 50.

25. A vector comprising a polynucleotide as claimed in claim 23 or claim 24.

26. A host cell transformed with a vector as claimed in claim 25.37

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