Growth promoting peptides and uses thereof

Abstract

It is an object of the present invention to provide an alternative, minimally invasive treatment of skin aging.SOLUTION: The present invention relates to a peptide of the amino acid sequence of SEQ ID NO: 283 and to a skin growth-promoting variant of this peptide which, compared to the amino acid sequence of SEQ ID NO: 283, has a deletion of 1 amino acid at the N-terminus, a deletion of 1 to 2 amino acids at the C-terminus or a deletion of 2 amino acids at the N-terminus and a deletion of 2 amino acids at the C-terminus.SELECTED DRAWING: Figure 1

Description

[Background technology]

[0001] The growing desire to maintain a youthful appearance is leading to an increasing amount of research into novel dermatological procedures for treating skin aging, particularly in order for people to live longer and healthier lives. While structural and functional changes are observed in human skin with age (Calleja-Agius J. et al. 2013), numerous factors contribute to these changes, such as environmental factors like UV exposure from sunlight or internal factors like hormonal changes due to menopause (Affinito P. et al. 1999).

[0002] Changes in connective tissue in the dermis and epidermis, particularly a reduction in the extracellular matrix, induce significant alterations in its mechanical properties, thus contributing to wrinkles and sagging of the skin. Furthermore, the metabolism and synthesis of the extracellular matrix are affected by the aging process through enzymatic activity.

[0003] Currently, there are four main solutions to combat the aging process.

[0004] Diet and Hormone Management: Combating the aging process by managing our diet through the use of nutritional supplements. This method is currently still controversial. Several studies suggest that antioxidant nutritional supplements such as vitamin C or lipoic acid may have anti-aging properties, for example.

[0005] Hormone therapy: A risky and controversial solution for anti-aging purposes. Anything related to hormones must be approached with extreme caution, as it can have a wide range of harmful effects. This solution is not widely used, and most research is still at the animal stage.

[0006] Surgical anti-aging solutions: While highly effective in the short term, they are expensive and may require a long healing period. As with any surgical procedure, there are risks and side effects. For example, surgical anti-aging solutions such as eyelifts and facelifts, which involve incisions at the hairline, carry some risk of subcutaneous bleeding, swelling, ptosis, and secondary infections.

[0007] In recent years, there has been a growing enthusiasm for minimally invasive treatments and technologies designed to address issues such as wrinkles, loss of volume, and other skin damage. The most common topical anti-aging solutions are creams and serums. Their active ingredients can be divided into several families.

[0008] Moisturizing ingredients maintain hydrated skin. They are the largest polar molecules that form bonds with water, such as glycosaminoglycans (e.g., hyaluronic acid).

[0009] Collagen and other extracellular matrix components contribute to maintaining a well-organized skin structure by stimulating biosynthesis, provided they can trigger the correct receptors. Cell proliferation components are equally important as they help regenerate skin cells that synthesize components needed by the skin, such as extracellular matrix and growth factors. [Prior art documents] [Patent Documents]

[0010] [Patent Document 1] U.S. Patent Application Publication No. 2014120131 [Patent Document 2] U.S. Patent Application Publication No. 2004132667 [Patent Document 3] U.S. Patent No. 4,186,183 [Patent Document 4] U.S. Patent No. 4,217,344 [Patent Document 5] U.S. Patent No. 4,235,871 Specification [Patent Document 6] U.S. Patent No. 4,261,975 Specification [Patent Document 7] U.S. Patent No. 4,485,054 Specification [Patent Document 8] U.S. Patent No. 4,501,728 Specification [Patent Document 9] U.S. Patent No. 4,774,085 Specification [Patent Document 10]<000​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​Deamer & Bangham, Biochim. Biophys. Acta 443:629-634 (1976) [Non-licensed document 3] Fraley, et al., PNAS 76:3348-3352 (1979)

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Non-licensed literature 9

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Non-licensed Document 13

[0012] The objective of this invention is to provide a minimally invasive treatment as an alternative to skin aging. [Means for solving the problem]

[0013] Description of the Invention The pea genome encodes more than 70,000 different proteins. The applicant has identified six of these proteins, each containing one or more peptides capable of promoting cell growth and / or proliferation (hereinafter referred to herein as "growth-promoting peptides" or "growth-promoting fragments"). Similarly, of the more than 60,000 proteins encoded by the rice genome, the applicant has identified seven proteins, each containing one or more peptides that are bioactive and typically capable of promoting cell growth and / or proliferation. Cell growth-promoting fragments of 14 identified proteins have been found to have effects on elastin and collagen production and cell proliferation (Figures 1 to 109). Specific plant proteins from which the natural peptides are derived are provided in SEQ ID NOs: 1-14 and 705-716. Specific pea proteins from which the peptides are derived include SEQ ID NOs: 1-2 and 7-10, and specific rice proteins from which the peptides are derived include SEQ ID NOs: 3-6 and 11-13. Homogenies of these proteins are described in SEQ ID NOs. 525 to 564. Specific peptides first identified in pea protein are shown in SEQ ID NOs. 15 to 215 and 283 to 340. Specific peptides first identified in rice protein are shown in SEQ ID NOs. 216 to 282 and 341 to 412. Additional peptides and their variants identified in pea and rice proteins disclosed herein are provided in SEQ ID NOs. 418 to 515 and 546 to 704 and 717 to 775.

[0014] In a first embodiment, the present invention provides peptides comprising (a) fragments of pea or rice proteins or homologs thereof disclosed herein, such as those selected from SEQ ID NOs: 1 to 14 and 705 to 716 and 717 to 732, or (b) variants of the fragments or (c) fragments of peptides (hereinafter referred to herein as "Peptides of the Invention"), typically having a length of 5 to 50 amino acids. In one embodiment, the peptides are biologically active. In one embodiment, the peptides have cell growth or proliferation-promoting activity.

[0015] In one embodiment, the peptide of the present invention comprises a sequence selected from SEQ ID NOs: 15-505, 546-704, and 717-775.

[0016] In one embodiment, the peptide of the present invention essentially consists of sequences selected from SEQ ID NOs: 15-505, 546-704, and 717-775.

[0017] In one embodiment, the peptide of the present invention consists of about 3 to 50 amino acids. In one embodiment, the peptide of the present invention consists of about 4 to 50 amino acids. In one embodiment, the peptide of the present invention consists of about 5 to 50 amino acids. In one embodiment, the peptide of the present invention consists of about 6 to 50 amino acids. In one embodiment, the peptide of the present invention consists of about 7 to 50 amino acids.

[0018] In one embodiment, the fragment has 8 to 37 amino acids. In one embodiment, the fragment has a charge between -10 and +4.

[0019] Preferably, the C-terminal amino acid is not cysteine ​​(C) or methionine (M).

[0020] Preferably, the N-terminal amino acid is not cysteine ​​(C), histidine (H), or proline (P).

[0021] Preferably, the C-terminal domain of the fragment does not contain cysteine ​​(C).

[0022] Preferably, the N-terminal domain of the fragment does not contain cysteine ​​(C).

[0023] Preferably, the fragment does not contain cysteine(C).

[0024] Preferably, the peptide does not contain cysteine ​​(C).

[0025] In one embodiment of the present invention, the peptide comprises a sequence selected from SEQ ID NOs: 15 to 505.

[0026] In one embodiment of the present invention, the peptide essentially consists of a sequence selected from SEQ ID NOs: 15 to 505.

[0027] Preferably, the fragment is selected from SEQ ID NOs: 15-215 and 283-340 or from bioactive variants of the fragment.

[0028] Preferably, the fragment is selected from sequence numbers 216-282 and 341-412 or from bioactive variants of the fragment.

[0029] Preferably, the peptide consists of a fragment or a bioactive variant of a fragment selected from SEQ ID NOs: 15 to 417.

[0030] Preferably, the peptide consists of a sequence selected from SEQ ID NOs: 15 to 417.

[0031] Preferably, the fragment is selected from sequence numbers 413-417 or from biologically active variants of the fragment.

[0032] In one embodiment, the peptide comprises or consists of a fragment or a bioactive variant of a fragment selected from SEQ ID NOs: 246, 283, 284, 245, and 42.

[0033] In one embodiment, the peptide comprises a fragment selected from SEQ ID NOs: 247 to 268.

[0034] In one embodiment, the peptide of the present invention is modified. In one embodiment, the peptide is modified with a protecting group. In one embodiment, the peptide is modified to increase its lipophilicity. In one embodiment, the peptide is modified to increase its half-life. In one embodiment, the N or C-terminal amino acid of the peptide is modified. In one embodiment, the N or C-terminal amino acid of the peptide is modified with a protecting group.

[0035] [Sequence ID 1 (Pea Protein 1-P13918)] Preferably, the peptide comprises a bioactive fragment of the protein of SEQ ID NO: 1 or its homologue, or a bioactive variant of that fragment.

[0036] Preferably, the peptide comprises a bioactive fragment selected from SEQ ID NOs: 15 to 90, or a bioactive variant of that fragment.

[0037] The present invention also provides a composition comprising at least one, preferably at least two, preferably at least three, preferably at least four, preferably at least five, preferably at least six, preferably at least seven, preferably at least eight, preferably at least nine, or preferably at least ten, bioactive peptides, each of which typically comprises a different bioactive fragment of SEQ ID NO: 1 or its homologue. Preferably, the composition comprises a first bioactive peptide comprising a first bioactive fragment (or a bioactive variant of the fragment) selected from SEQ ID NOs: 15 to 90 and a second bioactive peptide comprising a second bioactive fragment (or a bioactive variant of the fragment) selected from SEQ ID NOs: 15 to 90.

[0038] In one embodiment, the bioactive peptide, mutant, or fragment is, respectively, a cell growth or proliferation-promoting peptide, mutant, or fragment.

[0039] Homogenies of pea protein 1 (SEQ ID 1) include those of broad bean (Vicia fabia), chickpea (Cicer arietinum), and lentil (Lens culinaris) (SEQ IDs 525 to 527).

[0040] [Sequence ID 2 (Pea Protein 2-Q9M3X6)] Preferably, the peptide comprises a bioactive fragment of the protein of SEQ ID NO: 2 or its homologue, or a bioactive variant of that fragment.

[0041] Preferably, the peptide comprises a bioactive fragment selected from SEQ ID NOs: 91 to 215, or a bioactive variant of that fragment.

[0042] The present invention also provides a composition comprising at least one, preferably at least two, preferably at least three, preferably at least four, preferably at least five, preferably at least six, preferably at least seven, preferably at least eight, preferably at least nine, or preferably at least ten, bioactive peptides, each comprising a different bioactive fragment of SEQ ID NO: 2 or its homologue. Preferably, the composition comprises a first bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 91-215 and a second bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 91-215.

[0043] In one embodiment, the bioactive peptide, mutant, or fragment is, respectively, a cell growth or proliferation-promoting peptide, mutant, or fragment.

[0044] Homologous forms of pea protein 2 (SEQ ID NO: 2) include Pisum abyssinicum, Lathyrus annuus, and Vicia villosa (SEQ ID NOs: 528-530).

[0045] [Sequence ID 3 (Rice Protein 1-Q0DEV5)] Preferably, the peptide comprises a bioactive fragment of the protein of SEQ ID NO: 3 or its homologue, or a bioactive variant of that fragment.

[0046] Preferably, the peptide comprises a bioactive fragment selected from SEQ ID NOs. 216-244, or a bioactive variant of that fragment.

[0047] The present invention also provides a composition comprising at least one, preferably at least two, preferably at least three, preferably at least four, preferably at least five, preferably at least six, preferably at least seven, preferably at least eight, preferably at least nine, or preferably at least ten, bioactive peptides, each comprising a different bioactive fragment of SEQ ID NO: 3 or its homologue. Preferably, the composition comprises a first bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 216-244 and a second bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 216-244.

[0048] In one embodiment, the bioactive peptide, mutant, or fragment is, respectively, a cell growth or proliferation-promoting peptide, mutant, or fragment.

[0049] Homogenies of rice protein 1 (sequence number 15) include Oryza rufipogon, Oryza officinalis, and the barley (Hordeum vulgare) subspecies vulgare (sequence numbers 531 to 533).

[0050] [Sequence ID 4 (Rice Protein 2-P14323)] Preferably, the peptide comprises a bioactive fragment of the protein of SEQ ID NO: 4 or its homologue, or a bioactive variant of that fragment.

[0051] Preferably, the peptide comprises a bioactive fragment or a bioactive variant of the fragment selected from SEQ ID NOs. 245-246.

[0052] The present invention also provides a composition comprising at least one peptide of the present invention comprising different bioactive fragments of SEQ ID NO: 4 or its homologue. Preferably, the composition comprises a first peptide comprising bioactive fragment SEQ ID NO: 245 and a second peptide comprising bioactive fragment SEQ ID NO: 246.

[0053] In one embodiment, the bioactive peptide, mutant, or fragment is, respectively, a cell growth or proliferation-promoting peptide, mutant, or fragment.

[0054] Homologous forms of rice protein 2 (sequence number 4) include Oryza brachyantha and Zizania latifolia (sequence numbers 534 to 536).

[0055] [Sequence ID 5 (Rice Protein 3-P29835)] Preferably, the peptide comprises the protein of SEQ ID NO: 5 or a bioactive fragment of its homolog, or a bioactive variant of that fragment.

[0056] Preferably, the peptide comprises a bioactive fragment selected from SEQ ID NOs. 247-268, or a bioactive variant of that fragment.

[0057] The present invention also provides a composition comprising at least one, preferably at least two, preferably at least three, preferably at least four, preferably at least five, preferably at least six, preferably at least seven, preferably at least eight, preferably at least nine, or preferably at least ten bioactive peptides, each comprising a different bioactive fragment of SEQ ID NO: 5 or its homologue. Preferably, the composition comprises a first bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 247-268 and a second bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 247-268.

[0058] In one embodiment, the bioactive peptide, mutant, or fragment is, respectively, a cell growth or proliferation-promoting peptide, mutant, or fragment.

[0059] Homogenies of rice protein 3 (SEQ ID NO: 5) include maize (Zea Mays), sorghum (Sorghum bicolor), and millet (Setaria italica) (SEQ ID NOs: 537 to 539).

[0060] [Sequence ID 6 (Rice Protein 4-P14614)] Preferably, the peptide comprises a bioactive fragment of the protein of SEQ ID NO: 6 or its homologue, or a bioactive variant of that fragment.

[0061] Preferably, the peptide comprises a bioactive fragment selected from SEQ ID NOs. 269-282 or a bioactive variant of that fragment.

[0062] The present invention also provides a composition comprising at least one, preferably at least two, preferably at least three, preferably at least four, preferably at least five, preferably at least six, preferably at least seven, preferably at least eight, preferably at least nine, or preferably at least ten, bioactive peptides, each comprising a different bioactive fragment of SEQ ID NO: 6 or its homologue. Preferably, the composition comprises a first bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 269-282 and a second bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 269-282.

[0063] In one embodiment, the bioactive peptide, mutant, or fragment is, respectively, a cell growth or proliferation-promoting peptide, mutant, or fragment.

[0064] Homogenies of rice protein 4 (sequence number 6) include Oryza sativa Japonica Group and Brachipodium distachyon (sequence numbers 540 to 542).

[0065] [Sequence ID 7 (Pea Protein 3-P09918)] Preferably, the peptide includes the protein of SEQ ID NO: 7 or a bioactive fragment of its homolog, or a bioactive variant of that fragment.

[0066] Preferably, the peptide comprises the bioactive fragment of SEQ ID NO: 283 or a bioactive variant of that fragment.

[0067] The present invention also provides a composition comprising at least one, preferably at least two, preferably at least three, preferably at least four, preferably at least five, preferably at least six, preferably at least seven, preferably at least eight, preferably at least nine, or preferably at least ten, bioactive peptides, each comprising a different bioactive fragment of SEQ ID NO: 7 or its homologue. Preferably, the composition comprises a bioactive variant of the bioactive fragment SEQ ID NO: 283 or its fragment.

[0068] In one embodiment, the bioactive peptide, mutant, or fragment is, respectively, a cell growth or proliferation-promoting peptide, mutant, or fragment.

[0069] Homologous forms of pea protein 3 (SEQ ID NO: 7) include alfalfa (Medicago truncatula), wild soybean (Glycine soja), and kidney bean (Phaseolus vulgaris) (SEQ ID NOs: 543 to 545).

[0070] [Sequence ID 8 (Pea Protein 4-P02857)] Preferably, the peptide comprises a bioactive fragment of the protein of SEQ ID NO: 8 or its homolog, or a bioactive variant of that fragment.

[0071] Preferably, the peptide comprises a bioactive fragment selected from SEQ ID NOs. 284-307 or a bioactive variant of that fragment.

[0072] The present invention also provides a composition comprising at least one, preferably at least two, preferably at least three, preferably at least four, preferably at least five, preferably at least six, preferably at least seven, preferably at least eight, preferably at least nine, or preferably at least ten, bioactive peptides, each comprising a different bioactive fragment of SEQ ID NO: 8 or its homologue. Preferably, the composition comprises a first bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 284-307 and a second bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 284-307.

[0073] In one embodiment, the bioactive peptide, mutant, or fragment is, respectively, a cell growth or proliferation-promoting peptide, mutant, or fragment.

[0074] Homologous forms of pea protein 4 (SEQ ID NO: 8) include Vicia sativa, Vicia narbonesis, and Cicer arietinum (SEQ ID NOs: 546-548).

[0075] [Sequence ID 9 (Pea Protein 5-P02855)] Preferably, the peptide comprises the protein of SEQ ID NO: 9 or a bioactive fragment of its homolog, or a bioactive variant of that fragment.

[0076] Preferably, the peptide comprises a bioactive fragment selected from SEQ ID NOs. 308-339, or a bioactive variant of that fragment.

[0077] The present invention also provides a composition comprising at least one, preferably at least two, preferably at least three, preferably at least four, preferably at least five, preferably at least six, preferably at least seven, preferably at least eight, preferably at least nine, or preferably at least ten, bioactive peptides, each comprising a different bioactive fragment of SEQ ID NO: 9 or its homologue. Preferably, the composition comprises a first bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 308-339 and a second bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 308-339.

[0078] In one embodiment, the bioactive peptide, mutant, or fragment is, respectively, a cell growth or proliferation-promoting peptide, mutant, or fragment.

[0079] Homologous forms of pea protein 5 (sequence number 9) include Lathyrus hirsutus, Lathyrus cicero, and Lathyrus sativus (sequence numbers 549 to 551).

[0080] [Sequence ID 10 (Pea Protein 6-D3VNE1)] Preferably, the peptide includes the protein of SEQ ID NO: 10 or a bioactive fragment of its homolog, or a bioactive variant of that fragment.

[0081] Preferably, the peptide comprises the bioactive fragment SEQ ID NO: 340 or a bioactive variant of that fragment.

[0082] The present invention also provides a composition comprising at least one, preferably at least two, preferably at least three, preferably at least four, preferably at least five, preferably at least six, preferably at least seven, preferably at least eight, preferably at least nine, or preferably at least ten, bioactive peptides, each comprising a different bioactive fragment of SEQ ID NO: 10 or its homologue. Preferably, the composition comprises a first bioactive peptide comprising the bioactive fragment SEQ ID NO: 340.

[0083] In one embodiment, the bioactive peptide, mutant, or fragment is, respectively, a cell growth or proliferation-promoting peptide, mutant, or fragment.

[0084] Homologous forms of pea protein 6 (sequence number 10) include Medicago truncatula, Vicia peregrine, and Vicia lutea (sequence numbers 552 to 554).

[0085] [Sequence ID 11 (Rice Protein 5-P07728)] Preferably, the peptide includes the protein of SEQ ID NO: 11 or a bioactive fragment of its homolog, or a bioactive variant of that fragment.

[0086] Preferably, the peptide comprises a bioactive fragment selected from SEQ ID NOs. 341-358 or a bioactive variant of that fragment.

[0087] The present invention also provides a composition comprising at least one, preferably at least two, preferably at least three, preferably at least four, preferably at least five, preferably at least six, preferably at least seven, preferably at least eight, preferably at least nine, or preferably at least ten, bioactive peptides, each comprising a different bioactive fragment of SEQ ID NO: 11 or its homologue. Preferably, the composition comprises a first bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 341-358 and a second bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 341-358.

[0088] In one embodiment, the bioactive peptide, mutant, or fragment is, respectively, a cell growth or proliferation-promoting peptide, mutant, or fragment.

[0089] Homogenies of rice protein 5 (SEQ ID NO: 11) include rice indica (Oryza sativa Indica Group), wild rice (Zizania latifolia), and oats (Avena sativa) (SEQ ID NOs: 555 to 557).

[0090] [Sequence ID 12 (Rice Protein 6-P07730)] Preferably, the peptide includes the protein of SEQ ID NO: 12 or a bioactive fragment of its homolog, or a bioactive variant of that fragment.

[0091] Preferably, the peptide comprises a bioactive fragment selected from SEQ ID NOs. 359-401 or a bioactive variant of that fragment.

[0092] The present invention also provides a composition comprising at least one, preferably at least two, preferably at least three, preferably at least four, preferably at least five, preferably at least six, preferably at least seven, preferably at least eight, preferably at least nine, or preferably at least ten, bioactive peptides, each comprising a different bioactive fragment of SEQ ID NO: 12 or its homologue. Preferably, the composition comprises a first bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 359-401 and a second bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 359-401.

[0093] In one embodiment, the bioactive peptide, mutant, or fragment is, respectively, a cell growth or proliferation-promoting peptide, mutant, or fragment.

[0094] Homologous forms of rice protein 6 (sequence number 12) include Oryza brachyantha and Epipactis thunbergii (sequence numbers 558 to 560).

[0095] [Sequence ID 13 (Rice Protein 7-Q0D7S0)] Preferably, the peptide includes the protein of SEQ ID NO: 13 or a bioactive fragment of its homolog, or a bioactive variant of that fragment.

[0096] Preferably, the peptide comprises a bioactive fragment or a bioactive variant of the fragment selected from SEQ ID NOs. 402-412.

[0097] The present invention also provides a composition comprising at least one, preferably at least two, preferably at least three, preferably at least four, preferably at least five, preferably at least six, preferably at least seven, preferably at least eight, preferably at least nine, or preferably at least ten, bioactive peptides, each comprising a different bioactive fragment of SEQ ID NO: 13 or its homologue. Preferably, the composition comprises a first bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 402-412 and a second bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 402-412.

[0098] In one embodiment, the bioactive peptide, mutant, or fragment is, respectively, a cell growth or proliferation-promoting peptide, mutant, or fragment.

[0099] Homologous compounds of rice protein 7 (sequence number 13) include rice indica, wild rice, and oats (sequence numbers 561 to 564).

[0100] [Sequence ID 14 (Staphylococcus aureus protein 1-P0C1U8)] Preferably, the peptide comprises a fragment of the protein of SEQ ID NO: 14 or its homologue.

[0101] Preferably, the peptide comprises a bioactive fragment or a bioactive variant of the fragment selected from SEQ ID NOs: 413-417.

[0102] The present invention also provides a composition comprising at least one, preferably at least two, preferably at least three, preferably at least four, preferably at least five, preferably at least six, preferably at least seven, preferably at least eight, preferably at least nine, or preferably at least ten, bioactive peptides, each comprising a different bioactive fragment of SEQ ID NO: 14 or its homologue. Preferably, the composition comprises a first bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 413-417 and a second bioactive peptide comprising a bioactive fragment selected from SEQ ID NOs: 413-417.

[0103] In one embodiment, the bioactive peptide, mutant, or fragment is, respectively, a cell growth or proliferation-promoting peptide, mutant, or fragment.

[0104] Homogenetics of Staphylococcus aureus protein 1 (SEQ ID NO: 14) include: >gi|580560623|gb|EVF84961.1|Glutamyl endopeptidase [Staphylococcus aureus COAS6020] >gi|580687002|gb|EVH10169.1|Glutamyl endopeptidase [Staphylococcus aureus UCIM6080] >gi|751815683|gb|KIN24957.1|Glutamyl endopeptidase [Staphylococcus aureus MRSA_CVM43477] >gi|781884797|dbj|BAR08486.1|Glutamyl endopeptidase precursor [Staphylococcus aureus subspecies aureus] >gi|781887762|dbj|BAR11210.1|Glutamyl endopeptidase precursor [Staphylococcus aureus subspecies aureus] It includes.

[0105] The present invention also provides a composition comprising at least one, preferably a plurality of, peptides of the present invention, each of which comprises, for example, a bioactive fragment of a protein disclosed herein, or a bioactive variant of that fragment, selected from SEQ ID NOs: 1 to 14 or its homologues.

[0106] Typically, the peptides of the present invention, or each peptide, comprises a bioactive fragment or a bioactive variant of a fragment selected from SEQ ID NOs: 15-505 and 546-704 and 717-775.

[0107] Typically, the peptides of the present invention or each peptide are selected from bioactive fragments or bioactive variants of those fragments, selected from SEQ ID NOs: 15-505 and 546-704 and 717-775.

[0108] The present invention also provides compositions comprising at least one, preferably more than one, peptide of the present invention, wherein each peptide of the present invention comprises a bioactive fragment of pea or rice protein, typically selected from SEQ ID NOs. 1-2 and 7-10, as disclosed herein. Typically, each peptide of the present invention is selected from, or comprises, a bioactive fragment or a bioactive variant thereof, selected from SEQ ID NOs. 15-215 and 283-340.

[0109] The present invention also provides compositions comprising at least one, preferably more, peptides of the present invention, wherein each peptide of the present invention comprises a bioactive fragment of a protein, typically selected from SEQ ID NOs. 3-6 and 11-13, as disclosed herein. Typically, each peptide of the present invention is selected from, or comprises, a bioactive fragment or a bioactive variant thereof, selected from SEQ ID NOs. 216-282 and 341-412.

[0110] Preferably, the composition comprises at least two distinct growth-promoting peptides of the present invention.

[0111] Preferably, the composition comprises at least three distinct growth-promoting peptides of the present invention.

[0112] Preferably, the composition comprises at least four distinct growth-promoting peptides of the present invention.

[0113] Preferably, the composition comprises at least five distinct growth-promoting peptides of the present invention.

[0114] Preferably, the composition comprises at least six distinct growth-promoting peptides of the present invention.

[0115] Preferably, the composition comprises at least seven distinct growth-promoting peptides of the present invention.

[0116] Preferably, the composition comprises at least eight distinct growth-promoting peptides of the present invention.

[0117] Preferably, the composition comprises at least nine distinct growth-promoting peptides of the present invention.

[0118] Preferably, the composition comprises at least 10 distinct growth-promoting peptides of the present invention.

[0119] In one embodiment, the composition comprises one or more of the sequence numbers 247 to 268.

[0120] In one embodiment, the composition includes one or more of the sequence numbers 248, 249, 252, 253, and 257.

[0121] In one embodiment, the present invention includes a composition comprising substantially all of the fragment sequence numbers 15-215 and 283-340 or growth-promoting mutants of those fragments, or a mixture of growth-promoting fragments and mutants.

[0122] In one embodiment, the present invention includes a composition comprising substantially all of fragment sequence numbers 216-282 and 341-412 or growth-promoting mutants of those fragments, or a mixture of growth-promoting fragments and mutants.

[0123] In one embodiment, the composition is rich in peptides having a molecular weight of less than 10 kD.

[0124] In one embodiment, the composition is a powder.

[0125] The present invention also relates to plasters, bandages, or dressing materials comprising the peptide or composition of the present invention, which are suitable for application to wounds.

[0126] The present invention also relates to an artificial cell culture medium comprising the peptide of the present invention. The present invention also relates to an artificial cell culture medium comprising the composition of the present invention. In one embodiment, the cell culture medium is formulated for the culture of eukaryotic cells. In one embodiment, the cell culture medium is formulated for the culture of prokaryotic cells.

[0127] The present invention also relates to plasters, bandages, or dressing materials comprising the peptide or composition of the present invention, which are suitable for application to wounds.

[0128] The present invention also relates to an edible product containing the growth-promoting peptide of the present invention. Preferably, the edible product is artificial.

[0129] The present invention also relates to an edible product comprising a composition of the peptide of the present invention. Preferably, the edible product is artificial.

[0130] Preferably, the edible product is food for human or animal (mammal) or cellular consumption.

[0131] In one embodiment, the artificial edible product is a beverage. In one embodiment, the artificial edible product is a bakery product. In one embodiment, the artificial edible product is a dairy product. In one embodiment, the artificial edible product is a snack product. In one embodiment, the artificial edible product is a baked extruded food. In one embodiment, the artificial edible product is powdered milk. In one embodiment, the artificial edible product is an infant formula product. In one embodiment, the artificial edible product is a confectionery product. In one embodiment, the artificial edible product is yogurt. In one embodiment, the artificial edible product is a yogurt drink. In one embodiment, the artificial edible product is an ice cream product. In one embodiment, the artificial edible product is a frozen food. In one embodiment, the artificial edible product is a breakfast cereal. In one embodiment, the artificial edible product is bread. In one embodiment, the artificial edible product is a flavored milk drink. In one embodiment, the artificial edible product is a candy bar. In one embodiment, the artificial edible product is tea or a tea product. In one embodiment, the artificial edible product is a baked extruded snack product. In one embodiment, the artificial edible product is a fried snack product. In one embodiment, the artificial edible product is a nutritional supplement. In one embodiment, the artificial edible product is a sports nutrition product. In one embodiment, the artificial edible product is baby food. In one embodiment, the artificial edible product is a special food for immunocompromised individuals. In one embodiment, the artificial edible product is food for elderly patients.

[0132] The present invention also relates to peptides of the present invention for use in promoting cell growth.

[0133] The present invention also relates to peptides of the present invention for use in promoting the growth of cell cultures.

[0134] The present invention also relates to peptides of the present invention for use in promoting tissue growth.

[0135] The present invention also relates to peptides of the present invention for use in promoting the growth of dermal or epithelial tissue.

[0136] The present invention also relates to peptides of the present invention for use in promoting skin growth.

[0137] The present invention also relates to peptides of the present invention for use in promoting organ growth.

[0138] The present invention also relates to peptides of the present invention for use in promoting the growth of living organisms.

[0139] The present invention also relates to compositions for use in promoting cell growth.

[0140] The present invention also relates to compositions for use in promoting the growth of cell cultures.

[0141] The present invention also relates to compositions for use in promoting tissue growth.

[0142] The present invention also relates to compositions for use in promoting the growth of epithelial tissue.

[0143] The present invention also relates to compositions for use in promoting skin growth.

[0144] The present invention also relates to compositions for use in promoting organ growth.

[0145] The present invention also relates to compositions for use in promoting the growth of living organisms.

[0146] In one embodiment, a cell, tissue, or organism has normal pathology (e.g., aging skin). In one embodiment of the present invention, a cell, tissue, or skin has abnormal pathology (e.g., epithelial tissue in a GI tubule damaged due to trauma, drug use, or inflammatory disorder).

[0147] Growth-promoting uses may be in-vivo or in-vitro. Growth-promoting uses may include external (i.e., into the skin) or internal (i.e., into the GI duct) administration to mammals.

[0148] The present invention also relates to peptides of the present invention for use in slowing down or inhibiting the aging of human skin.

[0149] The present invention also relates to a method for slowing or inhibiting the aging of human skin, comprising the step of administering the peptide of the present invention to human skin. Typically, the peptide of the present invention is administered topically to the skin. Administration may be by plaster or patch or a formulation suitable for topical application.

[0150] The present invention also relates to compositions of the present invention for use in slowing or inhibiting the aging of human skin. The present invention also relates to peptides of the present invention for use in preventing or slowing the aging of human skin.

[0151] The present invention also relates to a method for slowing or inhibiting the aging of human skin, comprising the step of administering a composition of the present invention to human skin. Typically, the composition of the present invention is administered topically to the skin.

[0152] The present invention also relates to peptides of the present invention for use in the treatment of wounds in mammals.

[0153] The present invention also relates to a composition of the peptide for use in the treatment of wounds in mammals.

[0154] The present invention also relates to a wound treatment composition or product for use in the treatment of wounds in mammals.

[0155] The present invention also relates to peptides of the present invention for use in the treatment or prevention of diseases or conditions characterized by damaged epithelial cells or tissues.

[0156] The present invention also relates to a composition of the peptide for use in the treatment or prevention of diseases or conditions characterized by damaged dermal or epithelial cells or tissues.

[0157] In one embodiment, a disease or condition characterized by damaged dermal or epithelial cells or tissue is selected from cancer, trauma, and others.

[0158] The present invention also relates to peptides of the present invention for use in maintaining or restoring intestinal health in mammals.

[0159] The present invention also relates to a composition of the peptide for use in maintaining or restoring intestinal health in mammals.

[0160] The present invention also relates to peptides of the present invention for use in maintaining or restoring muscle health (e.g., lean tissue mass) in mammals.

[0161] The present invention also relates to a composition of the peptide for use in maintaining or restoring muscle health (e.g., lean tissue mass) in mammals.

[0162] The present invention also relates to pharmaceutical compositions comprising the peptide of the present invention in combination with a pharmaceutically acceptable carrier.

[0163] The present invention also relates to a pharmaceutical composition comprising a composition of the peptide of the present invention in combination with a pharmaceutically acceptable carrier.

[0164] The present invention also relates to the peptide of the present invention for use in the treatment or prevention of inflammatory disorders in mammals.

[0165] The present invention also relates to compositions of the present invention for use in the treatment or prevention of inflammatory disorders in mammals.

[0166] The present invention also relates to edible products, such as foods containing the peptides or compositions of the present invention, such as dairy or non-dairy products, solid foods or beverages, food additives or nutritional supplements. Dairy products may be milk, cheese or yogurt. In one embodiment, the food is a snack bar. The food may contain, for example, any amount of the composition of the present invention from 0.1% to 30% (w / w).

[0167] The peptide of the present invention is used in a preferred form with respect to the total weight of the composition at a concentration that is cosmetically or pharmaceutically effective to achieve the desired effect in the topical cosmetic composition or pharmaceutical composition of the present invention, between 0.00000001% (by weight) and 20% (by weight), preferably between 0.000001% (by weight) and 15% (by weight), more preferably between 0.0001% (by weight) and 10% (by weight), and even more preferably between 0.0001% (by weight) and 5% (by weight). Ideally, the peptide of the present invention is preferably used in a concentration of about 0.00001% w / w to about 0.5% w / w [0.1 to 5000 ppm] of the composition, more preferably between 0.00005 w / w to about 0.05 w / w [0.5 to 500 ppm], and most preferably between about 0.0001 w / w to about 0.01 w / w [1 to 100 ppm]. Ideally, the peptide of the present invention is preferably used in a composition at a concentration of about 0.0001% w / w to about 0.004% w / w.

[0168] The usual daily dose of the peptide composition of the present invention may be 0.2 g to 100 g. However, when administered as a food or medical diet for specific medical purposes, the daily dose may be 50 to 500 g per day.

[0169] The dosage of the composition of the present invention for use in foods and food nutritional supplements (i.e., edible compositions) is broadly in the range of 0.2 to 100 g / day. In one embodiment, the daily dosage is 1 to 10 g / day, ideally about 3 to 8 g / day. In one embodiment, the daily dosage is 10 to 20 g / day. In one embodiment, the daily dosage is 20 to 30 g / day. In one embodiment, the daily dosage is 30 to 40 g / day. In one embodiment, the daily dosage is 10 to 100 g / day. In one embodiment, the daily dosage is about 5 g / day, ideally about 3 to 8 g / day. In one embodiment, the dosage is 2 to 1000 mg / day / kg of body weight. In one embodiment, the dosage is 10 to 500 mg / day / kg of body weight. In one embodiment, the dosage is 10 to 100 mg / day / kg of body weight. In one embodiment, the dosage is 30-70 mg / day / kg of body weight. The dosage of the peptide of the present invention for food nutritional supplements may be 0.00001 mg to 0.01 mg per day or per dose.

[0170] Foods may be Foods for Specific Medicinal Purposes (FSMPs), defined as foods that are specially formulated, processed, and intended for the dietary management of a disease, injury, or medical condition in an individual being treated under medical supervision. These foods are intended for the exclusive or partial intake of a person whose nutritional requirements cannot be met by a normal diet.

[0171] The present invention also relates to an artificial personal care composition comprising the peptide of the present invention.

[0172] The present invention also relates to an artificial personal care composition comprising a composition of the peptides of the present invention.

[0173] In one embodiment, the personal care composition is a skincare product. In one embodiment, the personal care composition is a product formulated for topical application to human skin. In one embodiment, the personal care composition is an anti-aging product. In one embodiment, the personal care composition is a toothpaste product. In one embodiment, the personal care composition is a fragrance product. In one embodiment, the personal care composition is a deodorant product. In one embodiment, the personal care composition is an antiperspirant product. In one embodiment, the personal care composition is a soap. In one embodiment, the personal care composition is a liquid soap. In one embodiment, the personal care composition is a cream. In one embodiment, the personal care composition is a lotion. In one embodiment, the personal care composition is a gel. In one embodiment, the personal care composition is a powder.

[0174] The present invention also relates to an artificial wound treatment composition comprising the peptide of the present invention. The present invention also relates to an artificial wound treatment composition comprising the composition of the present invention. Typically, wound treatment compositions are formulated for topical application to wounds. In one embodiment, the composition comprises a cream, gel, lotion, or powder.

[0175] The present invention also provides topical compositions comprising the peptides of the present invention. It will be understood that the topical compositions may comprise multiple peptides, fragments, and / or variants. In one embodiment, the topical composition comprises substantially all peptides. In one embodiment, the topical composition comprises substantially all variants. The topical compositions of the present invention may be present in formulations selected from the group comprising creams, multiple emulsions, anhydrous compositions, aqueous dispersions, oils, milks, balsams, foams, lotions, gels, cream gels, water-alcohol solutions, hydroglycol solutions, cosmetic products, personal care products, hydrogels, liniments, serums, soaps, sprays, pastes, semi-solid formulations, liniments, serums, shampoos, conditioners, ointments, any rinse-off formulations, talcs, mousses, powders, sprays, aerosols, solutions, suspensions, emulsions, syrups, elixirs, polysaccharide films, patches, gel patches, bandages, adhesive systems, water-in-oil emulsions, oil-in-water emulsions, and silicone emulsions.

[0176] In one embodiment of the present invention, the emulsion contains lipids or oils. The emulsion may be, but is not limited to, oil-in-water, water-in-oil, water-in-water-in-oil, and oil-in-water-in-silicone emulsions. The emulsion may contain humectants. The emulsion may contain defoaming agents such as silicones. The emulsion may have any suitable viscosity. The emulsion may further contain emulsifiers and / or defoaming agents. Methods for preparing emulsions are known to those skilled in the art.

[0177] The topical compositions of the present invention may be incorporated into medical devices for administration. Such devices include, but are not limited to, textiles, patches, bandages, gauges, socks, tights, underwear, dressings, gloves, masks, adhesive patches, non-adhesive patches, occlusive patches, and microelectropatch or suitable adhesive systems. In one such embodiment, the device is in direct contact with a keratin layer, such as skin, and therefore releases the peptides of the present invention. It will be understood that the topical compositions may be incorporated into any suitable form as detailed herein. For example, the topical compositions or peptides of the present invention may be incorporated into a device, or present on the surface of a device, or in a cream, gel, or wax formulation or any suitable formulation as defined herein, and may be incorporated into or on the surface of a device. The device may be adapted for adhesion or attachment to skin.

[0178] In one embodiment, the device is adapted to release a fixed amount of the composition or peptide of the present invention. It will be understood that the amount of composition contained in the sustained-release system depends, for example, on the site where the composition is to be administered, the kinetics and duration of the release of the composition of the present invention, and the nature of the condition, disorder, and / or disease to be treated and / or cured. The device may be such that the composition is released by biodegradation of the device or by friction between the device and the body, depending on the moisture of the body, the pH of the skin, or body temperature.

[0179] In one embodiment of the present invention, the topical composition may further comprise at least one cosmetically or pharmaceutically acceptable excipient. The excipient may be used synonymously with a functional ingredient or additive. The topical composition of the present invention may be administered alone, but it will be understood that it is generally administered in a mixture with cosmetic or pharmaceutically acceptable excipients. Any known excipient may be used, provided that it is well known in the art, suitable for topical administration without excessive toxicity, incompatibility, and / or allergic reactions, and dermatologically acceptable.

[0180] Preferably, any excipients included are present in trace amounts. The amount of excipients included depends on a number of factors, including the type of excipient used, the properties of the excipient, the components (one or more) of the topical composition, the amount of the active substance or peptide in the topical composition, and / or the intended use of the topical composition. The properties and amounts of any excipients should not alter the benefits of the peptide of the present invention to an unacceptable degree.

[0181] In one embodiment of the present invention, the excipient may be a suitable diluent, carrier, binder, lubricant, preservative, coating agent, preservative, stabilizer, pigment, vehicle, solubilizer, base, emollient, emulsifier, fragrance, humectant, and / or surfactant.

[0182] Suitable diluents include, but are not limited to, any diluents disclosed in Patent Document 1 or Patent Document 2. Examples include ethanol, glycerol, and water.

[0183] Examples of suitable carriers include, but are not limited to, lactose, starch, glucose, methylcellulose, magnesium stearate, mannitol, sorbitol, and any suitable carriers disclosed in Patent Document 1 or Patent Document 2.

[0184] Examples of suitable binders include, but are not limited to, starch, gelatin, natural sugars such as glucose, anhydrous lactose, free-flow lactose, β-lactose, corn sweeteners, natural and synthetic rubbers such as gum arabic, tragacanth or sodium alginate, carboxymethylcellulose and polyethylene glycol, and any suitable binders disclosed in Patent Document 1 or Patent Document 2.

[0185] Examples of suitable lubricants include, but are not limited to, sodium oleate, sodium stearate, magnesium stearate, sodium benzoate, sodium acetate, and sodium chloride, as well as any suitable lubricants disclosed in Patent Document 1 or Patent Document 2.

[0186] The carrier may be any suitable carrier known in the art or disclosed in Patent Document 1 or Patent Document 2. In some embodiments, the carrier may include, but is not limited to, liquids such as water, oils or surfactants, polymers, oils such as peanut oil, mineral oil, castor oil, soybean oil, alcohols, polysorbates, sorbitan esters, ether sulfates, sulfates, betaines, glycosides, maltosides, fatty alcohols, nonoxynol, polyxamer, polyoxyethylene, polyethylene glycol, dextrose, glycerol or digitonin. It will be understood that the carrier is dermatologically acceptable. Preferred carriers contain emulsions such as oil-in-water, water-in-oil, water-in-oil-in-water and oil-in-water-in-silicone emulsions. The emulsion may further contain emulsifiers and / or defoamers.

[0187] In one embodiment of the present invention, the topical composition may further comprise one or more additional components. The topical composition of the present invention may be administered continuously, simultaneously, or sequentially together with one or more other additional agents. Such additional components may be beneficial to include in the topical composition, or may be beneficial depending on the intended use of the topical composition. The additional components may be active, functional, or both.

[0188] Examples of such additional ingredients include, but are not limited to, one or more cleansing agents, modifiers, sunscreens, pigments, moisturizers, thickeners, gelling agents, essential oils, astringents, dyes, anticaking agents, defoamers, binders, additives, buffers, chelating agents, topical analgesics, film-forming elements or materials, fillers, polymers, opacifiers, pH adjusters, sprays, reducing agents, scavengers, skin bleaching and whitening agents, skin modifiers, aloe vera, healing agents, analgesics, smoothing agents, pantothenic acid, therapeutic agents, thickeners, vitamins, colorants, formulations, preservatives, defoamers, buffers, astringents, polymers, pH adjusters, deodorants, or any other dermatologically acceptable carriers or surfactants.

[0189] It should be understood that the additional components listed may offer more than one benefit. The given classifications in this specification are for clarity and convenience only and are not intended to limit the additional components to their specific applications or categories.

[0190] Any additional ingredients must be suitable for application to the skin without causing excessive toxicity, incompatibility, and / or allergic reactions.

[0191] In some embodiments, additional components have glucose transport activity or assist glucose transport activity. In some embodiments, additional components have anti-inflammatory activity or assist anti-inflammatory activity. In some embodiments, additional components have anti-aging activity or assist anti-aging activity. In some embodiments, additional components are for the health and / or development of the keratin layer, skin health and / or development, and / or muscle health, recovery and / or development. The active agent may be a pharmacological enhancer. Such active agents are known and available on the market. In such cases, the topical compositions of the present invention may be administered continuously, simultaneously or sequentially with one or more other active agents.

[0192] In some embodiments, additional components may include farnesol ([2E,6E],-3,7,11,-trimethyl-2,6,10,dodecatriene-1-ol), phytantriol (3,7,11,15,tetramethylhexadecane-1,2,3,-triol), desquamating agents, enzymes, enzyme inhibitors, enzyme activators, plant and marine extracts, anti-acne agents, anti-wrinkle or anti-atrophy agents, antioxidants / radical scavengers, chelating agents, flavonoids, anti-inflammatory agents, anti-lipidemia agents, local anesthetics, tanning agents, skin whitening agents, skin healing agents, bisabolol, antibacterial or antifungal agents, sunscreen agents, granular substances, modifiers, structuring agents, and thickening agents.

[0193] Desquamating agents can be any suitable agents that enhance the appearance or texture of the skin, as disclosed in Patent Document 1 or Patent Document 2.

[0194] Examples of anti-acne active substances are disclosed in Patent Document 1 or Patent Document 2 and include resorcinol, salicylic acid, erythromycin, zinc, sulfur, and benzoyl peroxide.

[0195] Examples of thickeners are disclosed in Patent Document 1 or Patent Document 2 and include carboxylic acid polymers, crosslinked polyacrylate polymers, polyacrylamide polymers, and polysaccharides.

[0196] Examples of modifiers are disclosed in Patent Document 1 or Patent Document 2 and include humectants, moisturizers, or skin conditioners.

[0197] Examples of structuring agents include those disclosed in Patent Document 1 or Patent Document 2, and include any agents that provide rheological characteristics to a composition and contribute to the stability of the composition.

[0198] Any suitable antimicrobial or antifungal active substance may be used, examples of which are disclosed in Patent Document 1 or Patent Document 2. Such active substances can destroy microorganisms and prevent their growth or action. Examples include, but are not limited to, beta-lactams, quinolones, tetracyclines, erythromycin, streptomycin sulfate, salicylic acid, and benzoyl peroxide.

[0199] Examples of granular substances include metal oxides. Examples of anti-lipid deposition agents include xanthine agents. Examples of tanning active substances include 1,3-dihydroxy-2-propanone and those disclosed in Patent Document 1 or Patent Document 2. Examples of local anesthetics include benzocaine, lidocaine, and bupivacaine, as well as those disclosed in Patent Document 1 or Patent Document 2.

[0200] Examples of skin beautifying agents include any agent known in the art, such as kojic acid and ascorbic acid, and those disclosed in Patent Document 1 or Patent Document 2.

[0201] Examples of sunscreen active substances include any suitable organic or inorganic sunscreen active substances. Examples include metal oxides, 2-ethylhexyl-p-methoxycinnamate, and those disclosed in Patent Document 1 or Patent Document 2.

[0202] Examples of skin healing agents include panthenoic acid, as disclosed in Patent Document 1 or Patent Document 2.

[0203] Examples of anti-inflammatory drugs include, but are not limited to, any drugs that enhance the appearance, brightness, or color of the skin, as well as non-steroidal drugs such as corticosteroids, hydrocortisone, ibuprofen, and aspirin, and those disclosed in Patent Document 1 or Patent Document 2.

[0204] Examples of flavonoids include flavanones, methoxyflavonones, unsubstituted chalcones and mixtures thereof, as well as those disclosed in Patent Document 1 or Patent Document 2.

[0205] Examples of enzymes include lipase, protease, catalase, superoxide dismutase, amylase, peroxidase, glucuronidase, ceramidase, and hyaluronidase. Examples of enzyme inhibitors include trypsin inhibitors, Bowman-Burk inhibitors, chymotrypsin inhibitors, plant extracts, flavonoids, quercetin chalcone, and those disclosed in Patent Document 1 or Patent Document 2, and mixtures thereof. Examples of enzyme activators include coenzyme A, Q10 (ubiquinone), glycyrrhizin, berberine, chrysin, and those disclosed in Patent Document 1 or Patent Document 2, and mixtures thereof.

[0206] Examples of anti-wrinkle or anti-atrophy active substances include sulfur-containing D and L amino acids, in particular N-acyl derivatives such as N-acetyl-L-cysteine, hydroxy acids, phytic acids, lipoic acid, lysophosphatidic acid, exfoliants, vitamin B3, retinoids, and those disclosed in Patent Document 1 or Patent Document 2, and mixtures thereof.

[0207] Antioxidants / radical scavengers may be any agents useful for providing protection from UV irradiation or other environmental substances that may cause skin damage, such as those disclosed in Patent Document 1 or Patent Document 2. Examples of antioxidants / radical scavengers include ascorbic acid, its salts and derivatives (vitamin C), tocopherol, its salts and derivatives (vitamin E), butylated hydroxylbenzoic acid and its salts, peroxides, gallic acid and alkyl esters, sorbic acid, lipoic acid, amines, lycine pidolate, arginine pyrolate, nordihydroguaiaretic acid, bioflavonoids, curcumin, lysine, methionine, proline, superoxide dismutase, silymarin, tea extracts and mixtures thereof.

[0208] Examples of chelating agents include EDTA, NTA, hydroxamic acid, phytic acid, lactoferrin, and those disclosed in Patent Document 1 or Patent Document 2, and mixtures thereof. A chelating agent is an agent that can remove metal ions by forming a complex, thereby preventing the metal ions from participating in or catalyzing a chemical reaction. Chelating agents are useful for protection from UV irradiation or other environmental substances that can cause skin damage.

[0209] It will be understood that multiple additional components may be added. The amount of additional components may be about 0.001% to about 50% by weight of the composition, preferably about 0.01% to about 20%, preferably about 0.1% to about 10%, about 0.5% to about 10%, about 1% to about 5%, preferably 2% by weight of the composition. The amount of additional components included depends on a number of factors, including the type of additional component used, the nature of the additional component, the components (one or more) of the topical composition, the amount of the active substance or peptide in the topical composition, and / or the intended use of the topical composition. The nature and amount of any additional components should not alter the benefits of the peptide of the present invention to an unacceptable degree.

[0210] The topical composition may be alcohol-free.

[0211] In some embodiments of the present invention, the composition further comprises one or more additional active agents in addition to the peptide of the present invention (also known as the active substance of the composition). Furthermore, or otherwise, the composition may be administered with one or more other additional active agents. Typically, the aforementioned additional active agents are present only in trace amounts. In some embodiments, no additional active agents may be present in the composition. The amount of additional active agents included depends on a number of factors, including the type of additional active agent used, the nature of the additional active agent, the components (one or more) of the topical composition, the amount of the active substance or peptide in the topical composition, and / or the intended use of the topical composition. The nature and amount of any additional active agents should not alter the benefits of the peptide of the present invention to an unacceptable degree.

[0212] It must be understood that an ingredient considered "active" in one product may be a "functional" or "excipient" in another, and vice versa. It should be understood that some ingredients play a dual role, both as active ingredients and as functional or excipient ingredients.

[0213] Examples of additional active agents include glucose transport promoters, skin nutritional supplements, agents for the treatment and / or care of the skin, anti-inflammatory agents, anti-aging agents, cell growth promoters, and pharmacological enhancers. Such agents are well known in the art, and it will be understood that any suitable additional active agent may be used. Additional active agents for the treatment and / or healing of the skin include collagen synths, retinoids, exfoliants, anti-lipids, elastase inhibitors, melanin synthesis stimulants or inhibitors, self-tanning agents, anti-aging agents, antibacterial agents, antifungal agents, fungicidal agents, and healing agents. Active agents also include anti-inflammatory agents.

[0214] Any additional active ingredients must be suitable for application to the skin without causing excessive toxicity, incompatibility, and / or allergic reactions.

[0215] It will be understood that the given classifications in this specification are for clarity and convenience only and are not intended to limit any additional ingredients, excipients, or active substances to any particular application or category listed.

[0216] In particularly preferred embodiments, the methods and uses of the present invention involve administering the peptide or composition of the present invention in combination with one or more other active agents, such as existing growth promoters or pharmacological enhancers available on the market. In such cases, the compounds of the present invention may be administered continuously, simultaneously, or sequentially together with one or more other active agents.

[0217] The effects of the present invention are achieved by topical application or administration of the topical compositions of the present invention described herein to humans, animals, or patients in need of treatment or care. Topical delivery preferably means delivery to keratin layers such as skin, hair, and / or nails, but may also mean delivery to lumens of the body lined with epithelial cells, such as the lungs or airways, gastrointestinal tract, or buccal cavity. The effects may be limited to the surface of the skin, or intracutaneously, or a combination of both.

[0218] The topical compositions of the present invention are administered in amounts that are cosmetically or pharmaceutically effective; in other words, in amounts that are nontoxic in quantity but sufficient to provide the desired effect. Those skilled in the art will understand that it will be possible to determine an appropriate dose of the topical compositions of the present invention to be administered without excessive experimentation. Alternatively, a physician may determine the actual dose that is most appropriate for the patient, depending on the individual condition, the disease or disorder to be treated or cared for, and the person's age, weight, and / or health. This depends on various factors, including the activity of the particular compound used, the metabolic stability and duration of action of that compound, age, weight, overall health, sex, diet, mode and timing of administration, elimination rate, combination of drugs, the severity of the individual condition, and the therapy the individual is receiving. Of course, there may be individual cases where a high dose range is natural, or where a low dose range is natural, and such cases are within the scope of the present invention. For example, the composition may be administered in doses of 0.01 to 50 mg / kg of body weight, such as 0.1 to 30 mg / kg, more preferably 0.1 to 20 mg / kg of body weight, more preferably 0.1 to 10 mg / kg of body weight, and more preferably 0.1 to 5 mg / kg of body weight. In one exemplary embodiment, a single or multiple dose of 10 to 300 mg / day or more preferably 10 to 150 mg / day is administered to the patient. The amount and frequency are as optimal as possible for the purpose. The frequency of application or administration can vary considerably depending on the needs of each subject, with recommendations for application or dosing ranges from once a month to 10 times a day, preferably once a week to 4 times a day, more preferably three times a week to 3 times a day, and even more preferably once or twice a day.

[0219] In a preferred embodiment, repeated use of the topical composition is provided.

[0220] Topical compositions may be applied by rubbing or massaging into keratinous tissue, skin, or areas of the body to be treated or cared for, but are not limited to these. In some embodiments, the composition remains on or is not removed from the area of ​​the body. In other embodiments, the composition is removed after a certain period of time, but is not limited to about 2 to 60 minutes, about 5 to about 30 minutes, preferably about 10 to about 20 minutes. The composition may be removed immediately after application. In some embodiments of the present invention, the compositions of the present invention may be applied to areas to be treated by means of achieving greater penetration of the compositions and / or peptides of the present invention, such as ion electrophoresis, sonication, electroporation, microelectropatch, mechanical pressure, osmotic gradient, occlusive therapy, microinjection, or needle-free injection by pressure, such as oxygen pressure injection, or any combination thereof.

[0221] The peptide of the present invention is used in a preferred form relative to the total weight of the composition of the present invention, at a concentration that is cosmetically or pharmaceutically effective in order to achieve the desired effect, between 0.00000001% (by weight) and 20% (by weight), preferably between 0.000001% (by weight) and 15% (by weight), more preferably between 0.0001% (by weight) and 10% (by weight), and even more preferably between 0.0001% (by weight) and 5% (by weight).

[0222] In some embodiments of the present invention, compositions can be delivered to any one of the following: liposomes, mixed liposomes, oleosomes, niosomes, ethosomes, millicapsules, capsules, macrocapsules, nanocapsules, nanostructured lipid carriers, sponges, cyclodextrins, vesicles, micelles, surfactant mixed micelles, surfactant-phospholipid mixed micelles, millispheres, spheres, lipospheres, particles, nanospheres, nanoparticles, milliparticles, solid nanoparticles, and microemulsions comprising water-in-oil microemulsions having an inverse micelle internal structure, and nanoemulsions, microspheres, and microparticles.

[0223] Various methods are available for preparing liposomes. See, for example, Non-Patent Documents 1, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, Non-Patent Documents 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, Non-Patent Documents 3, 4, 5, 6, 7, 8, 9, and 10. Suitable methods include, for example, sonication, extrusion, high pressure / homogenization, micro-solution preparation, detergent dialysis, calcium-induced fusion and ether fusion of small liposome media, all of which are well known in the art.

[0224] These delivery systems can be adapted to achieve greater penetration of the compounds and / or peptides of the present invention. This can improve pharmacokinetic and pharmacodynamic properties. The delivery system may be a sustained-release system in which the compounds or peptides of the present invention are gradually released over a period of time, preferably at a constant release rate over a period of time. The delivery system is prepared by methods known in the art. The amount of peptide contained in the sustained-release system varies depending on the location and duration of release to which the composition is to be delivered, as well as the type of condition, disease, and / or disorder to be treated or cared for.

[0225] The topical compositions of the present invention may be for human and animal use in human medicine and veterinary medicine.

[0226] The topical compositions of the present invention may be used for pharmaceutical, personal care, and / or cosmetic purposes.

[0227] The composition may be used to treat or care for any disease, disorder, or condition of the skin, including, but not limited to, tinea, dermatitis, allergic dermatitis, eczema, spongiform cysts, edema, skin cancer, ulcers, acne, scarring, cellulitis, fibrosis elastica, keratosis, rosacea, varicose veins, and inflammatory disorders.

[0228] Topical compositions may be used to treat or care for visible signs of aging, including, but not limited to, wrinkles, striae and dark circles, dryness, fine lines, age spots, redness, sagging skin, and conditions caused by sun exposure, stress, pollution and / or dietary restrictions, including sunburn. Topical compositions may also be used to delay, slow, or inhibit aging skin or its onset. Compositions may be administered by medical devices such as plasters or patches as described herein.

[0229] Topical compositions may be used to treat or care for wounds in mammals. In another embodiment, topical compositions are for use in the treatment or prevention of diseases or conditions characterized by damaged epithelial cells or tissues and / or damaged dermis or epithelial cells or tissues. Diseases may include, but are not limited to, cancer and trauma.

[0230] Topical compositions may be used to treat or care for any muscular condition in the treatment or prevention of diseases or conditions characterized by lethargy or low energy levels, to improve muscular conditions in mammals, usually to promote muscle recovery after exercise, to maintain or repair muscle health (e.g., lean tissue mass) in mammals, and to enhance physical performance.

[0231] Topical compositions may be used to promote tissue growth, epithelial tissue growth, skin growth, organ growth, and biological growth. Skin may have normal and / or abnormal pathologies.

[0232] Topical compositions may also be used to treat or care for any inflammatory disorder.

[0233] Further aspects of the present invention relate to pharmaceutical compositions comprising the peptides of the present invention or compositions of the peptides of the present invention mixed with one or more pharmaceutically acceptable diluents, excipients, or carriers. The peptides and compositions of the present invention may be administered alone, but they are generally administered in mixtures with pharmaceutical carriers, excipients, or diluents, particularly for human therapy. Pharmaceutical compositions may be for human and animal use in human medicine and veterinary medicine. Examples of such suitable excipients for various different forms of pharmaceutical compositions described herein can be found in Non-Patent Document 11. In particular, formulations for topical delivery are described in Non-Patent Document 12, the complete contents of which are incorporated herein by reference. Acceptable carriers or diluents for therapeutic use are well known in the art of pharmaceuticals and are described, for example, in Non-Patent Document 13. Examples of suitable carriers include lactose, starch, glucose, methylcellulose, magnesium stearate, mannitol, sorbitol, and the like. Examples of suitable diluents include ethanol, glycerol, and water. The choice of pharmaceutical carriers, excipients, or diluents may be selected in relation to the intended route of administration and standard pharmaceutical practice. Pharmaceutical compositions may include, or in addition to, any suitable binders (one or more), lubricants (one or more), anti-precipitation agents (one or more), coating agents (one or more), and solubilizers (one or more) as carriers, excipients, or diluents. Examples of suitable binders include natural sugars such as starch, gelatin, and glucose; natural and synthetic rubbers such as anhydrous lactose, free-flow lactose, β-lactose, corn sweeteners, gum arabic, tragacanth, or sodium alginate; carboxymethylcellulose; and polyethylene glycol. Examples of suitable lubricants include sodium oleate, sodium stearate, magnesium stearate, sodium benzoate, sodium acetate, and sodium chloride. Preservatives, stabilizers, colorants, and even flavoring agents may be provided in the pharmaceutical composition. Examples of preservatives include sodium benzoate, sorbic acid, and p-hydroxybenzoic acid esters. Antioxidants and anti-precipitation agents may also be used.

[0234] The peptides or compositions of the present invention may be adapted for topical, oral, rectal, parenteral, intramuscular, intraperitoneal, intra-arterial, intra-bronchial, subcutaneous, intradermal, intravenous, intranasal, vaginal, buccal, or sublingual administration routes. For oral administration, compressed tablets, pills, tablets, gellules, drops, and capsules are particularly used. Preferably, these compositions contain 1 to 250 mg, more preferably 10 to 100 mg, of the active ingredient per dose. Other forms of administration may include solutions or emulsions prepared from sterile or sterileable solutions and may be injected intravenously, intra-arterial, subcutaneously, intradermally, intraperitoneally, or intramuscularly. The pharmaceutical compositions of the present invention may be in the form of suppositories, vaginal rings, pessaries, suspensions, emulsions, lotions, ointments, creams, gels, sprays, solutions, or powders. The compositions of the present invention may be formulated for topical delivery. Local delivery generally refers to delivery to the skin, but can also refer to delivery to lumens of the body lined with epithelial cells, such as the lungs or airways, gastrointestinal tract, and buccal cavity. In particular, formulations for local delivery are described in Non-Patent Document 12, the full content of which is incorporated herein by reference. Compositions or formulations for delivery to the airways are described in Non-Patent Document 14, Patent Document 13, Patent Document 14, Patent Document 15, and Patent Document 16. Compositions and formulations for delivering active agents to the ileum, particularly the proximal ileum, include microencapsulated products in which the active agent is encapsulated within a protective matrix formed from microparticles and polymers or milk proteins that are acid-resistant but tend to dissolve in the more alkaline environment of the ileum. Examples of such delivery systems are described in Patent Documents 17 and 18. An alternative to transdermal administration is the use of skin patches. For example, the active ingredient may be incorporated into a cream consisting of an aqueous emulsion of polyethylene glycol or liquid paraffin. The active ingredient may also be incorporated into an ointment consisting of a white wax or white soft paraffin base, in a concentration between 1 and 10% by weight, along with stabilizers and preservatives as needed.

[0235] The injectable form may contain between 10 and 1000 mg of the active ingredient per dose, preferably between 10 and 250 mg.

[0236] The composition may be formulated in unit dose form, that is, in the form of individual portions containing a unit dose, or in multiple or less than one unit dose.

[0237] Those skilled in the art can easily determine an appropriate dose of the composition to be administered to a subject without excessive experimentation. Typically, a physician determines the most appropriate actual dose for an individual patient, which depends on various factors including the activity of the particular compound, its metabolic stability and duration of action, age, weight, overall health, sex, diet, mode and timing of administration, elimination rate, drug combinations, the severity of the individual condition, and the therapy the individual is receiving. The doses disclosed herein are exemplary for the average case. Of course, there may be individual cases where a high dose range is natural, or where a low dose range is natural, and such cases are within the scope of the present invention. If necessary, the drug may be administered in doses of 0.01 to 30 mg / kg of body weight, such as 0.1 to 10 mg / kg, more preferably 0.1 to 1 mg / kg of body weight. In one exemplary embodiment, a single or multiple dose of 10 to 300 mg / day, or more preferably 10 to 150 mg / day, is administered to a patient for the treatment of an inflammatory disorder.

[0238] In one particularly preferred embodiment, the method and use of the present invention involves administering the peptide or composition of the present invention in combination with one or more other active agents, such as existing anti-inflammatory drugs or pharmacological enhancers available on the market. In such cases, the compounds of the present invention may be administered continuously, simultaneously, or sequentially with one or more other active agents.

[0239] In one embodiment of the present invention, the peptide may be administered in the form of a peptide-containing conjugate, which may optionally include a linker and a partner molecule, such as a protein, including an antibody molecule intended to increase the in vivo half-life of the conjugate. In one embodiment, the peptide may be modified by substituting one or more amino acids with amino acids used to conjugate with the partner molecule. For example, an amino acid may be substituted with a lysine residue for the purpose of conjugating a partner molecule such as a PEG molecule.

[0240] definition All publications, patents, patent applications, and other references described herein are specifically and individually referenced so as if each individual publication, patent, or patent application were incorporated by reference, and their entire text is incorporated herein by reference as if their contents were completely enumerated.

[0241] Where used herein, unless otherwise specified, the following terms shall have the following meanings in addition to any broader (or narrower) meanings in which they are used in the art: Unless required by context, the singular form used herein should be read as including the plural form, and vice versa. The terms “a” or “an” used in relation to an entity should be read as referring to one or more of that entity. As such, the terms “a” (or “an”), “one or more” and “at least one” are used synonymously herein.

[0242] In this specification, variations of the term “comprise,” “comprises,” or “comprising” should be read as indicating the inclusion of any enumerated integers (e.g., features, elements, characteristics, properties, methods / process steps, or limitations) or groups of integers (e.g., features, elements, characteristics, properties, methods / process steps, or limitations), but not as to exclude any other integers or groups of integers. Therefore, in this specification, the term “comprising” is inclusive or unrestricted and does not exclude additional unenumerated integers or methods / process steps.

[0243] In this specification, the term “disease” is used to define any abnormal condition that impairs physiological function and is associated with specific symptoms. The term is used more broadly to encompass any disorder, disease, abnormality, pathology, illness, condition, or syndrome in which physiological function is impaired, regardless of its etiology (or whether the causal basis of the disease is actually established). Thus, it includes conditions resulting from infection, trauma, injury, surgery, radiation ablation, poisoning, or malnutrition.

[0244] In this specification, the terms “treatment” or “to treat” refer to an intervention (e.g., administration of a drug to a subject) that cures, relieves, or alleviates the symptoms of a disease, or eliminates (or reduces the impact of) its cause (e.g., reduction of the accumulation of lysosomal enzymes at pathological levels). In this context, the term is used synonymously with the term “therapy.”

[0245] Furthermore, the term “treatment” or “to treat” refers to an intervention (e.g., administration of a drug to a subject) that prevents or delays the onset or progression of a disease, or reduces (or eradicates) its incidence within a treated population. In this case, the term “treatment” is used synonymously with the term “prevention.”

[0246] In this specification, an effective dose or therapeutically effective dose of a drug is defined as the amount that can be administered to a subject with a benefit / risk ratio that is balanced without excessive toxicity, irritation, allergic reactions, or other problems or complications, but is sufficient to provide the desired effect, e.g., treatment or prevention indicated by permanent or temporary improvement of the subject's condition. The dose varies from subject to subject depending on the individual's age and overall condition, mode of administration, and other factors. Therefore, it is not possible to determine an exact effective dose, but those skilled in the art will be able to determine an appropriate “effective” dose in any individual case using routine experiments and general background knowledge. In this regard, therapeutic outcomes include eradication or relief of symptoms, reduction of pain or discomfort, extension of survival, improvement of mobility, and other markers of clinical improvement. The therapeutic outcome does not necessarily have to be a complete cure.

[0247] The term "human or animal" should be understood to mean humans, mammals, or non-mammals such as fish.

[0248] The term "composition" should be understood to mean a composition of substances that are produced by human hands and do not exist in nature. Exemplary compositions include food compositions, beverage compositions, pharmaceutical compositions, nutritional supplement compositions, personal care compositions, and healthcare compositions.

[0249] As used herein, the term "peptide" typically refers to a polymer composed of 5 to 50 amino acid monomers via peptide bond linkage. The peptides of the present invention and for use herein (including their fragments and variants) may be prepared entirely or partially by chemical synthesis or by expression from nucleic acids. For example, the peptides of the present invention and for use herein may be readily prepared according to well-established, standard liquid-phase or, preferably, solid-phase peptide synthesis methods known in the art (see, for example, Non-Patent Document 15). Where necessary, any of the peptides used herein may be chemically modified to increase their stability. Chemically modified peptides or peptide analogs include any functional chemical equivalents of the peptides characterized by their increased stability and / or efficacy in vivo or in vitro with respect to the implementation of the present invention. The term peptide analog also refers to any amino acid derivative of the peptides described herein. Peptide analogs may be prepared by procedures including, but are not limited to, modification of side chains, incorporation of non-natural amino acids and / or derivatives during peptide synthesis, and the use of crosslinking agents and other methods that impose conformational constraints on the peptide or its analogue. Examples of side-chain modifications include reductive alkylation by reaction with an aldehyde followed by reduction with NaBH4, amidation with methyl acetimidate, acetylation with acetic anhydride, carbamylation of the amino group with cyanate, trinitrobenzylation of the amino group with 2,4,6-trinitrobenzenesulfonic acid (TNBS), alkylation of the amino group with succinic anhydride and tetrahydrophthalic anhydride, and modification of the amino group by pyridoxylation of lysine with pyridoxa-5'-phosphate followed by reduction with NABH4. The guanidino group of the arginine residue can be modified by the formation of heterocyclic condensation products using reagents such as 2,3-butanedione, phenylglyoxal, and glyoxal. The carboxyl group can be modified by carbodiimide activation by o-acyl isourea formation followed by subsequent derivatization to, for example, the corresponding amide.The sulfhydryl group can be modified by methods such as carboxymethylation using iodoacetic acid or iodoacetamide, performation oxidation to cysteic acid, formation of mixed disulfides using other thiol compounds, reaction with maleimide, maleic anhydride or other substituted maleimides, formation of mercury derivatives using 4-chloromercurybenzoic acid, 4-chloromercuryphenylsulfonic acid, phenylmercury chloride, 2-chloromercury-4-nitrophenol and other mercury compounds, and carbamylation using cyanate at an alkaline pH. The tryptophan residue can be modified, for example, by oxidation using N-bromosuccinimide or alkylation of the indole ring using 2-hydroxy-5-nitrobenzyl bromide or sulfonyl halides. The tyrosine residue can be modified by nitration using tetranitromethane to form 3-nitrotyrosine derivatives. Modification of the imidazole ring of histidine residues can be achieved by alkylation using iodoacetic acid derivatives or N-carbethoxylation using diethyl pyrocarbonate. Examples of incorporating non-natural amino acids and derivatives in peptide synthesis include, but are not limited to, norleucine, 4-aminobutyric acid, 4-amino-3-hydroxy-5-phenylpentanoic acid, 6-aminohexanoic acid, t-butylglycine, norvaline, phenylglycine, ornithine, sarcosine, 4-amino-3-hydroxy-6-methylheptanoic acid, 2-thienylalanine, and / or the use of D-isomers of amino acids. Peptide structure modification includes the generation of retroinversopeptides containing the reverse sequence encoded by the D-amino acid.

[0250] The term “modified peptide” is used synonymously with the term “peptide derivative.” A modified peptide includes peptides that are substituted with one or more groups as defined herein. The modification may be any modification that provides the peptide and / or composition of the present invention with increased ability to penetrate cells. The modification may be any modification that increases the half-life of the composition or peptide of the present invention. In one embodiment, the group is a protecting group. The protecting group may be an N-terminal protector, a C-terminal protector, or a side-chain protector. A peptide may have one or more of these protecting groups. Those skilled in the art are aware of suitable techniques for reacting amino acids with these protecting groups. These groups may be added by preparation methods known in the art, for example, by the methods outlined in paragraphs

[0104] to

[0107] of Patent Document 19. The group may remain on the peptide or be removed. Protecting groups may be added during synthesis. In one embodiment of the present invention, the peptide may be substituted with one or more hydroxyl, amino, aminoacyl, sulfate, or sulfide groups having 1 to 29 carbon atoms, or unsubstituted, saturated or unsaturated, linear or branched, long or short chains. The N-acyl derivatives include acyl groups derived from acetic acid, capric acid, lauric acid, myristic acid, octanoic acid, palmitic acid, stearic acid, behenic acid, linoleic acid, linolenic acid, lipoic acid, oleic acid, isostearic acid, elaidic acid, 2-ethylhexanoic acid, coconut oil fatty acids, tallow fatty acids, hydrogenated tallow fatty acids, palm kernel fatty acids, lanolin fatty acids, or similar acids. These may be substituted or unsubstituted. If substituted, they are preferably substituted with hydroxyl or, but not limited to, sulfur-containing groups such as SO3H, SH, or SS. In one embodiment of the present invention, the peptide is R1-X-R2. The R1 and / or R2 groups are linked to the amino terminus (N-terminus) and carboxyl terminus (C-terminus) of the peptide sequence, respectively. In one embodiment, the peptide is R1-X, or the peptide is X-R2. Preferably, R1 is H, C 1~4is alkyl, acetyl, benzoyl or trifluoroacetyl, X is the peptide of the present invention, and R2 is OH or NH2. In one embodiment, R1 is selected from the group consisting of H, an acyclic substituted or unsubstituted aliphatic group, a substituted or unsubstituted alicyclyl, a substituted or unsubstituted heterocyclyl, a substituted or unsubstituted heteroarylalkyl, a substituted or unsubstituted aryl, a substituted or unsubstituted aralkyl, t-butyloxycarbonyl, 9-fluorenylmethyloxycarbonyl (Fmoc) and R5-CO-, where R5 is selected from the group consisting of H, an acyclic substituted or unsubstituted aliphatic group, a substituted or unsubstituted alicyclyl, a substituted or unsubstituted aryl, a substituted or unsubstituted aralkyl, a substituted or unsubstituted heterocyclyl and a substituted or unsubstituted heteroarylalkyl, R2 is selected from the group consisting of -NR3R4, -OR3 and -SR3, where R3 and R4 are independently selected from the group consisting of H, an acyclic substituted or unsubstituted aliphatic group, a substituted or unsubstituted alicyclyl, a substituted or unsubstituted heterocyclyl, a substituted or unsubstituted heteroarylalkyl, a substituted or unsubstituted aryl and a substituted or unsubstituted aralkyl, with the condition that R1 and R2 are not α-amino acids. According to another preferred embodiment, R2 is -NR3R4, -OR3 or -SR3, where R3 and R4 are independently H, substituted or unsubstituted C1-C 24 alkyl, substituted or unsubstituted C2-C 24 alkenyl, t-butyloxycarbonyl, 9-fluorenylmethyloxycarbonyl (Fmoc), substituted or unsubstituted C2-C 24 alkynyl, substituted or unsubstituted C3-C 24 cycloalkyl, substituted or unsubstituted C5-C 24 cycloalkenyl, substituted or unsubstituted C8-C 24 cycloalkynyl, substituted or unsubstituted C6-C 30 aryl, substituted or unsubstituted C7-C 24The group is selected from aralkyls, 3-10 membered substituted or unsubstituted heterocyclyl rings, and substituted or unsubstituted heteroarylalkyls formed by 2-24 carbon atoms and 1-3 non-carbon atoms, where the alkyl chain has 1-6 carbon atoms. Optionally, R3 and R4 may be linked by saturated or unsaturated carbon-carbon bonds to form a ring with a nitrogen atom. More preferably, R2 is -NR3R4 or -OR3, where R3 and R4 are independently H, substituted or unsubstituted C1-C 24 Alkyl, substituted, or unsubstituted C2-C 24 Alkenyl, substituted or unsubstituted C2-C 24 Alkinyl, substituted or unsubstituted C3-C 10 Cycloalkyl, substituted or unsubstituted C6-C 15 R3 and R4 are selected from the group formed by aryls and 3- to 10-membered substituted or unsubstituted heterocyclines, substituted or unsubstituted heteroarylalkyls having a 3 to 10-membered ring, and alkyls with 1 to 6 carbon atoms. More preferably, R3 and R4 are selected from the group formed by H, methyl, ethyl, hexyl, dodecyl, or hexadecyl. Even more preferably, R3 is H, and R4 is selected from the group formed by H, methyl, ethyl, hexyl, dodecyl, or hexadecyl. In a more preferred embodiment, R2 is selected from -OH and -NH2.

[0251] According to another embodiment of the present invention, R1 is selected from the group formed by H, acetyl, lauroyl, myristoyl, or palmitoyl, and R2 is -NR3R4 or -OR3, where R3 and R4 are independently selected from H, methyl, ethyl, hexyl, dodecyl, and hexadecyl, preferably R2 is -OH or -NH2. More preferably R1 is acetyl or palmitoyl, and R2 is -NH2. In a preferred embodiment, the acyl group is bonded to the N-terminus of at least one amino acid of the peptide. In one embodiment of the present invention, the peptide is modified to include a side-chain protecting group. The side-chain protecting group may be one or more of a benzyl-containing or benzyl-based group, a t-butyl-based group, a benzyloxycarbonyl (Z) group, and an allyloxycarbonyl (alloc) protecting group. The side-chain protecting group may be derived from an achiral amino acid such as achiralglycine. The use of achiral amino acids helps stabilize the resulting peptide and also facilitates the convenient synthetic route of the present invention. Preferably, the peptide further comprises a modified C-terminus, preferably an amidated C-terminus. The achiral residue may be α-aminoisobutyric acid (methylalanine). It will be understood that the specific side-chain protecting group used depends on the peptide sequence and the type of N-terminal protecting group used.

[0252] "Conjugate": In one embodiment of the present invention, a peptide is conjugated, linked, or fused to a binding partner, such as one or more polyethylene glycol polymers or other compounds such as molecular weight increasing compounds or lipophilic groups. The molecular weight increasing compound is any compound that increases the molecular weight, typically by 10% to 90% or 20% to 50% of the resulting conjugate, and may have a molecular weight between 200 and 20,000, preferably between 500 and 10,000. The molecular weight increasing compound may be PEG, any water-soluble (amphiphilic or hydrophilic) polymer moiety, homo or copolymer of PEG, monomethyl-substituted polymer of PEG (mPEG) and polyoxyethylene glycerol (POG), polyamino acids such as polylysine, polyglutamic acid, and polyaspartic acid, particularly those in L-conformation, pharmacologically inactive proteins such as albumin, gelatin, fatty acids, polysaccharides, lipid amino acids and dextran. The polymer portion may be linear or branched and may have molecular weights of 500 to 40,000 Da, 5,000 to 10,000 Da, or 10,000 to 5,000 Da. The compound (binding partner) may be any suitable cell-permeable compound such as tat peptide, penetratin, or pep-1. The compound (binding partner) may be an antibody molecule. The compound (binding partner) may be a lipophilic portion or a polymer portion. Lipophilic substituents and polymer substituents are known in the art. Lipophilic substituents include N, O, or S atoms that form part of an acyl group, sulfonyl group, ester, sulfonyl ester, thioester, amide, or sulfonamide. The lipophilic portion may contain a hydrocarbon chain having 4 to 30 carbon atoms, preferably between 8 and 12 carbon atoms. It may be linear or branched, saturated or unsaturated. The hydrocarbon chain may be further substituted. It may be a cycloalkane or heterocycloalkane. Peptides can be modified at the N-terminus, C-terminus, or both. The polymer or compound (binding partner) is preferably linked to an amino, carboxyl, or thio group and can be linked by the N-terminus or C-terminus of the side chain of any amino acid residue.A polymer or compound (binding partner) can be conjugated to the side chain of any suitable residue. A polymer or compound (binding partner) can be conjugated via a spacer. The spacer may be a natural or non-natural amino acid, succinic acid, lysyl, glutamyl, asparagyl, glycyl, β-alanyl, or γ-aminobutanoyl. A polymer or compound (binding partner) can also be conjugated via esters, sulfonyl esters, thioesters, amides, carbamates, urea, or sulfonamides. Those skilled in the art will be aware of suitable means for preparing the described conjugates.

[0253] A "fragment" refers to a protein segment selected from Sequence IDs 1 to 14, which is typically a sequence of 7 to 37 amino acids in length, generally having a charge between -9 and +3, a C-terminal amino acid that is not cysteine ​​(C) or methionine (M), and an N-terminal amino acid that is not cysteine ​​(C), histidine (H), proline (P), or threonine (T). The charge of a peptide, fragment, or region is determined using the method described in Non-Patent Document 16.

[0254] The term “natural,” as applied to peptides, means (a) plant proteins, typically rice or pea proteins or variants of pea proteins including lentils, sweet peas or chickpeas, or fragments of rice proteins including oats, grass, maize, wild rice and bananas, or (b) fragments of plant proteins, such as peptides comprising variants of plant protein homolog fragments. The peptides or fragments of the present invention can be isolated from plant proteins or can be produced by synthesis using methods known to those skilled in the art and described herein.

[0255] In the context of a fragment, the "C-terminal domain" refers to the first three amino acids at the c-terminus of the fragment.

[0256] In the context of a fragment, the "N-terminal domain" refers to the last three amino acids at the n-terminus of the fragment.

[0257] As applied to peptides or fragments, “bioactivity” means that when administered to mammals, they have one or more health-promoting effects, such as promoting glucose transport, antibacterial properties, anti-inflammatory properties, or promoting cell growth or proliferation. In one embodiment, the term “bioactivity” means cell growth-promoting properties.

[0258] The terms "growth-promoting" or "growth-promoting activity," as applied to a peptide or fragment, mean a peptide or fragment capable of increasing elastin production or cell proliferation in human skin treated with a 20 μM solution of the peptide or fragment, as described in the assays below.

[0259] The terms "glucose transport-enhancing" or "glucose transport-enhancing activity," as applied to peptides, variants, or fragments, refer to peptides, variants, or fragments capable of increasing GLUT4 translocation to skeletal muscle compared to untreated controls when used at a concentration of 2 μM in the following in-vitro assays. L6-GLUT4myc cells were grown in 10% FBS and 2 μg / ml blastosidine. The cells were grown for 48–72 hours, then seeded in 2% FBS at 15,000 cells per well in 24-well plates and differentiated for 6–8 days prior to the experiment. L6-GLUT4myc cells were serum-deficient for 3 hours, then incubated with 100 nM insulin for 30 minutes or with 200, 20, 2.0, and 0.2 μM SP and peptide / peptide compositions of 2, 1, 0.5, and 0.25 mg / ml, respectively, for 3 hours. The 3-hour incubation period was chosen based on previous findings that 3-hour incubation with branched-chain amino acids containing dipeptides increases glucose uptake in L6 myotubes. The treatments were staggered to determine the GLUT4myc migration location at the same time point. The amount of myc-tagged GLUT4 on the cell surface was measured by a colorimetric assay coupled with an antibody. Briefly, L6-GLUT4myc cells were fixed by incubation with 3% paraformaldehyde (PFA) after either 30 minutes of incubation with insulin or 3 hours each with synthetic peptides or peptide compositions. The PFA was then quenched with 0.1 M glycine solution, and the cells were blocked with 5% goat serum. Myotube monolayers were exposed to anti-myc antibody and then incubated with donkey anti-mouse IgG conjugated with peroxidase. Each well was treated by adding 1 mL of o-phenylenediamine dihydrochloride (OPD) reagent and stopping the reaction by adding 250 μl / well of 3 M HCl. To determine the GLUT4 translocation to the cell surface, the measured aliquots for each condition were spectrophotometrically examined using a plate reader with absorbance at 492 nm.Preferably, the peptide or fragment can increase GLUT4 translocation by at least 50% (i.e., a relative unit increase in GLUT4 translocation from 1% to 1.5%) compared to an untreated control.

[0260] "Antibacterial" or "antibacterial activity" as applied to a peptide or fragment means a peptide or fragment that can visibly inhibit the growth of bacteria in the following agar plate-based growth inhibition assay: Peptide stock = 5 mg / mL dissolved in DMSO. Bacterial inoculum was adjusted to McFarland 0.5 standard and spread on MHA plates. Blank disks were placed on the plates and 10 μl of each compound (64 μg / mL - the maximum concentration tested) was added. The plates were incubated at 37 °C for 16 - 18 hours. Appropriate controls (DMSO; Mueller - Hinton medium alone; and two antibiotic disks - ciprofloxacin and tetracycline) were also performed.

[0261] "Anti - inflammatory" as applied to a peptide or fragment means a peptide or fragment that can significantly reduce the secretion of TNFα by J774.2 macrophages stimulated with LPS (compared to J774.2 macrophages stimulated with untreated LPS) when the macrophages are treated with 100 μΜ of the peptide or fragment. J774.2 macrophages were treated with 100 μΜ of the synthetic peptide for 24 hours and then stimulated with (A) LPS (10 ng / ml) for 5 hours or (B) LPS (10 ng / ml) for 5 hours followed by ATP (5 mM) for another 1 hour. Supernatants were collected and the levels of TNFα were determined by ELISA.

[0262] "Rich in peptides having a molecular weight of less than 10 KD" as applied to the compositions of the present invention means that the dry weight percentage of peptides in the composition having a molecular weight of less than 10 KD is greater than the dry weight percentage of polypeptides / proteins in the composition having a molecular weight of 10 KD or more.

[0263] The "homologous" of a reference protein must be understood to mean a protein derived from a different plant species that has at least 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence homology to the reference protein. Therefore, for example, homologs of the pea protein P13918 include: >gi|137584|sp|P08438.1|VCL_VICFA RecName:Full=Vicillin;Flags:Precursor [Broad bean (Vicia faba)] >gi|22057|emb|CAA68559.1|Bicilin [Fava bean minor variety]>gi|383931031|gb|AFH56916.1|Bicilin [Fava bean] >gi|502105533|ref|XP_004492829.1|PREDICTED:Bicillin-like isotype X1 [Chickpea] Chickpea >gi|29539109|emb|CAD87730.1|Allergen Len c1.0101[Lentils]Lentils It includes.

[0264] The term "mutant" of a growth-promoting fragment should be understood to mean a fragment having an amino acid sequence substantially identical to that of a reference growth-promoting fragment and possessing the growth-promoting activity described above. Therefore, for example, the term should be understood to include fragments in which one or more amino acid residues have been modified. Preferably, such modifications include insertions, additions, deletions, and / or substitutions of five or fewer amino acids, more preferably four or fewer, even more preferably three or fewer, and most preferably just one or two amino acids. Insertions, additions, and substitutions using native and modified amino acids are possible. A mutant may have a conserved amino acid modification, in which case the introduced amino acid is structurally, chemically, or functionally similar to the substituted one. Generally, a mutant has at least 70% amino acid sequence homology with the reference growth-promoting fragment, preferably at least 80%, more preferably at least 90%, and ideally at least 95%, 96%, 97%, 98%, or 99% sequence homology.

[0265] In this specification, the term “sequence identity” should be understood to include both sequence identity and similarity; that is, a variant (or homolog) that shares 70% sequence identity with a reference sequence is one in which any 70% of the aligned residues of the variant (or homolog) are identical to or conserved substitutions of the corresponding residues in the reference sequence over the entire length of the sequence. Sequence identity is the amount of exactly corresponding letters between two different sequences. As a result, gaps are not counted, and the measurement is relevant to the shorter of the two sequences. With respect to “sequence homology,” this term should be understood to mean a variant (or homolog) that shares a defined percentage of similarity or identity with a reference sequence if the percentage of aligned residues of the variant (or homolog) is either identical to or conserved substitutions of the corresponding residues in the reference sequence, and the variant (or homolog) shares identical function with the reference sequence. This alignment and homology or sequence identity percentage can be determined using software programs known in the art, for example, BLAST, which uses default parameters, as one alignment program. Details of these programs can be found at the following internet address: http: / / www.ncbi.nlm.nih.gov / blast / Blast.cgi. A variant of sequence number 448 (QSFLLSGNQ) The following provides variants of Sequence ID No. 448 (QSFLLSGNQ) that include variants having one or two conserved amino acid substitutions, one, two to three non-conservative amino acid substitutions, one or two amino acid additions, or one, two, or three amino acid deletions: One conservative amino acid substitution: QSFILSGNE, ESFLLSGNQ, QSYLLSGNQ, QSFLLSGDQ (Sequence IDs 418-421) Two conservative amino acid substitutions: QSYLLSGNE, ESFLLSGNE, ESYLLSGNQ, QSFLLSGDE, QSYLLSGDQ (Sequence codes 422 to 426) One non-conservative amino acid substitution QSFRLSGNQ, QSFLLSYNQ, QFFLLSGNQ, QSFLLSGAQ, QSFLLSGNP (Sequence IDs 427 to 431) Two non-conservative amino acid substitutions QSFRRSGNQ, QSFLLSYIQ, QFFLLSGNL, ​​QSFLLSGAQ, QSFLLSGNP (Sequence IDs 432 to 436) Addition of one or two amino acids QSFLLSGNQQ, QSFLLLSGNQ, AQSFGLLSGNQ, RQSFLLISGNQ, QSFLLSGNQK (Sequence IDs 437 to 441) One, two, or three amino acid deletions QFLLSGNQ, SFLLSGNQ, QSFLLSGN, QSFLLGNQ, QSFLSGNQ, QSLLSGNQ, SFLLSGNQ, QSFLLSGN, SFLLSGN, QSFSGNQ (Sequence codes 442 to 451) The term “mutant” also includes a fragment of the peptide of the present invention. “Peptide fragment of the present invention” or “peptide fragment” means one fragment of the peptide of the present invention having at least 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, or 22 amino acids and typically having biological activity, such as anti-inflammatory activity, anti-aging activity, glucose transport-promoting activity, or antibacterial activity. In one embodiment, the fragment consists of at least 30%, 40%, 50%, 60%, 70%, 80%, or 90% of the reference sequence. Therefore, the present invention also provides biologically active fragments of the peptide of the present invention and peptides comprising one or more of these fragments. In one embodiment, the fragment is biologically active. In one embodiment, the fragment is a cell growth or proliferation-promoting fragment. Examples of peptide fragments of the present invention are provided in SEQ ID NOs: 494 to 524.

[0266] "Anti-aging" means inhibiting or slowing down the appearance of aging in human skin and / or reversing the appearance of aging. "Slowing down or inhibiting skin aging" means slowing down or inhibiting the aging process in skin and / or reversing the appearance of aging.

[0267] "A disease or condition characterized by damaged dermal or epithelial cells or tissues" means any condition or disease that results in damaged dermal or epithelial tissue or cells or organs. One example is trauma, which often results in damaged skin. Another example is inflammatory skin conditions such as psoriasis or eczema, which often results in damaged skin. Another example is inflammatory disorders of the lower intestine, which can result in damaged epithelial cells / tissue lining the inside of the lower intestine. Another example is damaged epithelial cells / tissue lining the inside of the lower intestine, caused by oral ingestion of toxic or damaging substances, such as toxic chemicals or drugs. Another example is cancer, such as colon cancer, which can result in damaged epithelial tissue in the intestine. Another condition is peripheral inflammatory disorders, such as atopic dermatitis, which can result in damage to the skin in humans.

[0268] "Inflammatory disorders" refer to immune-mediated inflammatory conditions affecting humans, generally characterized by dysregulation of one or more cytokines. Examples of inflammatory disorders include skin inflammatory disorders, joint inflammatory disorders, cardiovascular inflammatory disorders, certain autoimmune diseases, lung and airway inflammatory disorders, and intestinal inflammatory disorders. Examples of skin inflammatory disorders include dermatitis, e.g., atopic dermatitis and contact dermatitis, acne vulgaris, and psoriasis. Examples of joint inflammatory disorders include rheumatoid arthritis. Examples of cardiovascular inflammatory disorders include cardiovascular diseases and atherosclerosis. Examples of autoimmune diseases include type 1 diabetes, Graves' disease, Guillain-Barré disease, lupus, psoriatic arthritis, and ulcerative colitis. Examples of lung and airway inflammatory disorders include asthma, cystic fibrosis, COPD, emphysema, and acute respiratory distress syndrome. Examples of intestinal inflammatory disorders include colitis and inflammatory bowel disease. Other inflammatory disorders include cancer, hay fever, periodontitis, allergies, hypersensitivity, ischemia, depression, systemic diseases, post-infection inflammation, and bronchitis. The present invention also relates to peptides or compositions of the present invention for use in the treatment of inflammatory disorders in mammals.

[0269] "Metabolic disorders" should be understood to include prediabetes, diabetes, type 1 diabetes, type 2 diabetes, metabolic syndrome, obesity, diabetic dyslipidemia, hyperlipidemia, hypertension, hypertriglyceridemia, hyperfattyacidemia, hypercholesterolemia, hyperinsulinemia, and MODY. The present invention also relates to peptides or compositions of the present invention for use in the treatment of metabolic disorders in mammals.

[0270] "A disease or condition characterized by damaged dermal or epithelial cells or tissues" means any condition or disease that results in damaged dermal or epithelial tissue or cells or organs. One example is trauma, which often results in damaged skin. Another example is inflammatory skin conditions such as psoriasis or eczema, which often results in damaged skin. Another example is inflammatory disorders of the lower intestine, which can result in damaged epithelial cells / tissue lining the inside of the lower intestine. Another example is damaged epithelial cells / tissue lining the inside of the lower intestine, caused by oral ingestion of toxic or damaging substances, such as toxic chemicals or drugs. Another example is cancer, such as colon cancer, which can result in damaged epithelial tissue in the intestine. Another condition is peripheral inflammatory disorders such as atopic dermatitis, which can result in damage to the skin in humans.

[0271] "A disease or condition characterized by bacterial infection" means any condition or disease characterized by having a pathology caused by bacterial growth or bacterial infection, including, for example, MRSA, Salmonella, Listeria, bacterial pneumonia, staphylococcal food poisoning, and bacterial meningitis. Specific examples are provided at https: / / en.wikipedia.org / wiki / List_of_infectious_diseases.

[0272] It must be understood that "artificial" substances, as applied to edible products, mean that they are created by humans and do not exist in nature.

[0273] Maintaining or restoring gut health means reducing and / or regulating pro-inflammatory responses in the gut, more specifically, in the epithelial cells. A healthy microbiome provides some protection from pathogenic viruses and bacteria, and its presence is necessary to guide the development of our immune system. These bacteria have been shown to be manifested by inflammation and, as a result, can react to human signals of stress, illness, or age, which can switch on their pathogenic genes and cause or contribute to disease. Having the ability to reduce and maintain inflammatory responses at healthy levels can help maintain healthy bacteria. Digestive problems, including the number one health issue in North America, appear to be occurring more frequently in recent years. One way to maintain digestive health is to maintain proper inflammation and gut flora.

[0274] "Improving muscle condition" means improving muscle health, such as skeletal muscle protein synthesis, enhanced glucose absorption by the skeleton, improved lean tissue mass in therapeutic or non-therapeutic situations, generally accelerated muscle recovery after strenuous exercise, or improved muscle performance. Methods or uses may be therapeutic or non-therapeutic. The term "improving lean tissue condition" should be understood to mean increasing lean tissue mass or inhibiting or preventing the rate of lean tissue breakdown.

[0275] "Promoting muscle recovery" means causing increased glucose absorption in skeletal muscle compared to untreated skeletal muscle.

[0276] "A disease or condition characterized by somnolence or low energy levels" means any condition or disease characterized by mood or fatigue or low energy. Examples include allergies, asthma, anemia, cancer and its treatment, chronic pain, heart disease, infections, depression, eating disorders, mourning, sleep disorders, thyroid problems, medication side effects, alcohol use or drug use.

[0277] "Maintaining or restoring muscle health" means being useful for maintaining or restoring the health of mammalian muscle resulting from injury received during exercise. The peptides promote recovery from exercise by promoting glucose transport in skeletal muscle and reduce muscle pain / pain and injury associated with exercise. They can also be used to reduce muscle spasms and to allow for more rapid recovery from muscle spasms in order to prevent them. Spasms can be caused by physical stress, mental stress and / or repetitive strain injury stress. By promoting glucose transport, the peptides are useful for reducing muscle muscle diseases in mammals and for preventing sarcopenia in mammals, promoting recovery from injury during exercise, and reducing muscle pain / pain and injury associated with exercise. The present invention also relates to the peptides or compositions of the present invention for use in maintaining or restoring muscle health in mammals

[0278] As applied to the list of peptides herein, the term "substantially all" must be understood to mean at least 60%, 70%, 80%, 90% or 95% of the peptides.

[0279] "Artificial", as applied to an edible product, must be understood to mean made by humans and not occurring in nature.

Brief Description of the Drawings

[0280] [[ID=K19]] [Figure 1] It is a figure showing the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDF). [Figure 2]This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 3] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 4] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 5] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 6] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 7] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 8] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 9] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 10] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 11] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 12] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 13] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 14] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 15] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 16] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 17] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 18] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 19] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 20] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 21] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 22] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 23] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 24] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 25] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 26] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 27] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 28] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 29] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 30] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 31]This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 32] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 33] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 34] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 35] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 36] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 37] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 38] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 39] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 40] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 41] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 42] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 43] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 44] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 45] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 46] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 47] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 48] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 49] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 50] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 51] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 52] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 53] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 54] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 55] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 56] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 57] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 58] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 59] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 60]This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 61] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 62] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 63] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 64] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 65] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 66] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 67] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 68] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 69] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 70] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 71] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 72] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 73] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 74] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 75] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 76] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 77] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 78] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 79] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 80] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 81] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 82] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 83] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 84] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 85] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 86] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 87] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 88] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 89]This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 90] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 91] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 92] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 93] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 94] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 95] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 96] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 97] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 98] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 99] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 100] This figure shows the effect of the synthetic peptide of the present invention on the proliferation of human dermal fibroblasts (HDFs). [Figure 101] This figure shows the effect of the synthetic peptide (SEQ ID NO: 42) of the present invention on elastin synthesis in human dermal fibroblasts (HDF). [Figure 102] This figure shows the effect of the synthetic peptide (SEQ ID NO: 42) of the present invention on collagen synthesis in human dermal fibroblasts (HDFs). [Figure 103]This figure shows the effect of the synthetic peptide (SEQ ID NO: 701) of the present invention on elastin synthesis in human dermal fibroblasts (HDFs). [Figure 104] This figure shows the effect of the synthetic peptide (SEQ ID NO: 701) of the present invention on collagen synthesis in human dermal fibroblasts (HDF). [Figure 105] This figure shows the effect of the synthetic peptide (SEQ ID NO: 246) of the present invention on elastin synthesis in human dermal fibroblasts (HDFs). [Figure 106] This figure shows the effect of the synthetic peptide (SEQ ID NO: 246) of the present invention on collagen synthesis in human dermal fibroblasts (HDFs). [Figure 107] This figure shows the effect of the synthetic peptide (SEQ ID NO: 284) of the present invention on elastin synthesis in human dermal fibroblasts (HDFs). [Figure 108] This figure shows the effect of the synthetic peptide (SEQ ID NO: 245) of the present invention on elastin synthesis in human dermal fibroblasts (HDFs). [Figure 109] This figure shows the effect of the synthetic peptide (SEQ ID NO: 245) of the present invention on collagen synthesis in human dermal fibroblasts (HDFs). [Figure 110] This figure shows the completeness control and viability control of the assay system. [Figure 111] This figure shows the percentage of elastin expression in the superficial dermis for peptides P1, P2, and P3 compared to a control (water or DMSO). It shows a significant increase in elastin expression in the superficial and intermediate dermis. [Figure 112] This figure shows the percentage of elastin expression in the intermediate dermis for peptides P1, P2, and P3 compared to a control (water or DMSO). *Significant increase in elastin expression in the superficial and intermediate dermis. [Figure 113] This figure shows the percentage of cell proliferation in the basal layer of the epidermis compared to a control (water or DMSO) for peptides P6 and P8 and peptide compositions P9 and P10. *Significant increase is shown. [Figure 114-1]This figure shows the histological analysis of elastic fibers (+catechin, x200). [Figure 114-2] This figure shows the histological analysis of elastic fibers (+catechin, x200). [Figure 115-1] This figure shows the immunohistochemical evaluation of the mitotic index (Ki67, x400). [Figure 115-2] This figure shows the immunohistochemical evaluation of the mitotic index (Ki67, x400). [Modes for carrying out the invention]

[0281] Detailed description of the present invention [Examples]

[0282] Cell proliferation assay BrDu is incorporated into newly synthesized DNA strands in actively proliferating cells. After partial denaturation of double-stranded DNA, BrDu can be detected immunochemically, enabling evaluation of the population of cells synthesizing DNA.

[0283] Human dermal fibroblasts (HDF-Sigma 10605a) were seeded at a rate of 10,000 cells per well in DMEM containing 10% fetal bovine serum (FCS), 1% Pen / strep, and 1% L-glutamine, and allowed to adhere for 24 hours.

[0284] After the initial 24-hour incubation, the cells were incubated for another 24 hours with synthetic peptides at concentrations of 5 μg / ml, 0.5 μg / ml, or 0.05 μg / ml, respectively.

[0285] After incubation with synthetic peptides for 18 hours, 20 μl of BrDu reagent was added to each well. After incubation for 24 hours, the cells were fixed and the amount of 2-DG6P was measured using the BrdU cell proliferation assay, with all steps performed according to the manufacturer's instructions for use.

[0286] Results were calculated as a percentage of the untreated control. Increased optical density readings indicate greater BrDu incorporation and increased cell proliferation.

[0287] The results are shown in Figures 1-100 and Table 1 below.

[0288] [Table 1-1]

[0289] [Table 1-2] [Examples]

[0290] Collagen production assay Hydroxyproline in tissue preparation is a direct measure of the amount of collagen present. The FIRELISA human hydroxyproline ELISA kit assay is designed to measure hydroxyproline in tissue or peptide compositions.

[0291] Human dermal fibroblasts (HDF Sigma 10605a) were seeded at a rate of 50,000 cells per well in DMEM containing 10% fetal bovine serum (FCS), 1% Pen / strep, and 1% L-glutamine, and allowed to adhere for 24 hours.

[0292] After the initial 24-hour incubation, the cells were incubated for 96 hours with synthetic peptides at concentrations of 5 μg / ml, 1 μg / ml, or 0.1 μg / ml, respectively.

[0293] After treatment, cells were lysed using four freeze-thaw cycles in liquid nitrogen. The lysed cells were centrifuged, and each supernatant was assayed at 50 μl / ml using the FIRELISA Human Elastin ELISA Kit. All steps were performed according to the manufacturer's instructions for use.

[0294] The results were calculated as a percentage of the untreated control. An increase in optical density reading indicates increased collagen content.

[0295] The results are shown in Figures 102, 104, 106, and 109. [Examples]

[0296] Elastin production assay Elastin is a highly elastic protein found in connective tissue, enabling numerous tissues throughout the body to regain their shape after stretching or contraction. The FIRELISA Human Elastin ELISA Kit assay is designed to measure elastin in tissues or protein / peptide compositions.

[0297] Human dermal fibroblasts (HDFs) were seeded at a rate of 50,000 cells per well in DMEM containing 10% fetal bovine serum (FCS), 1% Pen / strep, and 1% L-glutamine in a 24-well plate, and allowed to adhere for 24 hours.

[0298] After the initial 24-hour incubation, the cells were incubated for 96 hours with synthetic peptides at concentrations of 5 μg / ml, 1 μg / ml, or 0.1 μg / ml, respectively.

[0299] After treatment, cells were lysed using four freeze-thaw cycles in liquid nitrogen. The lysed cells were centrifuged, and each supernatant was assayed at 50 μl / ml using the FIRELISA Human Hydroxyproline ELISA Kit. All steps were performed according to the manufacturer's instructions for use.

[0300] The results were calculated as a percentage of the untreated control. An increase in optical density reading indicates increased collagen content.

[0301] The results are shown in Figures 101, 103, 105, 107, 108, and 109. [Examples]

[0302] Elastin and cell proliferation assay

[0303] [Table 2]

[0304] device Incubator, Flow Laminar Chamber, Sterile Polished Plastic Rod, Pipette, Maintenance Medium, 6-well Plate, 24-well Plate.

[0305] reagent MTT, PBS, SDS, formaldehyde, xylene, anhydrous ethanol, Dulbecco's phosphate-buffered saline (DPBS), metal-enhanced DAB substrate kit, ABC peroxidase staining kit, citrate, sodium hydroxide 2N, hydrogen peroxide 30%, anti-filaggrin, anti-rabbit IgG-biotin, Tween 20.

[0306] Testing System Properties: Human skin tissue, 5mm diameter Batch numbers: EXP004050B009 and EXP004050B011 Provided by: Laboratoire Biopredic International-8-18 rue Jean Pecker-35000 Rennes-France. Tel:+33(0)2.99.14.36.14-Fax:+33 (0)2.99.54.44.72. The certificate of analysis is shown in Attachment 1.

[0307] Two batches are used in the assay. Batch EXP004050B005 is used for day 1 of the experiment, and batch EXP004050B006 is used for day 5 of the experiment.

[0308] Maintenance culture medium Maintenance medium: Batch number: MIL 218C Provided by:Laboratoire Biopredic International-8-18 rue Jean Pecker-35000 Rennes-France.

[0309] Tested peptides P1: Sequence ID 283 P2: Sequence ID 246 P3: Sequence ID 284 P4:RPYYSNAPQEIF P5:VLLEQQEQEPQH P6: Sequence ID 245 P7:QQYGIAASPFLQSAA P8: Sequence ID 42

[0310] Tested composition P9(14-CHL-0723-09) is a pea composition (SEQ ID NOs: 50, 85, 74, 140, 82, 136, 189, 77, 169, 149, 171, 178, 143, 127, 190, 141, 147, 133, 186, 125, 122, 119, 87, 90, 86, 89, 138, 1 These are 29, 123, 120, 117, 113, 110, 121, 105, 98, 55, 161, 19, 317, 135, 130, 146, 177, 160, 170, 188, 83, 78, 36, 96, 159, 26, 330, 168, 148, 184, 151, 151, 165, 114, and 284.

[0311] P10 (14-CHL-0723-010) is a rice composition (SEQ ID NOs: 245, 246, 263, 250, 257, 259, 276, 255, 251, 264, 256, 266, 274, 270, 269, 356, 245, 380, 262, 258, 356, 218, 252, 358, 271, 253, 344, 275, 272, 226, 224, 220, 248, 261, 265, 373, 375, 247, 249, 363, 273, 343, 273, 362).

[0312] How to apply Skin grafts were prepared from abdominal reconstructive surgery. Several grafts were degreased with alcohol to obtain dehydrated skin.

[0313] These grafts were maintained for 5 days in maintenance medium supplied by the provider, Biopredic International. The test parameters were applied twice daily using 5 μL per graft.

[0314] At the end of the experiment, viability control was established for two types of grafts using MTT, and a third graft was fixed in 4% formaldehyde for histological and cytological staining.

[0315] Histology is performed on degreased grafts, test items, and grafts treated with DMSO 0.3% control and water control for each analysis (D1 and D5).

[0316] Each skin graft in the maintenance medium is degreased with 5 μL of alcohol for 3 hours after receiving it in the laboratory.

[0317] Three hours later, all skin grafts were treated twice daily with the test item and incubated at 37°C ± 2°C in 5% CO2 for 1 or 5 days.

[0318] The system's integrity is confirmed on days 1 and 5 using a viability control with MTT.

[0319] immunostaining Histology is performed in the Gredeco laboratory, and immunohistochemistry for elastin and Ki67 is performed in the same laboratory. Immunohistochemistry for filaggrin is performed in the Intertek laboratory.

[0320] Elastin (rabbit monoclonal antibody, clone PI5502, LSBio) was detected using a two-layer immunoperoxidase technique (ABC kit, Vector Laboratories) and indicated by AEC (3-amino-9-ethylcarbazole). Immunohistochemical staining intensity in elastic fibers was evaluated using a semi-quantitative histological score.

[0321] Epithelial proliferation was analyzed by immunohistochemistry using an anti-Ki67 antibody. Immunodetection was performed using indirect immunoperoxidase technology (3-layer), amplified (DAKO kit), and labeled with AEC (3-amino-9-ethylcarbazole). The number of labeled cells (keratinocytes in the basal layer of the epidermis) was counted, providing the total number of basal cells and calculating the percentage of labeled cells.

[0322] Specific staining for filaggrin is performed using immunoperoxidase staining (ABC kit, Fisher). The intensity of the immunohistochemical marker in the epidermis is evaluated against a negative control of the solvent (water or 0.3% DMSO).

[0323] C: Result Survival rate comparison Completeness controls and viability controls are shown in Figure 1. These controls allow for confirmation of the assay system. Viability is >50% for the test items, and they do not exhibit cytotoxicity by the test.

[0324] immunostaining Elastin expression Dermal elastic fibers were identified by catechin staining and morphometrically quantified using computer-aided imaging. The area percentage occupied by elastic fibers in the dermis and mean superficial dermis was calculated. The results are shown in Table 1, Figure 2, and Figure 3.

[0325] [Table 3]

[0326] Under the experimental conditions of the study, samples 0723-1 and 0723-3 showed a twofold increase in elastic fibers in the superficial dermis compared to the control water on day 5 (Figure), and an increase in the intermediate dermis compared to the water control.

[0327] Sample 0723-2 shows a twofold increase in the intermediate dermis on day 1 and further increase on day 5 compared to the control water.

[0328] Ki67 expression The results of the immunohistochemical analysis of Ki67 are reported in the table and expressed as the percentage of cells labeled in the basal layer of the epidermis. The figure shows the percentage of Ki67 cells compared to negative controls (water or DMSO). Immunohistochemical analysis of mitotic activity is shown in Appendix 4, along with the average values ​​for each analysis condition.

[0329] [Table 4]

[0330] Under the experimental conditions of the study, test items 0723-06, 0723-08, 0723-09, and 0723-010 showed an increase in the number of dividing cells compared to EGF on day 1. A decrease in the mitotic index was observed on day 5 compared to day 1 for all analyzed conditions.

[0331] This decrease in cell staining on day 5 is induced in the model. In fact, cell turnover is depleted in this model after about 3 days.

[0332] The present invention is not limited to the embodiments described herein, and its configuration and details may be modified without departing from the spirit of the invention.

[0333] Sequence information

[0334] Protein: P13918 - 2 - Pea MAATTMKASFPLLMGISFLASVCVSSRSDPQNPFIFKSNKFQTLFENENGHIRLLQKFDQRSKIFENLQNYRLEYKSKPHTIFLPQHTDADYILVVLSGKAILTVLKPDDR NSFNLERGDTIKLPAGTIAYLVNRDDNEELRVLDLAIPVNRPGQLQSFLLSGNQNQQNYLSGFSKNILEASFNTDYEEIEKVLLEEHEKETQHRRSLKDKRQQSQEENVIVKLSR GQIEELSKNAKSTSKKSVSSESEPFNLRSRGPIYSNEFGKFFEITPEKNPQLQDLDIFVNSVEIKEGSLLLPHYNSRAIVIVTVNEGKGDFELVGQRNENQQEQRKEDDEEEEQG EEEINKQVQNYKAKLSSGDVFVIPAGHPVAVKASSNLDLLGFGINAENNQRNFLAGDEDNVISQIQRPVKELAFPGSAQEVDRILENQKQSHFADAQPQQRERGSRETRDRLSSV [SEQ ID 1]

[0335] Peptide: QNYLSGFSKNILE [SEQ ID 15] Peptide: TIKLPAGTIAYLVNRDDNEE [SEQ ID 16] Peptide: LAIPVNRPGQLQSFL [SEQ ID 17] Peptide: AIPVNRPGQLQ [SEQ ID 18] Peptide: PAGHPVAVK [SEQ ID 19] Peptide: VQNYKAKLSSGDVFVIPAG [SEQ ID 20] Peptide: NNQRNFLAGDEDNVISQIQRPVKE [SEQ ID 21] Peptide: INKQVQNYKAKLSSGDVFVIPAG [SEQ ID 22] Peptide: LAIPVNRPGQ [SEQ ID 23] Peptide: NFLAGDEDNVISQIQRPVKE [SEQ ID 24] Peptide: DLAIPVNRPGQLQSF [SEQ ID 25] Peptide: VIPAGHPVAVK [SEQ ID 26] Peptide: DTIKLPAGTIAYLVNRDDNEE [SEQ ID 27] Peptide: LAIPVNRPGQLQSF [SEQ ID 28] Peptide: KQVQNYKAKLSSGDVFVIPAG [SEQ ID 29] Peptide: RGDTIKLPAGTIAYLVNRDDNEE [SEQ ID 30] Peptide: FLAGDEDNVISQIQRPVKE [SEQ ID 31] Peptide: LAIPVNRPGQLQS [SEQ ID 32] Peptide: VLDLAIPVNRPGQLQ [SEQ ID 33] Peptide: DLAIPVNRPGQLQ [SEQ ID 34] Peptide: VFVIPAGHPVAVK [SEQ ID 35] Peptide: TIFLPQHTDADYILVVLSGK [SEQ ID 36] Peptide: NQRNFLAGDEDNVISQIQRPVKE [SEQ ID 37] Peptide: LAIPVNRPGQLQ [SEQ ID 38] Peptide: HPVAVKASSNLDLLGFG [SEQ ID 39] Peptide: LAIPVNRPGQL [SEQ ID 40] Peptide: DLAIPVNRPGQL [SEQ ID 41] Peptide: SKPHTIFLPQHTDADYILVVLSGK [SEQ ID 42] Peptide: FVIPAGHPVAVK [SEQ ID 43] Peptide: DLAIPVNRPGQLQS [SEQ ID 44] Peptide: SGDVFVIPAGHPVAVKASSNLD [SEQ ID 45] Peptide: AIPVNRPGQLQSF [SEQ ID 46] Peptide: ELAFPGSAQEVDR [SEQ ID 47] Peptide: LAIPVNRPGQLQSFLLSG [SEQ ID 48] Peptide: VFVIPAGHPVAVKASSNLDLLGFG [SEQ ID 49] Peptide: AGHPVAVK [SEQ ID 50] Peptide: HPVAVKASSNLDLLGFGINAE [SEQ ID 51] Peptide: LAIPVNRPGQLQSFLLSGNQNQ [SEQ ID 52] Peptide: SGDVFVIPAG [SEQ ID 53] Peptide: GSLLLPHYNSRAIVIVTVNE [SEQ ID 54] Peptide: NFLAGDEDNVISQIQRPVK [SEQ ID 55] Peptide: SGDVFVIPAGHPVA [SEQ ID 56] Peptide: GSLLLPHYNSRAIVIV [SEQ ID 57] Peptide: RGDTIKLPAGTIAYLVNRDD [SEQ ID 58] Peptide: SGDVFVIPAGHPVAVK [SEQ ID 59] Peptide: LSSGDVFVIPAGHPVAVK [SEQ ID 60] Peptide: LDLAIPVNRPGQL [SEQ ID 61] Peptide: AIPVNRPGQL [SEQ ID 62] Peptide: LAIPVNRPGQLQSFLL [SEQ ID 63] Peptide: PHTIFLPQHTDADYILVVLSGK [SEQ ID 64] Peptide: VFVIPAGHPVAVKASSNLD [SEQ ID 65] Peptide: LAIPVNRPGQLQSFLLS [SEQ ID 66] Peptide: VLDLAIPVNRPGQLQSF [SEQ ID 67] Peptide: AIPVNRPGQLQS [SEQ ID 68] Peptide: DTIKLPAGTIAYLVNRDDNE [SEQ ID 69] Peptide: NYKAKLSSGDVFVIPAG [SEQ ID 70] Peptide: GKAILTVLKPDDRNSFNLE [SEQ ID 71] Peptide: YKSKPHTIFLPQHTDAD[SEQ ID 72] Peptide: ASSNLDLLGFG[SEQ ID 73] Peptide: DEEEEQGEEEINK [SEQ ID 74] Peptide: YKSKPHTIFLPQHTD[SEQ ID 75] Peptide: VLDLAIPVNR[SEQ ID 76] Peptide: FFEITPEKNPQLQDLDIFVNSVEIK[SEQ ID 77] Peptide: TIFLPQHTDADYIL[SEQ ID 78] Peptide: SFLLSGNQNQQNYLSG[SEQ ID 79] Peptide: SFLLSGNQNQQNYLSGFS[SEQ ID 80] Peptide: NQQEQRKEDDEEEEQGEEE[SEQ ID 81] Peptide: EEQGEEEINK [SEQ ID 82] Peptide: SRGPIYSNE[SEQ ID 83] Peptide: EDDEEEEQGEEEINK[SEQ ID 84] Peptide: DDEEEEQGEEEINK[SEQ ID 85] Peptide: KEDDEEEEQGEEEIN [SEQ ID 86] Peptide: KEDDEEEEQGEE [SEQ ID 87] Peptide: QRKEDDEEEEQGEEE[SEQ ID 88] Peptide: KEDDEEEEQGEEEINK[SEQ ID 89] Peptide: KEDDEEEEQGEEE[SEQ ID 90]

[0336] Protein: Q9M3X6 - 3 - Pea MATTIKSRFPLLLLLGIIFLASVVCVTYANYDEGSEPRVPAQRERGRQEGEKEEKRHGEWRPSYEKEEDEEEGQRERGRQEGEKEEKRHGEWRPSYEKQEDEEEKQKYRYQREKEDEEEKQKYQYQREKKEQKEVQPGRERWEREEDEEQVDE EWRGSQRREDPEERARLRHREERTKRDRRHQREGEEEERSSESQERRNPFLFKSNKFLTLFENENGHIRLLQRFDKRSDLFENLQNYRLVEYRAKPHTIFLPQHIDADLILVVLSGKAILTVLSPNDRNSYNLERGDTIKLPAGTTSYLVNQD DEEDLRLVDLVIPVNGPGKFEAFDLAKNKNQYLRGFSKNILEASYNTRYETIEKVLLEEQEKDRKRRQQGEETDAIVKVSREQIEELKKLAKSSSKKSLPSEFEPINLRSHKPEYSNKFGKLFEITPEKKYPQLQDLDLFVSCVEINEGALML PHYNSRAIVVLLVNEGKGNLELLGLKNEQQEREDRKERNNEVQRYEARLSPGDVVIIPAGHPVAITASSNLNLLGFGINAENNERNFLSGSDDNVISQIENPVKELTFPGSVQEINRLIKNQKQSHFANAEPEQKEQGSQGKRSPLSSILGTFY [SEQ ID 2]

[0337] Peptide: HPVAITASSNLNLLG[SEQ ID 91] Peptide: ASSNLNLLGFG[SEQ ID 92] Peptide: ITASSNLNLLGFG[SEQ ID 93] Peptide: ITASSNLNLLGFGINAE[SEQ ID 94] Peptide: SSNLNLLGFG[SEQ ID 95] Peptide: VDLVIPVNGPGKF[SEQ ID 96] Peptide: LVIPVNGPGKFE[SEQ ID 97] Peptide: LVIPVNGPGKFEA [SEQ ID 98] Peptide: LRLVDLVIPVNGPGKFE[SEQ ID 99] Peptide: YRAKPHTIFLPQHIDAD[SEQ ID 100] Peptide: HPVAITASSNLNLLGFGINAE[SEQ ID 101] Peptide: SNLNLLGFG [SEQ ID 102] Peptide: HPVAITASSNLNLLGFGINAENNE[SEQ ID 103] Peptide: LVDLVIPVNGPGKFE[SEQ ID 104] Peptide: LVIPVNGPGKF[SEQ ID 105] Peptide: TIKLPAGTTSYLVNQDDE[SEQ ID 106] Peptide: DLRLVDLVIPVNGPGKFE[SEQ ID 107] Peptide: EDLRLVDLVIPVNGPGKFE[SEQ ID 108] Peptide: HPVAITASSNLNLLGFG[SEQ ID 109] Peptide: LVDLVIPVNGPGKFEAFDLAK [SEQ ID 110] Peptide: DNVISQIENPVKE [SEQ ID 111] Peptide: VVIIPAGHPVAITASSNLNLLGFG[SEQ ID 112] Peptide: LVDLVIPVNGPGKFEAF[SEQ ID 113] Peptide: YPQLQDLDL[SEQ ID 114] Peptide: VIPVNGPGKF [SEQ ID 115] Peptide: SKKSLPSE [SEQ ID 116] Peptide: LPQHIDADLILVVLSGK[SEQ ID 117] Peptide: RGDTIKLPAGTTSYLVNQD[SEQ ID 118] Peptide: IPVNGPGKF [SEQ ID 119] Peptide: LPQHIDADL [SEQ ID 120] Peptide: LVIPVNGPGK [SEQ ID 121] Peptide: IFLPQHIDAD[SEQ ID 122] Peptide: LPQHIDAD[SEQ ID 123] Peptide: VIPVNGPGK [SEQ ID 124] Peptide: IFLPQHIDA [SEQ ID 125] Peptide: TIKLPAGTTSYLVNQDDEE[SEQ ID 126] Peptide: HGEWRPSYEKEEDEEEGQRER[SEQ ID 127] Peptide: EKRHGEWRPSYEKEEDEEEGQRE[SEQ ID 128] Peptide: LPAGTTSYLVNQDDEEDLR[SEQ ID 129] Peptide: PSYEKEEDEEEGQRER [SEQ ID 130] Peptide: EKRHGEWRPSYE [SEQ ID 131] Peptide: TIKLPAGTTSYLVNQDDEED[SEQ ID 132] Peptide: HGEWRPSYEKQEDEEEK[SEQ ID133] Peptide: EWRPSYEKEEDEEE[SEQ ID 134] Peptide: PSYEKEEDEEEGQR[SEQ ID 135] Peptide: EKEEDEEEGQR [SEQ ID 136] Peptide: EWRPSYEKEEDEEEGQRE[SEQ ID 137] Peptide: KEEDEEEGQR [SEQ ID 138] Peptide: VQPGRERWEREEDEEQVDE[SEQ ID 139] Peptide: DVVIIPAGHPVA [SEQ ID 140] Peptide: HGEWRPSYEKQEDE[SEQ ID 141] Peptide: EEDEEEGQR [SEQ ID 142] Peptide: HGEWRPSYEKEEDEEEGQR[SEQ ID 143] Peptide: EEWRGSQRREDPEE [SEQ ID 144] Peptide: REEDEEQVDEEWRGSQRREDPEE[SEQ ID 145] Peptide: RHGEWRPSY [SEQ ID 146] Peptide: HGEWRPSYEKQEDEE [SEQ ID 147] Peptide: VVIIPAGHPVA [SEQ ID 148] Peptide: HGEWRPSYE [SEQ ID 149] Peptide: KEEDEEEGQRER [SEQ ID 150] Peptide: VVIIPAGHPVAIT [SEQ ID 151] Peptide: EKRHGEWRPSYEKEEDE [SEQ ID 152] Peptide: QVDEEWRGSQRREDPEE[SEQ ID 153] Peptide: GDTIKLPAGTTSYLVNQDDEEDLR[SEQ ID 154] Peptide: GSEPRVPAQRE[SEQ ID 155] Peptide: EEKRHGEWRPSYEKE [SEQ ID 156] Peptide: EWRPSYEKEEDEE [SEQ ID 157] Peptide: NYDEGSEPRVPAQRE[SEQ ID 158] Peptide: VIIPAGHPVAIT [SEQ ID 159] Peptide: RHGEWRPSYEK [SEQ ID 160] Peptide: NYDEGSEPR [SEQ ID 161] Peptide: WRPSYEKEEDEE [SEQ ID 162] Peptide: WRPSYEKQEDEEE[SEQ ID 163] Peptide: EKRHGEWRPSYEKQEDEEE[SEQ ID 164] Peptide: VVIIPAGHPVAITA [SEQ ID 165] Peptide: KRHGEWRPSYE [SEQ ID 166] Peptide: GSDDNVISQIENPVKE [SEQ ID 167] Peptide: VVIIPAGHPV [SEQ ID 168] Peptide: HGEWRPSY [SEQ ID 169] Peptide: RPSYEKEEDEEEGQR[SEQ ID 170] Peptide: HGEWRPSYEK [SEQ ID 171] Peptide: KRHGEWRPSYEKEE [SEQ ID 172] Peptide: VVIIPAGHPVAITAS [SEQ ID 173] Peptide: RGDTIKLPAGTTSYLVNQDDEED[SEQ ID 174] Peptide: KRHGEWRPSYEKQEDEEE[SEQ ID 175] Peptide: DEEQVDEEWRGSQRREDPEE[SEQ ID 176] Peptide: RHGEWRPSYE [SEQ ID 177] Peptide: HGEWRPSYEKE [SEQ ID 178] Peptide: KRHGEWRPSYEKEEDEEE[SEQ ID 179] Peptide: EKRHGEWRPSYEKEEDEEE[SEQ ID 180] Peptide: TIKLPAGTTSYLVNQDDEEDLRLVD[SEQ ID 181] Peptide: WRPSYEKEEDEEEGQRE[SEQ ID 182] Peptide: KRHGEWRPSYEKEEDEE [SEQ ID 183] Peptide: VVIIPAGHPVAI [SEQ ID 184] Peptide: EWRGSQRREDPEE [SEQ ID 185] Peptide: HGEWRPSYEKQEDEEEKQK[SEQ ID 186] Peptide: SGSDDNVISQIENPVKE [SEQ ID 187] Peptide: RPSYEKEEDEEEGQRER [SEQ ID 188] Peptide: EKEEDEEEGQRER [SEQ ID 189] Peptide: HGEWRPSYEKQ[SEQ ID 190] Peptide: WRPSYEKEEDEEE[SEQ ID 191] Peptide: LAKNKNQYLRGFS[SEQ ID 192] Peptide: NKNQYLRGFS [SEQ ID 193] Peptide: LRGFSKNILE [SEQ ID 194] Peptide: LAKNKNQYLRGFSKN[SEQ ID 195] Peptide: TVLSPNDRNSY [SEQ ID 196] Peptide: QYLRGFSKNILE [SEQ ID 197] Peptide: GKAILTVLSPNDRNSYNLE[SEQ ID 198] Peptide: RGFSKNILE [SEQ ID 199] Peptide: NKNQYLRGFSKNILE[SEQ ID 200] Peptide: ASSNLNLLGFGINAE[SEQ ID 201] Peptide: ASSNLNLLGF [SEQ ID 202] Peptide: LAKNKNQYLRGFSK[SEQ ID 203] Peptide: RGDTIKLPAGTTSYLVNQDDEE[SEQ ID 204] Peptide: ARLSPGDVVIIPAGHPVAITASSN[SEQ ID 205] Peptide: VQRYEARLSPGD[SEQ ID 206] Peptide: ARLSPGDVVIIPAGHPVAIT[SEQ ID 207] Peptide: RGDTIKLPAGTTSYLVNQDDE[SEQ ID 208] Peptide: ARLSPGDVVIIPAGHPVA[SEQ ID 209] Peptide: GALMLPHYNSRAIVVLLVNE[SEQ ID 210] Peptide: ARLSPGDVVIIPAGHPVAITASS[SEQ ID 211] Peptide: LSPGDVVIIPAGHPVAITASSNLNLLGFGINAENNER[SEQ ID 212] Peptide: ARLSPGDVVIIPAGHPVAITAS[SEQ ID 213] Peptide: LSPGDVVIIPAGHPVAITASSNL[SEQ ID 214] Peptide: ARLSPGDVVIIPAGHPVAITA[SEQ ID 215]

[0338] Protein: Q0DEV5 - 5 - Rice MSALTTSQLATSATGFGIADRSAPSSLLRHGFQGLKPRSPAGGDATSLSVTTSARATPKQQRSVQRGSRRFPSVVVYATGAGMNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYDQYKDAWDTSVVAEIKVADRYERVRF FHCYKRGVDRVFIDHPSFLEKVWGKTGEKIYGPDTGVDYKDNQMRFSLLCQAALEAPRILNLNNNPYFKGTYGEDVVFVCNDWHHTGPLASYLKNNYQPNGIYRNAKVAFCIHNISYQGRFAFEDYPELNLSERFRSSFDFIDGYDTPVEGRK INWMKAGILEADRVLTVSPYYAEELISGIARGCELDNIMRLTGITGIVNGMDVSEWDPSKDKYITAKYDATTAIEAKALNKEALQAEAGLPVDRKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGK VRAVVKFNAPLAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFHMGRLSVDCKVVEPSDVKKVAATLKRAIKVVGTPAYEEMVRNCMNQDLSWKGPAKNWENVLLGLGVAGSAPGIEGDEIAPLAKENVAAP [SEQ ID 3]

[0339] Peptide: NWENVLLGLGVAGSAPGIEGDEIAPLAK[SEQ ID 216] Peptide: YDQYKDAWDTSVVAEIK[SEQ ID 217] Peptide: SSFDFIDGYDTPVEGR[SEQ ID 218] Peptide: GPDTGVDYKDNQM [SEQ ID 219] Peptide: ILNLNNNPYFK[SEQ ID 220] Peptide: VVGTPAYEE [SEQ ID 221] Peptide: IDGYDTPVEGR[SEQ ID 222] Peptide: VVGTPAYE [SEQ ID 223] Peptide: IYGPDTGVDYK[SEQ ID 224] Peptide: VAGSAPGIEGDE [SEQ ID 225] Peptide: IYGPDTGVDYKDNQMR[SEQ ID 226] Peptide: VVGTPAYEEMVR[SEQ ID 227] Peptide: DFIDGYDTPVEGR[SEQ ID 228] Peptide: LGLGVAGSAPGIEGDEIAPLAK [SEQ ID 229] Peptide: FNAPLAHLIMAGADVLAVPSR[SEQ ID 230] Peptide: LGLGVAGSAPGIEGDE[SEQ ID 231] Peptide: LGLGVAGSAPGIEGDEIAPL[SEQ ID 232] Peptide: VLTVSPYYAEELISGIAR [SEQ ID 233] Peptide: EALQAEAGLPVDR[SEQ ID 234] Peptide: LGLGVAGSAPGIEGD[SEQ ID 235] Peptide: IMAGADVLAVPSR[SEQ ID 236] Peptide: GLGVAGSAPGIEGDE[SEQ ID 237] Peptide: EALQAEAGLPVDRK[SEQ ID 238] Peptide: TGGLGDVLGGLPPAMAANGHR[SEQ ID 239] Peptide: LEEQKGPDVMA [SEQ ID 240] Peptide: LGVAGSAPGIEGDEIAPLAK [SEQ ID 241] Peptide: GLGVAGSAPGIEGDEIAPLAK [SEQ ID 242] Peptide: TGGLGDVLGGLPPAM [SEQ ID 243] Peptide: NVLLGLGVAGSAPGIEGDE[SEQ ID 244]

[0340] Protein: P14323 - 6 - Rice MASSVFSRFSIYFCVLLLCHGSMAQLFNPSTNPWHSPRQGSFRECRFDRLQAFEPLRKVRSEAGVTEYFDEKNELFQCTGTFVIRRVIQPQGLLVPRYTNIPGVVYIIQGRGSMGLTFPGCPAT YQQQFQQFSSQGQSQSQKFRDEHQKIHQFRQGDIVALPAGVAHWFYNDGDAPIVAVYVYDVNNNANQLEPRQKEFLLAGNNNRAQQQQVYGSSIEQHSGQNIFSGFGVEMLSEALGINAVAAKRL QSQNDQRGEIIHVKNGLQLLKPTLTQQQEQAQAQDQYQQVQYSERQQTSSRWNGLEENFCTIKVRVNIENPSRADSYNPRAGRITSVNSQKFPILNLIQMSATRVNLYQNAILSPFWNVNAHSLV YMIQGRSRVQVVSNFGKTVFDGVLRPGQLLIIPQHYAVLKKAEREGCQYIAIKTNANAFVSHLAGKNSVFRALPVDVVANAYRISREQARSLKNNRGEEHGAFTPRFQQQYYPGLSNESESETSE [SEQ ID 4]

[0341] Peptide: TVFDGVLRPGQL[SEQ ID 245] Peptide: RLQSQNDQRGEIIHVK[SEQ ID 246]

[0342] Protein: P29835 - 5 - Rice MASKVVFFAAALMAAMVAISGAQLSESEMRFRDRQCQREVQDSPLDACRQVLDRQLTGRERFQPMFRRPGALGLRMQCCQQLQDVSRECRCAAIRRMVRSYEESMPMPLEQGWSSSSSEYYGGEGSSSEQGYYGEGSSEEGYYGEQQQQPGMTRVRLTRARQYAAQLPSMCRVEPQQCSIFAAGQY [SEQ ID 5]

[0343] Peptide: EGYYGEQQQQPGMTR[SEQ ID 247] Peptide: GYYGEQQQQPGMTR[SEQ ID 248] Peptide: EEGYYGEQQQQPGMTR[SEQ ID 249] Peptide: YYGGEGSSSEQGYYGEGSSE[SEQ ID 250] Peptide: YGGEGSSSEQGYYGEGSSE[SEQ ID 251] Peptide: SSEEGYYGEQQQQPGMTR[SEQ ID 252] Peptide: SEEGYYGEQQQQPGMTR[SEQ ID 253] Peptide: QGYYGEGSSEE [SEQ ID 254] Peptide: YGGEGSSSEQGYYGEGSSEEGY[SEQ ID 255] Peptide: YGEQQQQPGMTR[SEQ ID 256] Peptide: YYGEQQQQPGMTR[SEQ ID 257] Peptide: SYEESMPMPLEQGWSSSSSE[SEQ ID 258] Peptide: YYGEGSSEEGYYGEQQQQPGMTR[SEQ ID 259] Peptide: QQQQPGMTRV[SEQ ID 260] Peptide: GEQQQQPGMTR[SEQ ID 261] Peptide: SYEESMPMPLEQGWSSSSSEY[SEQ ID 262] Peptide: YYGGEGSSSEQGYYGEGSSEEGY[SEQ ID 263] Peptide: YGEQQQQPGMTRVR[SEQ ID 264] Peptide: GEGSSEEGYYGEQQQQPGMTR[SEQ ID 265] Peptide: YGEGSSEEGYYGEQQQQPGMTR[SEQ ID 266] Peptide: QQQQPGMTRVR[SEQ ID 267] Peptide: QYAAQLPSMCRVEPQQCSIFAAGQY[SEQ ID 268]

[0344] Protein: P0C1U8 - 5 - Staphylococcus aureus MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQTQSSKQQTPKIQKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFS PNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDNNNSDNPDAA [SEQ ID 14]

[0345] Peptide: APTGTFIASGVVVGKD[SEQ ID 413] Peptide: LAIVKFSPNEQNKHIGE[SEQ ID 414] Peptide: RHQITDTTNGHYAPVTYIQVE[SEQ ID 415] Peptide: GDLAIVKFSPNEQNKHIGE[SEQ ID 416] Peptide: NPDNPDNPNNPDNPNNPD [SEQ ID 417]

[0346] Protein: P14614 - 4 - Rice MATIAFSRLSIYFCVLLLCHGSMAQLFGPNVNPWHNPRQGGFRECRFDRLQAFEPLRRVRSEAGVTEYFDEKNEQFQCTGTFVIRRVIEPQGLLVPRYSNTPGMVYIIQGRGSMGLTFPGCPATY QQQFQQFLPEGQSQSQKFRDEHQKIHQFRQGDIVALPAGVAHWFYNEGDAPVVALYVFDLNNNANQLEPRQKEFLLAGNNNREQQMYGRSIEQHSGQNIFSGFNNELLSEALGVNALVAKRLQGQ NDQRGEIIRVKNGLKLLRPAFAQQQEQAQQQEQAQAQYQVQYSEEQQPSTRCNGLDENFCTIKARLNIENPSHADTYNPRAGRITRLNSQKFPILNLVQLSATRVNLYQNAILSPFWNVNAHSLV YIVQGHARVQVVSNLGKTVFNGVLRPGQLLIIPQHYVVLKKAEHEGCQYISFKTNANSMVSHLAGKNSIFRAMPVDVIANAYRISREQARSLKNNRGEELGAFTPRYQQQTYPGFSNESENEALE [SEQ ID 6]

[0347] Peptide: TVFNGVLRPGQL[SEQ ID 269] Peptide: TVFNGVLRPGQLL[SEQ ID 270] Peptide: SGFNNELLSEALGVNALVAK [SEQ ID 271] Peptide: NGVLRPGQL [SEQ ID 272] Peptide: ALVAKRLQGQNDQRGEI[SEQ ID 273] Peptide: VPRYSNTPGM [SEQ ID 274] Peptide: PRYSNTPGMV [SEQ ID 275] Peptide: YSNTPGMVY [SEQ ID 276] Peptide: LVPRYSNTPGM [SEQ ID 277] Peptide: FYNEGDAPVV [SEQ ID 278] Peptide: FYNEGDAPVVAL[SEQ ID 279] Peptide: FEPLRRVRSEAGVTE[SEQ ID 280] Peptide: FYNEGDAPVVALY[SEQ ID 281] Peptide: FYNEGDAPVVA [SEQ ID 282]

[0348] Protein: P09918 - 14 - Pisum sativum MFSGVTGILNRGHKIKGTVVLMRKNVLDINSLTTVGGVIGQGFDILGSTVDNLTAFLGRSVSLQLISATKPDATGKGKLGKATFLEGIISSLPTLGAGQSAFKIHFEWDDDMGIPGAFYIKNFMQTEFFLVSLTLDDIPNHGSIYFVCNSWIYNAKHHKIDRIFFANQTYLPSETPAPLVHYREEELNNLRGDGGTGERKEWERIYDYDVYNDLGN PDSGENHARPVLGGSETYPYPRRGRTGRKPTRKDPNSESRSDYVYLPRDEAFGHLKSSDFLTYGLKAVSQNVVPALESVFFDLNFTPNEFDSFDEVHGLYEGGIKLPTNILSQISPLPVLKEIFRTDGENTLKYPPKPVIQVSRSGWMTDEEFAREMLAGVNPNVICCLQEFPPRSKLDSQIYGDHSKISKEHLEPNLEGLTVEEAIQNKKLFL LDHHDSIMPYLRRINSTSTKAYATRTILFLNNNQNLKPLAIELSLPHPQGDEHGAVSYVYQPALEGVESSIWLAKAYVIVNDSCYHQLVSHWNLTHAVVEPFVIATNRHLSCHLPIYKLLYPHYRDTMNINSLARLSLVNDGGIIEKTFLWGRYSMEMSKVYKNWVFTEQALPADLIKRGMAIEDSPSPCGVKLVVEDYPYAVDGLEIWAIIK TWVQDYVSLYYTSDEKLRQDSELQAWWKELVEVGHGDKKNEPWWPKMQTREDLIEVCSIVIWTASALHAAVNFGQYSYGGLILNRPTLSRRFMPEKGSAEFEELVKSPQKAYLKTITPKFQTLIDLSVIEILSRHASDELYLGERDNPNWTSDKRALEAFKKFGNKLAEIEKKLTQRNNDEKLRNHGPVEMPYTLPSSKEGLTFRGIPNSISI [SEQ ID 7]

[0349] peptide : HGPVEMPYTLLYPSSK[SEQ ID 283]

[0350] Protein: P02857 - 1 - Pea MAKLLALSLSFCFLLLGGCFALREQPQQNECQLERLDALEPDNRIESEGGLIETWNPNNKQFRCAGVALSRATLQRNALRRPYYSNAPQEIFIQQGNGYFGMVFPGCPETFEEPQESEQGEGRRYRDRH QKVNRFREGDIIAVPTGIVFWMYNDQDTPVIAVSLTDIRSSNNQLDQMPRRFYLAGNHEQEFLQYQHQQGGKQEQENEGNNIFSGFKRDYLEDAFNVNRHIVDRLQGRNEDEEKGAIVKVKGGLSIISP PEKQARHQRGSRQEEEDEDEEKQPRHQRGSRQEEEDEDEERQPRHQRRRGEEEEEDKKERGGSQKGKSRRQGDNGLEETVCTAKLRLNIGPSSSPDIYNPEAGRIKTVTSLDLPVLRWLKLSAEHGSLH KNAMFVPHYNLNANSIIYALKGRARLQVVNCNGNTVFDGELEAGRALTVPQNYAVAAKSLSDRFSYVAFKTNDRAGIARLAGTSSVINNLPLDVVAATFNLQRNEARQLKSNNPFKFLVPARESENRASA [SEQ ID 8]

[0351] Peptide: LDALEPDNR [SEQ ID 284] Peptide: DALEPDNR [SEQ ID 285] Peptide: HGSLHKNAMFVPHYNLNANSIIYA[SEQ ID 286] Peptide: LAGTSSVINNLPLDVVAATF [SEQ ID 287] Peptide: FREGDIIAVPTGIVFW[SEQ ID 288] Peptide: GTSSVINNLPLDVVAATFNLQRNE[SEQ ID 289] Peptide: KGAIVKVKGGLSIISPPE[SEQ ID 290] Peptide: RLAGTSSVINNLPLD[SEQ ID 291] Peptide: AGTSSVINNLPLDVVAATFNLQRNE[SEQ ID 292] Peptide: AGTSSVINNLPL [SEQ ID 293] Peptide: LAGTSSVINNLPLDVVA[SEQ ID 294] Peptide: AGTSSVINNLPLDV [SEQ ID 295] Peptide: AGRIKTVTSLDLPVLRW[SEQ ID 296] Peptide: AGRIKTVTSLDLPVLR[SEQ ID 297] Peptide: FREGDIIAVPTGIVF [SEQ ID 298] Peptide: AGTSSVINNLPLD [SEQ ID 299] Peptide: LAGTSSVINNLPL[SEQ ID 300] Peptide: LAGTSSVINNLPLDVV[SEQ ID 301] Peptide: EGDIIAVPTGIVF [SEQ ID 302] Peptide: LAGTSSVINNLPLDV[SEQ ID 303] Peptide: AGRALTVPQNYAVAAKSLSD[SEQ ID 304] Peptide: AGRALTVPQNYA[SEQ ID 305] Peptide: LAGTSSVINNLPLD[SEQ ID 306] Peptide: RAGIARLAGTSSVINNLPLDVVA[SEQ ID 307]

[0352] Protein: P02855 - 4 - Pea DNAEIEKILLEEHEKETHHRRGLRDKRQQSQEKNVIVKVSKKQIEELSKNAKSSSKKSVSSRSEPFNLKSSDPIYSNQYGKFFEITPKKNPQLQDLDIFVNYVEIKEGSLWLPHYNSRAIVIVTVNEGKGDFELVGQRNENQQGLREEDDEEEEQREEETKNQVQSYKAKLTPGDVFVIPAGHPVAVRASSNLNLLGFGINAENNQRNFLAGEEDNVISQIQKQVKDLTFPGSAQEVDRLLENQKQSYFANAQPQQRETRSQEIKEHLYSILGAF [SEQ ID 9]

[0353] Peptide: RASSNLNLLGFGINAE[SEQ ID 308] Peptide: VTVNEGKGDFEL[SEQ ID 309] Peptide: VRASSNLNLLGFGINAE[SEQ ID 310] Peptide: VRASSNLNLLGFG[SEQ ID 311] Peptide: HPVAVRASSNLNLLGFG[SEQ ID 312] Peptide: TKNQVQSYKAKLTPGD[SEQ ID 313] Peptide: HPVAVRASSNLNLLG[SEQ ID 314] Peptide: KAKLTPGDVFVIPAG[SEQ ID 315] Peptide: DLTFPGSAQEVDRLLENQK[SEQ ID 316] Peptide: PAGHPVAVR [SEQ ID 317] Peptide: AKLTPGDVFVIPAGHPVA[SEQ ID 318] Peptide: SYKAKLTPGDVFVIPAGHPVA[SEQ ID 319] Peptide: LTPGDVFVIPAGHPVAVR[SEQ ID 320] Peptide: VQSYKAKLTPGDVFVIPAG[SEQ ID 321] Peptide: YKAKLTPGDVFVIPAGHPVA[SEQ ID 322] Peptide: FVIPAGHPVAVR[SEQ ID 323] Peptide: YKAKLTPGDVFVIPAG[SEQ ID 324] Peptide: DLTFPGSAQEVDR[SEQ ID 325] Peptide: AKLTPGDVFVIPAGHPVAVR[SEQ ID 326] Peptide: LTPGDVFVIPAG [SEQ ID 327] Peptide: SYKAKLTPGDVFVIPAG[SEQ ID 328] Peptide: SYKAKLTPGDVFVIPAGHPVAVR[SEQ ID 329] Peptide: VIPAGHPVAVR[SEQ ID 330] Peptide: QVQSYKAKLTPGDVFVIPAG[SEQ ID 331] Peptide: AKLTPGDVFVIPAG [SEQ ID 332] Peptide: HPVAVRASSNLNLLGFGINAE [SEQ ID 333] Peptide: YKAKLTPGDVFVIPAGHPVAVR[SEQ ID 334] Peptide: TKNQVQSYKAKLTPGDVFVIPAG[SEQ ID 335] Peptide: PFNLKSSDPIYS[SEQ ID 336] Peptide: IEKILLEE [SEQ ID 337] Peptide: SRSEPFNLKSSDPIYS[SEQ ID 338] Peptide: HPVAVRASSNLNL[SEQ ID 339]

[0354] Protein: D3VNE1 - 5 - Pea MAATPIKPLMLLAIAFLASVCVSSRSDQENPFIFKSNRFQTLYENENGHIRLLQKFDKRSKIFENLQNYRLLEYKSKPRTLFLPQYTDADFILVVLSGKATLTVLKSNDRNSFNLERGDTIKLPAGTIAYLANRDDNEDLRVLDLTIPVNKPGQLQSFLLSGTQNQPSLLSGFSKNILEAAFNTNYEEIEKVLLEQQEQEPQHRRSLKDRRQEINEENVIVKVSREQIEELSKNAKSSSSKKSVSSESGPFNLRSRNPIYSNKFGKFFEITPEKNQQLQDLDIFVNSVDIKEGSLLLPNYNSRAIVIVTVTEGKGDFELVGQRNENQGKENDKEEEQEEETSKQVQLYRAKLSPGDVFVIPAGHPVAINASSDLNIGFGINAENNERNFLAGEEDNVISQVERPVKELAFPGSSHEVDRLLKNQKQSYFANAQPLQRE [SEQ ID 10]

[0355] peptide : TLFLPQYTDADFILVVLSGK[SEQ ID 340]

[0356] protein : P07728 - 1 - イネ MASINRPIVFFTVCLFLLCNGSLAQQLLGQSTSQWQSSRRGSPRECRFDRLQAFEPIRSVRSQAGTTEFFDVSNEQFQCTGVSVVRRVIEEPRGLLLPHYTNGASLVYIIQGRGITGPTFPGCPE SYQQQFQQSGQAQLTESQSQSQKFKDEHQKIHRFRQGDVIALPAGVAHWCYNDGEVPVVAIYVTDLNNGANQLDPRQRDFLLAGNKRNPQAYRREVEERSQNIFSGFSTELLSEALGVSSQVARQ LQCQNDQRGEIVRVEHGLSLLQPYASLQEQEQGQVQSRERYQEGQYQQSQYGSGCSNGLDETFCTLRVRQNIDNPNRADTYNPRAGRVTNLNTQNFPILSLVQMSAVKVNLYQNALLSPFWNINA HSVVYITQGRARVQVVNNNGKTVFNGELRRGQLLIIPQHYAVVKKAQREGCAYIAFKTNPNSMVSHIAGKSSIFRALPNDVLANAYRISREEAQRLKHNRGDEFGAFTPIQYKSYQDVYNAAESS [SEQ ID 11]

[0357] Peptide: EVEERSQNIF [SEQ ID 341] Peptide: VEERSQNIFSGF [SEQ ID 342] Peptide: ASLQEQEQGQVQ[SEQ ID 343] Peptide: QEQEQGQVQSR[SEQ ID 344] Peptide: ASLQEQEQGQVQSR[SEQ ID 345] Peptide: EVEERSQNIFSGF [SEQ ID 346] Peptide: VTDLNNGANQLDPRQRD[SEQ ID 347] Peptide: VEHGLSLLQPYASL[SEQ ID 348] Peptide: IYVTDLNNGANQLDPRQRDFL[SEQ ID 349] Peptide: VTDLNNGANQLDPRQRDFL[SEQ ID 350] Peptide: VEHGLSLLQPYASLQEQEQGQVQSR[SEQ ID 351] Peptide: VTDLNNGANQLDPR[SEQ ID 352] Peptide: IYVTDLNNGANQLDPRQRD[SEQ ID 353] Peptide: YVTDLNNGANQLDPRQRDFL[SEQ ID 354] Peptide: YVTDLNNGANQLDPR[SEQ ID 355] Peptide: STELLSEALGVSSQVAR [SEQ ID 356] Peptide: HGLSLLQPYASLQEQE[SEQ ID 357] Peptide: SGFSTELLSEALGVSSQVAR [SEQ ID 358]

[0358] Protein: P07730 - 2 - Rice MASINRPIVFFTVCLFLLCDGGSLAQQLLGQSTSQWQSSRRGSPRGCRFDRLQAFEPIRSVRSQAGTTEFFDVSNELFQCTGVSVVRRVIEEPRGLLLPHYTNGASLVYIIQGRGITGPTFPGCPE TYQQQFQQSGQAQLTESQSQSHKFKDEHQKIHRFRQGDVIALPAGVAHWCYNDGEVPVVAIYVTDINNGANQLDPRQRDFLLAGNKRNPQAYRREVEEWSQNIFSGFSTELLSEAFGISNQVARQ LQCQNDQRGEIVRVERGLSLLQPYASLQEQEQGQMQSREHYQEGGYQQSQYGSGCPNGLDETFCTMRVRQNIDNPNRADTYNPRAGRVTNLNSQNFPILNLVQMSAVKVNLYQNALLSPFWNINA HSIVYITQGRAQVQVVNNNGKTVFNGELRRGQLLIVPQHYVVVKKAQREGCAYIAFKTNPNSMVSHIAGKSSIFRALPTDVLANAYRISREEAQRLKHNRGDEFGAFTPLQYKSYQDVYNVAESS [SEQ ID 12]

[0359] Peptide: GAFTPLQYKSYQD[SEQ ID 359] Peptide: GLLLPHYTNGASLVY [SEQ ID 360] Peptide: FLLAGNKRNPQAYRRE[SEQ ID 361] Peptide: ALPTDVLANAYR [SEQ ID 362] Peptide: DFLLAGNK [SEQ ID 363] Peptide: DVLANAYR [SEQ ID 364] Peptide: GAFTPLQYK [SEQ ID 365] Peptide: QGDVIALPAGVAHW [SEQ ID 366] Peptide: FGAFTPLQYKSY[SEQ ID 367] Peptide: FLLAGNKRNPQAYR[SEQ ID 368] Peptide: FGAFTPLQYKSYQ[SEQ ID 369] Peptide: GLSLLQPYASLQEQE[SEQ ID 370] Peptide: AFTPLQYK [SEQ ID 371] Peptide: FGAFTPLQYKSYQD[SEQ ID 372] Peptide: GDEFGAFTPLQYK[SEQ ID 373] Peptide: FGAFTPLQYKSYQDV[SEQ ID 374] Peptide: FGAFTPLQYK [SEQ ID 375] Peptide: FGAFTPLQYKS[SEQ ID 376] Peptide: VYIIQGRGITGPTF[SEQ ID 377] Peptide: YIIQGRGITGPTF[SEQ ID 378] Peptide: KTNPNSMVSHIAGK [SEQ ID 379] Peptide: TNPNSMVSHIAGK [SEQ ID 380] Peptide: PNSMVSHIAGKS [SEQ ID 381] Peptide: NIDNPNRADTYNPRAGRVTN[SEQ ID 382] Peptide: QRDFLLAGNKR [SEQ ID 383] Peptide: LLQPYASLQEQE[SEQ ID 384] Peptide: QRDFLLAGNK [SEQ ID 385] Peptide: QEQEQGQMQSR[SEQ ID 386] Peptide: SLLQPYASLQEQE[SEQ ID 387] Peptide: ASLQEQEQGQM [SEQ ID 388] Peptide: ASLQEQEQGQMQSR[SEQ ID 389] Peptide: DFLLAGNKR [SEQ ID 390] Peptide: QAFEPIRSVRSQAGTTEF[SEQ ID 391] Peptide: KTNPNSMVSHIAGKSSIF [SEQ ID 392] Peptide: VRRVIEPRGLLLPHYTNGASL[SEQ ID 393] Peptide: FGAFTPLQYKSYQDVYN[SEQ ID 394] Peptide: IALPAGVAHW [SEQ ID 395] Peptide: RVRQNIDNPNRADTYNPRAGRVTNL[SEQ ID 396] Peptide: NIDNPNRADTYNPRAGRVTNL[SEQ ID 397] Peptide: GAFTPLQYKSYQDVYN[SEQ ID 398] Peptide: PNSMVSHIAGKSSIFR [SEQ ID 399] Peptide: RLQAFEPIRSVRSQAGTTE[SEQ ID 400] Peptide: TNPNSMVSHIAGKSSIFR[SEQ ID 401]

[0360] Protein: Q0D7S0 - 3 - Rice MASNKVVFSVLLLAVVSVLAATATMAEYHHQDQVVYTPGPLCQPGMGYPMYPLPRCRALVKRQCVGRGTAAAAEQVRRDCRQLAAVDDSWCRCEAISHMLGGIYRELGAPDVGHPMSEVFRGCRRGDLERAAASLPAFCNVDIPNGGGGVCYWLARSGY [SEQ ID 13]

[0361] Peptide: ELGAPDVGHPM [SEQ ID 402] Peptide: LGAPDVGHPM [SEQ ID 403] Peptide: ELGAPDVGHPMSEVF [SEQ ID 404] Peptide: ELGAPDVGHPMS [SEQ ID 405] Peptide: ELGAPDVGHPMSEVFR[SEQ ID 406] Peptide: ELGAPDVGHPMSEV [SEQ ID 407] Peptide: ELGAPDVGHPMSE[SEQ ID 408] Peptide: LGAPDVGHPMSE[SEQ ID 409] Peptide: YRELGAPDVGHPMSE[SEQ ID 410] Peptide: LGAPDVGHPMSEV [SEQ ID 411] Peptide: RELGAPDVGHPMSE[SEQ ID 412]

[0362] Additional peptides (and source proteins) HPRPPKPDAPR [SEQ ID 452] - Q0D9DO LQQAPPPPQR [SEQ ID 453] - Q6AVS5 VGWGEQPWSPY [SEQ ID 454] - Q8H920 FHMPP [SEQ ID 455] - O49927 FRRP [SEQ ID 456] - P29835 FWM [SEQ ID 457] - P15838 HMPPS [SEQ ID 458]-049927 PVEMPTLLYPS [SEQ ID 459] HMPSS [SEQ ID 460] - O49927 HRFR [SEQ ID 461] - Q712V4 HRRS [SEQ ID 462] - P13918 HSPR [SEQ ID 463] - P14323 HWF [SEQ ID 464-P14323 MFRR [SEQ ID 465] - Q41000 MFRRP [SEQ ID 466-P29835 MPPS [SEQ ID 467]-049927 MPRR [SEQ ID 468] - P15838 NMPS [SEQ ID 469] - P20698 PHMP [SEQ ID 470] - O49927 PHMPS [ SEQ ID 471 - O49927 PRRF [SEQ ID 472] - P15838 WMK [SEQ ID 473] - O04434 DSINALEPDHR [SEQ ID 474] - P05692 ELTFPGSVQ [SEQ ID 475] - Q9M3X6 ELTFPGSVQE [SEQ ID 476] - Q9M3X6 IFEDAITIPGR [ SEQ ID 477 ] - P09886 LDALEPDNRIESE [SEQ ID 478] - P02857 KTLDYWPSLR [SEQ ID 479] - P08688 RHGEWGPSY [SEQ ID 480] ILVDGSHDIER [SEQ ID 481] - Q5N725 LVSHPIAAHEGR [SEQ ID 482] - P14614 NLAQAPAQALL [SEQ ID 483] - Q0DJ38 FLPQHTD [SEQ ID 484] - P13918 LEPDNR [SEQ ID 485] - P15838 LQSQND [SEQ ID 486] - P14323 LQSQNDQRGEI [SEQ ID 487] - P14323 QSQNDQRGEIIHVK [SEQ ID 488] - P14323 RGEIIHVK [SEQ ID 489] - P14323 RLQSQNDQ [SEQ ID 490] - P14323 RLQSQNDQRG [SEQ ID 491] - P14323 RLQSQNDQRGEIIH [SEQ ID 492] - P14323 VFDGVLRPG [SEQ ID 493] - P14323 HNPR [SEQ ID 494] - P14614 HPMS [SEQ ID 495] - Q0D7S0 HPSF [SEQ ID 496] - Q0DEV5 MPMP [SEQ ID 497] - P29835 PMPL [SEQ ID 498] - P29835 PNSM [SEQ ID 499] - P07728 WDP [SEQ ID 500] - B5A8N6 LRGFSK [SEQ ID 501] - Q9M3X6 RSQNIF [SEQ ID 502] - P07728 YLRGFS [SEQ ID 503] - Q9M3X6 GALMLPHYN [SEQ ID 504] - Q9M3X6 GALMLPHYNSR [SEQ ID 505] - Q9M3X6 KNPQLQDLDIFVNYVEIK [SEQ ID 700] P02855 PGQLQSFLLSGNQNQQNYLSGFSK [SEQ ID 701] P13918 RGPQQYAEWQINEK [SEQ ID 702] Q6K7K6 VLDLAIPVNRPGQL [SEQ ID 703] Q6K508 GYVGLTFPGCPATHQQQFQLFEQR [SEQ ID 704] P09918 LDVTPLSLGL [SEQ ID 717] EEGIQLVAEAIR [SEQ ID 718] YSLKPLVPR [SEQ ID 719] WHT [SEQ ID 720] WHN [SEQ ID 721] NNPF [SEQ ID 722] MRFR [SEQ ID 723] MPPSS [SEQ ID 724] HMPS [SEQ ID 725] HMPPS [SEQ ID 726] GHPM [SEQ ID 727] FWN [SEQ ID 728] FHMP [SEQ ID 729 WTIVQGLPIDE [SEQ ID 730] GYPMYPLPR [SEQ ID 731] HGGEGGRPY [SEQ ID 732] LRGFSK GALMLPHYN GALMLPHYNSR VFDGVLRPG LQSQND LQSQNDQRGEI QSQNDQRGEIIHVK RGEIIHVK [SEQ ID 740] RLQSQNDQ RLQSQNDQRG RLQSQNDQRGEIIH MPMP PMPL LEPDNR GIARLAGTSSVIN RSQNIF PNSM GHPM [SEQ ID 750] HPMS FLPQHTD EWQINEK GPQQYAEWQINEK PQQYAEWQ RGPQQYA<000203HNPR WHN WDP HPSF [SEQ ID 760] PGQLQSFLLSGNQNQQNYLSGF QLQSFLLSGNQNQQNYLSGFSK QSFLLSGNQNQQ PGQLQSFLLSGN QSFLLSGNQ QNQQNYLSGFSK YLRGFS <000204PVEMPTLLYPS RGPQQYAEWQINE GYVGLTFPGCPATHQQQFQLFEQR[SEQ ID 770] KNPQLQDLDIFVNYVEIK PGQLQSFLLSGNQNQQNYLSGFSK<s RGPQQYAEWQINEK<00VLDLAIPVNRPGQL RGPQQYAEWQINEK [SEQ ID 775]

[0363] Protein P02855 [SEQ ID 546-552] Peptide: SRAIVIVTVNE Peptide: AKLTPGDV Peptide: IVIVTVNEGK Peptide: LDALEPDNRIESEGGL (also in P02857) Peptide: RPYYSNAPQE (also in P02857) Peptide: LDALEPDNRIESEGGLIETWNPNNK (also in P02857) Peptide: AIVIVTVNEGK (also in P13918)

[0364] Protein P02857 [SEQ ID 553-565] Peptide: LQVVNCNGNTVFDGEL Peptide: QVVNCNGNTVFDGEL Peptide: IIAVPTGIVF Peptide: GRRYRDRHQKVNRFRE Peptide: RPYYSNAPQEI Peptide: RLDALEPDNRIE Peptide: RLDALEPDNRIESE Peptides: LDALEPDNRIESEGGLIETW Peptide: LDALEPDNRIE Peptide: LDALEPDNRIESEGGLIE Peptide: LDALEPDNRIESEGGL (also in P02855) Peptide: RPYYSNAPQE (also in P02857) Peptide: LDALEPDNRIESEGGLIETWNPNNK (also in P02855)

[0365] Protein P07728 [SEQ ID 566-609] Peptides: VEHGLSLLQPYASLQEQEQGQVQSRER Peptide: RSQNIFSGF Peptide: GITGPTFPGCPESY Peptides: CNGS Peptides: SPREC Peptides: PREC Peptides: PRECR Peptide: CPES Peptides: SGCS Peptides: CSNG Peptide: RSQNIFSGFSTE Peptide: VEEWSQNIFSGFST Peptide: WSQNIFSGFSTEL Peptide: WSQNIFSGFSTE Peptide: STSQWQSSRR Peptide: NRPI Peptides: CDGS Peptides: PRGC Peptides: PRGCR Peptide: RGCR Peptides: GCRF Peptides: PTFP Peptide: PGCPE Peptides: GCPE Peptides: CPET Peptides: AHWC Peptides: HWCY Peptides: SGCP Peptide: SGCPN Peptide: GCPN Peptides: CPNG Peptide: TFC™ Peptide: FCTM Peptide: FCTMR Peptides: CTMR Peptide: EGCA Peptide: SQNIFSGFSTELL Peptide: SQNIFSGFSTE Peptide: QNDQRGEIVR Peptide: SQNIFSGFSTEL (also in P07730) Peptide: QLQCQNDQRGEI (also in P07730) Peptide: LGQSTSQWQSSR (also in P07730) Peptide: QQLLGQSTSQWQSSR (also in P07730) Peptide: LLGQSTSQWQSSR (also in P07730)

[0366] Protein P07730 [SEQ ID 610-619] Peptide: NDQRGEIVR Peptide: GQSTSQWQSSR Peptide: STSQWQSSR Peptides: GITGPTFPGCPET Peptide: GITGPTFPGCPETY Peptide: SQNIFSGFSTEL (also in P07728) Peptide: QLQCQNDQRGEI (also in P07728) Peptide: LGQSTSQWQSSR (also in P07728) Peptide: QQLLGQSTSQWQSSR (also in P07728) Peptide: LLGQSTSQWQSSR (also in P07728)

[0367] Protein P09918 [620-630] Peptide: IFFANQTYL Peptide: EHLEPNLEGLTVEE Peptide: IFFANQTYLPSETPAPLVHYREEELNNLRGDGTGER Peptide: IHFEWDDDMGIPGAFYIK Peptide: IFFANQTYLPSETPAPLVHYREEELNNLR Peptide: TEQALPADLIK Peptide: EHLEPNLEGLTVEEAIQNKK Peptide: ISKEHLEPNLEGLTVEEAIQNKK Peptide: LSLPHPQGDEHGAVSY Peptide: ISKEHLEPNLEGLTVEEAIQNK Peptide: EHLEPNLEGLTVEEAIQNK

[0368] Protein P0C1U8 [SEQ ID 631] Peptide: LSTTGGNSGSPVFNEKNE

[0369] Protein P13918 [SEQ ID 632-639] Peptide: QSFLLSGNQNQQNYLSG Peptide: VLDLAIPVNRPGQLQS Peptide: VLDLAIPVNRPGQLQSFL Peptide: FLLSGNQNQQNYLSG Peptide: FLLSGNQNQQNYLSGFSK Peptide: DPQNPFIFKSNKFQTLFE Peptide: ELAFPGSAQEVDRILENQK Peptide: AIVIVTVNEGK (also in P02855)

[0370] Protein P14323 [SEQ ID 640-667] Peptide: INAVAAKRLQSQNDQRGE Peptide: NRAQQQQVYGSSIE Peptide: PSTNPWHSPR Peptides: CHGS Peptide: CHGSM Peptides: PWHS Peptides: FREC Peptides: RECR Peptides: ECRF Peptides: CRFD Peptide: CRFDR Peptide: CTGT Peptides: FPGC Peptides: FPGCP Peptides: PGCP Peptide: PGCPA Peptide: PGCPAT Peptide: GCPA Peptide: CPAT Peptides: ENFC Peptides: NFCT Peptides: NFCTI Peptides: FCTI Peptide: AQQQQVYGSSIEQH Peptide: AQQQQVYGSSIEQHSGQNIFSGF Peptide: AAKRLQSQNDQRGE Peptide: QARSLKNNRGEE (also in P14614) Peptide: FNPSTNPWHSPRQGS (also in Q0DEV5)

[0371] Protein P14614 [SEQ ID 668] Peptide: QARSLKNNRGEE (also in P14323)

[0372] Protein Q0D7S0 [SEQ ID 669] Peptide: AAASLPAFCNVDIPNGGGGVCYWLAR

[0373] Protein Q0DEV5 [SEQ ID 670-680] Peptide: VAGSAPGIEGDEIAPLAK Peptide: LGVAGSAPGIEGDEIAPLAKEN Peptide: GSAPGIEGDEIAPLAKE Peptide: VAGSAPGIEGDEIAP Peptide: GVAGSAPGIEGDEIAPLAK Peptide: GVAGSAPGIEGDEIAPLAKEN Peptide: VAGSAPGIEGDEIAPLAKEN Peptide: SAMGIEGDEIAPLAK Peptide: GSAPGIEGDEIAPLAK Peptide: SAPGIEGDEIAPLAKEN Peptide: FNPSTNPWHSPRQGS (also in P14323)

[0374] Protein Q9M3X6 [SEQ ID 681-699] Peptide: VDLVIPVNGPGK Peptide: LVDLVIPVNGPGK Peptide: IKLPAGTTSY Peptide: IKLPAGTTSYL Peptide: RRNPFLFKSNKF Peptide: IENPVKELTFPGSVQEINR Peptide: RRNPFLFKSNKFLT Peptide: AKPHTIFLPQHIDA Peptide: AKPHTIFLPQHIDAD Peptide: KQKYRYQRE Peptide: KQKYQYQRE Peptides: MLPH Peptide: RRNPFLFKSNKFLTLFENE Peptide: PFLFKSNKFLTLFE Peptide: SQERRNPFLFKSNKFLTLFE Peptide: RRNPFLFKSNKFLTLFE Peptide: SQERRNPFLFKSNKFLTLFENE Peptide: LTFPGSVQE Peptide: ELTFPGSVQEINR

[0375] Rice Protein: Q0D9D0 MLCLTSSSSSAPAPLLPSLADRPSPGIAGGGGNVRLSVVSSPRRSWPGKVKTNFSVPATA RKNKTMVTVVEEVDHLPIYDLDPKLEEFKDHFNYRIKRYLDQKCLIEKHEGGLEEFSKGY LKFGINTVDGATIYREWAPAAQEAQLIGEFNNWNGAKHKMEKDKFGIWSIKISHVNGKPA IPHNSKVKFRFRHGGGAWVDRIPAWIRYATFDASKFGAPYDGVHWDPPACERYVFKHPRP PKPDAPRIYEAHVGMSGEEPEVSTYREFADNVLPRIRANNYNTVQLMAIMEHSYYASFGY HVTNFFAVSSRSGTPEDLKYLVDKAHSLGLRVLMDVVHSHASNNVTDGLNGYDVGQNTHE SYFHTGDRGYHKLWDSRLFNYANWEVLRFLLSNLRYWMDEFMFDGFRFDGVTSMLYHHHG INKGFTGNYKEYFSLDTDVDAIVYMMLANHLMHKLLPEATIVAEDVSGMPVLCRPVDEGG VGFDFRLAMAIPDRWIDYLKNKEDRKWSMSEIVQTLTNRRYTEKCIAYAESHDQSIVGDK TIAFLLMDKEMYTGMSDLQPASPTINRGIALQKMIHFITMALGGDGYLNFMGNEFGHPEW IDFPREGNNWSYDKCRRQWSLVDTDHLRYKYMNAFDQAMNALEEEFSFLSSSKQIVSDMN EKDKVIVFERGDLVFVFNFHPNKTYKGYKVGCDLPGKYRVALDSDALVFGGHGRVGHDVD HFTSPEGMPGVPETNFNNRPNSFKVLSPPRTCVAYYRVDEDREELRRGGAVASGKIVTEY IDVEATSGETISGGWKGSEKDDCGKKGMKFVFRSSDEDCK [SEQ ID 705]

[0376] イネ Protein: Q6AVS5 MDRYQRVERPRPESAIEENEIRITAQGLIRNYVSYATSLLQDRIKEIVLKAMGQAISKS VAVAEIIKKRVPGLYQDTNISSVSITDVWEPIEEGLVPLEMTRHVSMISITLSPRLDDKN SPGYQTPVYVEQPRQQPRLQQAPPPPQRQVRQPPPDYEDSYVRGRGRGRGRGRGRGWGRG GYGGYGGYGNNQGGYNQGGGYYDNQGGYGGYDNQGGYGGYDNQGGYGGGGYGYNQGRYGN YQENGGYNRGRGGMRGRGNWNYRGGYERGRGGGFPGGRGYGGRGRGRMGGRGGRGN [SEQ ID 706]

[0377] イネ protein: Q8H920 MALEHLGRRNVAGSLLLLNLLMYVFLLGFAGWALNSSIKNAGADVGVGWGEQPWSPYYRQ SAWFASRFHLATFAALAGALGVAAKASAAYHGGRSGASWRPQGLAAAASLGTAAWAATAL AFGVACREIHDAAAAGPAGAARGWRMRALEGLTVTLAFTQLLYVLLLHAAVAGERCGLAC AADA [SEQ ID 707]

[0378] End protein: O49927 MAIKTKLSLTIFLFFLLLALLCSNLAVGRKEKDPELTTCKDQCDMQRQYDEEDKRICMERC DDYIKKKQERQKHKEHEEEEEQEQEEDENPYVFEDNDFETKIDTKDGRVLILNKFNEKSK LLKNIENYGLAVLEIKANAFLSPHHYDSEAILFNIKGRGIIGLVAEDRTERFNLEEGDIM RVPAGTPMYLVNRDENEKLYIAAFHMPPSSGSAPVNLEPFFESAGRKPESVLNTFSSKVL QAALKSSKGELETVLDEQKKGRIFKIEKEDVRGLAPKKSLWPFGGPFKSPFNIFSNNNPAF SNKFGSLFEVGPSQEKSGLEGLNLMLTLANITKGSMSTIHYNTNANKIALVIDGEGELEM ACPHMPSSSSNSRQKKSSISYHNINAKLRPGVMFVVPAGHPFVNIASKKKNLIVVCFEVN AQRNKKLAAGKKNIVSALDKAAKEVAFDIAAEKVDEVFERKEEFFFPYDNEERKEEHGR AVV [SEQ ID 708]

[0379] End protein: Q41000 MFRRATSTFLSRASATRRFSTDVATPATNSSFVEAWRKVSPNIDPKPKTPLEFLKTRPPVP STIPTKLTVNFVLPYSSQLAAKEVDSVIIPATTGEMGVLPGHVATIAELKPGVLTVQEGT DTTKYFVSSGFRFIHANSVADIIAVEAVPVNQLDRDLVQKGLQEFTQKLNSATTDLEKRE AQIGIDVDSALNSALTG [SEQ ID 709]

[0380] イネ protein: P20698 MKIIFFALLAIACSASAQFDAVTQVYRQYQLQPHLMLQQQMLSPCGEFVRQQCSTVAT PFFQSPVFQLRNCQVMQQQCCQQLRMIAQQSHCQAISSVQAIVQQLRLQQFASVYFDQSQ AQAQAMLALNMPSICGIYPSYNTAPCSIPTVGGIWY [SEQ ID 710]

[0381] End protein: O04434 MQDSSTMKFSPLDLMTAIIKGKFNPSNDSSQAPASIIFENREFVMILTTSIAVLIGCVVV LIWRRSNSNKSKQIEVPKLVIKKLPELDVDDGKKKVTVFFGTQTGTAEGFAKAIAEEAKA RYEKAKFRVVDMDDYAADDDDEYLEKLKRETMALFFLATYGDGGEPTDNAARFYKWFTEEYE GEEDSFKNLSYGVFGGLGNRQYEHFNKVAKVVDDKLLEQGGKRLVPVGLGDDDQCIEDDFT AWKEELWPALDQLLRDEDDTPVATPYTAAVSEYRVVIHDPLDATVDEKKRHNVNGHAVVD AQHPVRANVAVRRELHTPASDRSCTHLEFDISGTGVVYETGDHVGVYCENLSDTVEEAER ILGLSPDTYLSIHTDDEEGKPLGGSSLPPPFPPCTLRTALTKYADLLSSPKKSALVALAA HASDPSEADRLRHLASPAGKDEYAEWVISSQRSLLEVMAEFSSAKPPIGVFFAAVAPRLQ PRYYISSSSPRMAPSRIHVTCALVHDKMPTGRIHKGVCSTWMKNSVPLEKNQDCSWAPIF VRQSNFRLPADNKVPVIMIGPGTGLAPFRGFLQERLALKEDGAELGPSVLFFGCRNRQVD YIYEDELNHFVNGGALSELIVAFSRDGPTKEYVQHKMMEKASDIWNMISQGAYVYVCGDA KGMARDVHRTLHTILQEQGSLDSSKTESMVKNLQMTGRYLRDVW [SEQ ID 711]

[0382] Rice protein: Q5N725 MSAYCGKYKDELIKNAAYIGTPGKGILAADESTGTIGKRFASINVENVEENRRSLRELLF TTPGALQHLSGVILFEETLYQKTKDGKPFVDVLKEGGVLPGIKVDKGTVEVAGTNKETTT QGHDDLGKRCAKYYEAGARFAKWRAVLKIGPNEPSQLSIDLNAQGLARYAIICQENGLVP IVEPEILVDGSHDIERCAYVTEKVLAACYKALNEHHVLLEGSLLKPNMVTPGSESKKVSP QLIAEYTVRALQRTVPAAVPAIVFLSGGQSEEEATVNLNAMNKLSTKKPWALSFSFGRAL QQSTLKAWGGKTENVVKAQKAFITRCKANSEATLGTYQGDAVLGEGASESLHVKDYKY [SEQ ID 712]

[0383] Pea Protein: B5A8N6 MASLQTQMISFYAIFLSILLTTILFFKVNSTETTSFLITKFSPDQQNLIFQGDGYTTKEK LTLTKAVKNTVGRALYSSPIHIWDRETGNVANFVTSFTFVINAPNSYNVADGFTFFIAPV DTKPQTGGGYLGVFNSAEYDKTTQTVAVEFDTFYNAAWDPSNRDRHIGIDVNSIKSVNTK SWKLQNGEEANVVIAFNAATNVLTVSLTYPNSLEEENVTSYTLSDVVSLKDVVPEWVRIG FSATTGAEYAAHEVLSWSFHSELSGTSSSKQAADA [SEQ ID 713]

[0384] Rice protein: Q6K508 MATTTSLLSSCLCALLLAPLFSQGVDAWESRQGASRQCRFDRLQAFEPLRKVRSEAGDTE YFDERNEQFRCAGVFVIRRVIEPQGLVVPRYSNTPALAYIIQGKGYVGLTFPGCPATHQQ QFQLFEQRQSDQAHKFRDEHQKIHEFRQGDVVALPASVAHWFYNGGDTPAVVVYVYDIKS FANQLEPRQKEFLLAGNNQRGQQIFEHSIFQHSGQNIFSGFNTEVLSEALGINTEASKRL QSQNDQRGDIIRVKHGLQLLKPTLTQRQEEHRQYQQVQYREGQYNGLDENFCTIKARVNI ENPSRADYYNPRAGRITLLNNQKFPILNLIGMGAARVNLYQNALLSPFWNINAHSVVYII QGSVRVQVANNQGRSVFNGVLHQGQLLIIPQNHAVIKKAEHNGCQYVAIKTISDPTVSWV AGKNSILRALPVDVIANAYRISRDEARRLKNNRADEIGPFTPRFPQKSQRGYQFLTEGLS LIGM [SEQ ID 714]

[0385] Pea Protein: Q712V4 QKAPRKQLATKAARKSAPATGGVKKPHRFRPGTVALREIRKYQKSTELLIRKLPFQRLVR EIAQDFKTDLRFQSSAVSALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRG ERA [SEQ ID 715]

[0386] Linked Co. Number: P09886 MAQSVSLSTIASPILSQKPGSSVKSTPPCMASFPLRRQLPRLGLRNVRAQAGGDGDNKDN SVEVHRVNKDDQGTAWORKPRRSSIDISPFGLLDPWSPMRSMRQMLDTMDRIFEDAITIP GRNIGGGEIRVPWEIKDEEHEIRMRFDMPGVSKEDVKVSVEDDVLVIKSDHREENGGEDC WSRKSYSCYDTRLKLPDNCEKEKVKAELKDGVLYITIPKTKIERTVIDVQIQ [SEQ ID 716]

[0387] Remove the snowflake from the snowflake P13918 (Carlington) >gi|137584|sp|P08438.1|VCL_VICFA RecName: Full=Vicillin; Flags: Precursor [Vice faba] >gi|22057|emb|CAA68559.1| vicilin [Vicia faba var. minor] >gi|383931031|gb|AFH56916.1| vicilin [Vica faba] MAATTLKDSFPLLTLLGIAFLASVCLSSRSRDQDNPPFVFESNRFQTLFENENGHIRLLQFDQHSKLLENLQNYRLLEYKSKPHTIFLPQTDADFILVLSGKAILTVLLPNDRNS FSLERGDTIKLPAGTIGYLVNRDDEEDLRVLDLVIPVNRPGEPQSFLLSGNQNQPSILSGSKNILEASFNTDYKEIEKVLLEEHGKEKYHRRGLKDRRQRGQEENVIVKISRKQIE ELNKNAKSSSKKSTSEPFNLRREPIYSNKFGKFFEITPKRNPQDLQDLNIFVNYVEINEGSLLLPHYNSRAIVTVNEGKGDFELVGQRNENQGLREEYDEEKEQGEEEIRK QVQNYKAKLSPGDVLVIPAGYPVAIKASSNLNLVGFGINAENNQRYFLAGEEDNVISQIHKPVKELAFPPGSAQEVDTLENQQSHFANAQPRERERGSQEIKDHLYSILGSF[SEQ ID 506]

[0388] >gi|502105533|ref|XP_004492829.1| PREDICTED: vicilin-like isoform X1 [Cicer arietinum] ChickPea MAIKARFPLLVLLGIVFLASVCAKSDKENPFFFKSNNCQTLFENENGHVRLLQRFDKRSQLFENLQNYRLMEYNSKPHTLFLPQHNDADFILVVLRGRAILTVLNPNDRNTF KLERGDTIKLPAGTIAYLANRDDNEDLRVLDLAIPVNRPGQFQSFSLSGNENQQSYFQGFSKKILEASFNSDYEEIERVLLEEQEQKPEQRRGHKGRQQSQETDVIVKISREQ IEELSKNAKSNCKKSVSSESEPFNNLRSRSPIYSNRFGNFFEITPEKNPQLKDLDIFVNSVEIKEGSLLLPHFNSRATVILVVNEGKGEVELVGLRNENEQENKKEDEEEEED RNVQVQRFQSKLSSGDVVVIPASHPFSINASSDLFLLGFGINAQNNQRNFLAGEEDNVISQIQRPVKEVAFPGSAEEVDRLLKNQRQSHFANAQPQQKRKGSQRIRSPF[SEQ ID 507]

[0389] >gi|29539109|emb|CAD87730.1| allergen Len c 1.0101 [Lens culinaris] Lentil SRSDQENPFIFKSNRFQTIYENENGHIRLLQRFDKRSKIFENLQNYRLLEYKSKPHTIFLPQFTDADFILVVLSGKAILTVLNSNDRNSFNLERGDTIKLPAGTIAYLANRDDNEDLRVLDLAIPVNRPGQLQSFLLSGTQNQPSFLSGFSKNILEAAFNTEYEEIEKVLLEEQEQKSQHRRSLRDKRQEITNEDVIVKVSREQIEELSKNAKSSSKKSVSSESEPFNLRSRNPIYSNKFGKFFEITPEKNPQLQDLDIFVNSVEIKEGSLLLPNYNSRAIVIVTVNEGKGDFELVGQRNENQQEQREENDEEEGQEEETTKQVQRYRARLSPGDVLVIPAGHPVAINASSDLNLIGFGINAKNNQRNFLAGEEDNVISQIQRPVKELAFPGSSREVDRLLTNQKQSHFANAQPLQIE[SEQ ID 508]

[0390] Q9M3X6 (エンドウマメ) >gi|164512526|emb|CAP06312.1| cvc [Pisum abyssinicum] MATTVESRFPLLLFPGIIFLASVCVTYANYDEGSETRVPGQRERGRQEGEKEEKRHGEWRPSYEKEEDEEEKQKYRYQREKEDEEEKQKYRYQREKKEEKEVQPGRERWEREEDEEQVDEEWRGSQRRQDPEERARLRHREERTKRDRRHKREGEEEERSSESQEQRNPFLFKSNKFLTLFENENGHIRRLQRFDKRSDLFENLQNYRLVEYRAKPHTIFLPQHIDADLILVVLNGKAILTVLSPNDRNSYNLERGDTIKIPAGTTSYLVNQDDEEDLRVVDFVIPVNRPGKFEAFGLSENKNQYLRGFSKNILEASLNTKYETIEKVLLEEQEKKPQQLRDRKRRQQGGERDAIIKVSREQIEELRKLAKSSSKKSLPSEFEPFNLRSHKPEYSNKFGKLFEITPEKKYPQLQDLDILVSCVEINKGALMLPHYNSRAIVVLLVNEGKGNLELLGLKNEQQEREDRKERNNEVQRYEARLSPGDVVIIPAGHPVAISASSNLNLLGFGTNAENNQRNFLSGSDDN[SEQ ID 509]

[0391] >gi|164512538|emb|CAP06318.1| cvc [Lathyrus annuus] [SEQ ID 510]

[0392] >gi|164512558|emb|CAP06328.1| cvc [Villa villosa] [SEQ ID 511]

[0393] P09918 (エンドウマメ) >gi|357454557|ref|XP_003597559.1| Seed lipoxygenase-3 [Medicago truncatula] >gi|355486607|gb|AES67810.1| seed linoleate 9S-lipoxygenase [Medicago truncatula] MFSGVTGILNRGHKIKGTVVLMRKNVLDINSLTSVGGVIGQGFDILGSTLDNLTAFLGRSVSLQLISATKPDANGKGKLGKATFLEGIITSLPTLGAGQSAFKIHFEWDDDMGIPGAFYIKNFMQTEFFLVSLTLEDIPNHGSIYFVCNSWIYNAKHHKLDRIFFANKAYLPSETPAPLVHYREEELNNLRGDGTGERKEWERIYDYDVYNDLGNPEKGDNHARPVLGGSDTYPYPRRGRTGRKPNPKDPKSESRSDFVYLPRDEAFGHLKSSDFLTYGLKAVSQNVVPALESVIFDLNFTPNEFDSFDEVHGLYEGGIKLPTDVLSKISPLPVLKEIFRTDGEQFLKYPPPKVLQVSRSAWMTDEEFAREMLAGVNPNVICCLQEFPPRSKLDSQVYGDHTSKITKEHLEPNLEGLTVEEAIQNKKLFLLDHHDSIMPYLRRINSTPTKAYATRTILFLSSDKTLKPLAIELSLPHPDGDEHGAVSHVYQPALEGVESTIWLLAKAYVVVNDSCYHQLVSHWLNTHAVVEPFVIATNRHLSYLHPIYKLLYPHYRDTMNINSLARQSLVNDGGIIEKTFLWGRYSMEMSSKVYKNWTLPGQALPADLIKRGMAIEEPSSPCGVKLVVEDYPYAHDGLEIWAAIKTWVQDYVSLYYTTDDILRQDSELQAWWKELVEVGHGDKKNEPWWPKMQAREELVEVCTTVIWIASALHAAVNFGQYSYGGLILNRPTLSRRFMPEKGSAEYNELVKSPQKAYLKTITPKFQTLIDLSVIEILSRHASDEVYLGERDNPNWTSDTRALEAFKKFGNKLAEIEKNLAQRNNDEKLRHRLGPVQMPYTLLHPSSEEGLTFRGIPNSISI[SEQ ID 512]

[0394] >gi|734403888|gb|KHN32710.1| Seed linoleate 9S-lipoxygenase-3 [Glycine soja] MLGGLLHRGHKIKGTVVLMRKNVLDVNSVTSVGGIIGQGLDLVGSTLDTLTAFLGRSVSLQLISATKADANGKGKLGKATFLEGIITSLPTLGAGQSAFKINFEWDDGSGIPGAFYIKNFMQTEFFLVSLTLEDIPNHGSIHFVCNSWIYNAKLFKSDRIFFANQTYLPSETPAPLVKYREEELHNLRGDGTGERKEWERIYDYDVYNDLGDPDKGENHARPVLGGNDTFPYPRRGRTGRKPTRKDPNSESRSNDVYLPRDEAFGHLKSSDFLTYGLKSVSQNVLPLLQSAFDLNFTPREFDSFDEVHGLYSGGIKLPTDIISKISPLPVLKEIFRTDGEQALKFPPPKVIQVSKSAWMTDEEFAREMLAGVNPNLIRCLKDFPPRSKLDSQVYGDHTSQITKEHLEPNLEGLTVDEAIQNKRLFLLDHHDPIMPYLRRINATSTKAYATRTILFLKNDGTLRPLAIELSLPHPQGDQSGAFSQVFLPADEGVESSIWLLAKAYVVVNDSCYHQLVSHWLNTHAVVEPFIIATNRHLSVVHPIYKLLHPHYRDTMNINGLARLSLVNDGGVIEQTFLWGRYSVEMSAVVYKDWVFTDQALPADLIKRGMAIEDPSCPHGIRLVIEDYPYAVDGLEIWDAIKTWVHEYVFLYYKSDDTLREDPELQACWKELVEVGHGDKKNEPWWPKMQTREELVESCAIIIWTASALHAAVNFGQYPYGGLILNRPTLSRRFMPEKGSAEYEELRKNPQKAYLKTITPKFQTLIDLSVIEILSRHASDEVYLGERDNPNWTSDTRALEAFKRFGNKLAQIENKLSERNNDEKLRNRCGPVQMPYTLLLPSSKEGLTFRGIPNSISI[SEQ ID 513]

[0395] >gi|593700103|ref|XP_007150490.1| hypothetical protein PHAVU_005G157000g [Phaseolus vulgaris] >gi|561023754|gb|ESW22484.1| hypothetical protein PHAVU_005G157000g [Phaseolus vulgaris] [SEQ ID 514]

[0396] P02857 (キンドウマメ) >gi|483449|emb|CAA83677.1| legume A [Vicia sativa] MAKLLALSLSFCFLLFSSCFALREQSQQNECQLERINALEPDNRIESEGGLIETWNPNNRQFRCARVALSRATLQRNALRRPYYSNAPQEIQGNGYFGMVFPGCPETHEEPQQSEQGEGRRY RDSHQKVNRFREGDIAVPTGIAFWMYNDQDTPVIAISLTDTGSSNNQLDQMPRRFYLAGNQEQEFLRYQHQGGKQDNDGNNIFSGFKRDFLEDAFNVNRHIVDRLQGRNEDEEKGAIVKVKG GLSIAPPERQARHERGSRQEEDEDEKEERQPSHHKSRRDEDDKKRHSQKGQSRRQGDNGLEETVCTAKLRANIGSSPSPDIYNPQAGRIKTVTSLDLPVLRWLKLSAEHGSLHKNAMFVPH YNLNANSVIYALKGRARLQVVNCNGNTVFDGELEAGRALTVPQNYAVAAKSERFTYVAFKTDDRASIARLAGTSSVIDDLPLDVVAATFNMQRNEARQLKSNNPFKFLVPPRQSEMRASA[SEQ ID 515]

[0397] >gi|600108|emb|CAA86824.1| legumin A precursor [Vicia narbonensis] MAKLLALSLSLCFLLFSNSFALREQSQQNECQLERLDALEPDNRIESEGGLIETWNPNNRQFRCAGVALSRVTLQRNALRRPYYSNAPQEIQGNGYFGVVFPGCPETFEEPQESEQRE RRRYRDSHQKVNRFREGDIAVPTGNVLWMYNDQDTPVIAISLTDTGSSNNQLDQIPRRFYLAGNQEQEFLRYQREQGGKQQENDGNIFSGFKRDFLEDALNVNRHIVDRLQGRNEDEEK GAIVKVKGGLSIITPPERQRGSRQEEDEDEKEERQPSRRRDESQKGESRRHGDNGLEETVCTAKLRVNIGSSPSPDIYNPQAGRINTVTSLDLPVLRWLKLSAEHGSLRKNALIVPHYNRN ANSVIYALKGRARLQVVNCNGNTVFDGELEAGRALTVPQNYAVAXLSERFTYVAFKTNDRDGIARLAGTSSVINDLPLDVVAATFNLQRNEARQLKSNNPFKLLVPPRESEKRASA[SEQ ID 516]

[0398] >gi|502110016|ref|XP_004493779.1| PREDICTED: legumin-like [Cicer arietinum] MAKLLALSLSFCFLLFGSCFALRDQPEQNECQLEHLNALEPDNRIKSEGGLIETWNPSNKQFRCAGVALSRATLQPNSLRRPFYTNAPQEIFIQQGNGYFGMVFPGCVETFEEPRESEQGEGSKF RDSHQKVNRFREGDIAVPTGVVFWMFNDQDTPVIAVSLIDTSSFQNQLDQMPRRFYLAGNHEXXXXXXXXQEGSEEEENEGGNIFSGFKRDFLEDALNVNRRIVNKLQGRNEDEEKGAIVKVKG GLSIITPPEKEPRQKRGSRQEEDEDEDEKRQPHRHSRQDEDEDEKRQPRRHSRGGSKSQRDNGFEETICTARLHQNIGSSSSPDIYNPQAGRICTVTSFDLPALRFLKLSAEFGSLHKNAMFVPHY NLNANSILYALKGRARLQIVNCKGNSWFDGELEAGRALIVPQNFAIAAKSLSDRFSYVAFKTNDRAIGRLLGASSLINGMPEEVVAAAFNMERNEARQLKFNSPFSFLVPPRSDSDNKAAA[SEQ ID 517]

[0399] P02855 (エンドウマメ) >gi|164512536|emb|CAP06317.1| cvc [Lathyrus hirsutus] [SEQ ID 518]

[0400] >gi|164512542|emb|CAP06320.1| cvc [Lathyrus cicera] MATIIKSRFPLLLLLGIIFLASVCVTLANYDEGSEPRVPAQRERGRQEGEKEEKRHGEWRPSHEKEYDEGSEPRVPGRRERGRQEGEKEEKRHGEWRPSYEKEYDEGSEPRVPGRRERGRQEGEKEEKRHGEWRPSYEKEYDEEEKQKYQYEREKEEQKEVQPGRERWERKEDEEKEEDQWRGSQRHEDPEERARLRYRKERTKKYVEEDTEETSSESQGRRNPFLFKSNKFLTLFENENGYIRRLQRFDERSDIFENLQNYRLVEYRAKPHTIFLPQHIDADLILVILNGKAILTVLSPNDRNSYNLERGDTIKLPAGTTSYLVNEDDEEDLRVVDLVIPVNRPGKFEAFDLNQYLGGFSKSVLEASLNTKYETIEKVLLEEQQKQGQETNAIVKVSREQIEELRKLAKSSSKKSLLSELEPVNLRSHSPKYSNKFGKFFEITPEKKYPQLQDLDVSISCVEINEGALLLPHYNSRAIVVVLVNEGKGNLELLGVQNEDEQQERKERNKEVQRYEARLSPGDVVIIPSGHPVAVSASSNLNLLGFGINAENNQRNFLSGSDDN[SEQ ID 519]

[0401] >gi|164512544|emb|CAP06321.1| convicilin [Lathyrus sativus] [SEQ ID 520]

[0402] D3VNE1 (エンドウマメ) >gi|357507721|ref|XP_003624149.1| Provicilin [Medicago truncatula] >gi|87162569|gb|ABD28364.1| Cupin, RmlC-type [Medicago truncatula] >gi|355499164|gb|AES80367.1| vicilin 47 kDa protein [Medicago truncatula] MAIKAPFQLLMLLGIFFLASVCVSSRDDRHDQENPFFFNANHFQTLFENENGHIRLLQRFDKRSKIFENLQNYRLLEYHSKPHTLFLPQHNDADFILAVLSGKAILTVLNPDNRNS FNLERGDTIKLPAGSIAYLANRDNEDLRVLDLAIPVNRPGKFQSFLSGSQNQQFFSGFSKNILEAAFNANYEEIERVLIEEEHEQEPQHRRGLRKDRRQQSQDSNVIVKVSREQI EELSRHAKSSSRRSSESAPFNLRSREPIYSNEFGNFFEITPEKNPQLKDLDILVNYAEIREGSLLLPHFNSRATVIVVVDEGKGEFELVGQRNENQQREEDEQQEEERSQQVQ RYRARLSPGDVYVIPAGHPTVVSASSDLSLLGFGINAENNERNFLAGEEDNVISQIERPVKEVAFPPGSAQDVESLLKNQRQSYFANAQPQQREREEGRSQRQRELISSILGVF[SEQ ID 521]

[0403] >gi|164512560|emb|CAP06329.1| convicilin [Vicia peregrina] MATTFKSRFSLLLLLGIIFLAFVCVTCANYDEGSEPRVPGQRERGRQEGEKEEQSRERHPQREPSREKEEDEEEKQKYDEGTEPRVPGQRERGRQEGEKEEQRRERHPGQREPSQEEDEEREESDRRQEGSSKSEEQRNPFLFKSNKFLTLFQNGNGHIRLLQRFDKRSDLFENLQNYRLLEYRAKPHTIFLPQHIDADLILVVLSGRAILTVLSPDDRNSYNLERGDTIKLPAGTTSYPLNQDDEEDLRVVDLAISVNRPGKVESFNLSGNKNQYLRGFSENILEASFNTKYETIEKVLLEEQDKESQQPRGQRLQRQETNALVKVSREQVEELKRLARTSSKKGVSSEFEPFNLRSHGPKYSNKFGKFFEITPEKKYPQLQDLDISVSSVEINEGALFLPHYNSRAIVVVLVDEGKGNLELVGFKNEQQEQREKEDEQEERNKQVQRYEAKLSPGDVVIIPAGHPVAVSASSNLNLLGFGINAENNQRNFLTGSDDN[SEQ ID 522]

[0404] >gi|164512562|emb|CAP06330.1| convicilin [Vicia lutea] MATTIKLRFPLLLLLGVILLASVCVTCANYDEGSEPRVPGRPEGEKEEKHRGKLRPSYEKEEDEGEKQRYHYEKKEQKEQPRREKKEQKEEEKQVEEESQRYEDPGERARERYRAEIIKRQVEKE REERDRRHQREGEEEEGSSKSRNPFLFKSNNFLTLFENENGHIRLLQRFDKRSDLFENLQNYRLVEYRAKPHTIFLPQHIDADLILVLSGKAILTVLSPNNRNSYNLKRGDTIKLPAGTTSYLLNSDDE EDLRMVDLAISVNRPGKVESFNLSGNKNQYLRGFSKNILEASFNTKYETIEKVLLEEQDKESQSIGQKRISQRQETNALVKVSREQIEEPKRLARSSSRKGVSSEFEPINLRSQRPKYSNKFGKFYEIS PECKYPQLQDLDVSVSSVEINEGALLLPHYNSRAIVTVLVNEGKGNLELIGFQNEQGQREKEDEQHERNKQVQRYDARLSSGDVVIIPAGHPAVSASSNLDLLGFGINAENSQRNFLTGSDDN[SEQ ID 523]

[0405] P07728 (イネ) >gi|531874314|gb|AGT59174.1| glutelin, partial [Oryza sativa Indica Group] CRFDRLQAFEPIRSVRSQAGTTEFFDVSNEQFQCTGVSAVRVIEPRGLLLPHYTNGASLVYIIQGRGITGPTFPGCPESYQQFQQSGQQLTESQSQSHKFKDEHQKIHRFR QGDVIALPAGVAHWCYNDGEVPVVAIYVTDLNNGANQLDPRQRDFLAGNKRNPQAYRREVEERSQNIFSGFSTELLSEALGVSSQVARQLQCQNDQRGEIVRVEHGLSLLQPYA SLQEQGQVQSRERYQEGQYQQSQYGSGCSNGLDETFC™KVRQNIDNPNRADTYNPRAGRVTNLNTQNFPILNLVQMSAVKVNLYQNALLSPWNINAHSSVVYITQGRARVQ VVNNNGKTVFNGELRRGQLLIIPQHYAVVKKAQREGCAYAFKTNPNSMVSHIAGKSSIFRALPNDVLANAYRISREEAQRLKHNRGDEFGAFTPIQYKSYQDVYNAAESS[SEQ ID 524]

[0406] >gi|109894635|gb|ABG47337.1| glutelin precursor [Zizania latifolia] MNMATINGPTIFFTVCLFLLCHGSLAQLLGQSTSQWQSSHRGSSRQCRFDRLQAFEPVRSVRSQAGTTEFFDASNELFQCAGVSIVRRIIEPRGLLLPQYTNGATIMYIIQGRGITGQTFPGCPESYQQQFQQSMQAQLTGSQSQSQKFKDEHQKINRFRQGDVIALPAGVAHWCYNDGEVPVVAIYVIDINNAANQLDPRQRDFLLAGNMRSPQAYRREVENQSQNIFSGFSAELLSEALGISTGVARQLQCQNDQRGEIVRVEHGLSLLQPYASLQEQEQKQEQPRERYQVTQHQQSQYGGGCSNGLDETFCAMRIWQNIDNPNLADTYNPRAGRVTNLNSQKFPILNLIQMSAVKVNLYQNALLSPFWNINSHSVVYVTQGCARVQVVNNNGKTVFNGELRRGQLLIIPQHYVVVKKAQREGCAYIAFKTNPNSMVSHIVGKSSIFRALPTDVLANAYRISREDAQRLKHNRGDELGAFTPLQYKSYQDVSSVAASS[SEQ ID 525]

[0407] >gi|472867|emb|CAA52764.1| 11S globulin [Avena sativa] [SEQ ID 526]

[0408] P14614 (イネ) >gi|115445309|ref|NP_001046434.1| Os02g0248800 [Oryza sativa Japonica Group] >gi|37993738|gb|AAR06952.1| glutelin type-B [Oryza sativa Japonica Group] >gi|47497729|dbj|BAD19794.1| glutelin type-B [Oryza sativa Japonica Group] >gi|113535965|dbj|BAF08348.1| Os02g0248800 [Oryza sativa Japonica Group] >gi|215768942|dbj|BAH01171.1| unnamed protein product [Oryza sativa Japonica Group] >gi|284431772|gb|ADB84627.1| glutelin [Oryza sativa Japonica Group] MTISVFSRFSIYFCVLLLCNGSMAQLFDPATNQWQTHRQGSFRECRFERLQAFEPLQNVRSEAGVTEYFDETNELFQCTGTFVIRRVIQPQGLLIPRYANTPGMVYIIQGRGSMGLTFPGCPATYQQQSQQFLFQGESQSQKFIDEHQKIHQFRQGDIVVLPTGVAHWFYNDGDTPVVALYVYDINNSANQLEPRHREFLLAGKNNRVQQVYGRSIQQHSGQNIFNGFSVEPLSEALNINTVTTKRLQSQNDQRGEIIHVKNGLQLLKPTLTQRQEQEQAQYQEVQYSEKPQTSSRWNGLEENLCTIKTRLNIENPSRADSYDPRAGRITSLDSQKFPILNIIQMSATRVNLYQNAILTPFWNVNAHSLMYVIRGRARVQVVSNFGKTVFDGVLRPEQLLIIPQNYVVLKKAQHEGCQYIAINTNANAFVSHLAGVDSVFHALPVDVIANAYCISREEARRLKNNRGDEYGPFPPRLQQQIYPEFSNESKGETSE[SEQ ID 527]

[0409] >gi|428674402|gb|AFZ41188.1| glutelin, partial [Oryza sativa Japonica Group] LLCHGSMAQIFSLGINPWQNPRQGGSRECRFDRLQAFEPLRKVRHEAGVTEYFDEKNEQFQCTGTLVIRRIIEPQGLLLPRYSNTPGLVYIIQGTGVLGLTFPGCPATYQKQFRHFGLEGGSQRQGKKLRDENQKIHQFRQGDVVALPSGIPHWFYNEGDTPVVALFVFDVNNNANQLEPRQKEFLLAGNNIEQQVSNPSINKHSGQNIFNGFNTKLLSEALGVNIEVTRRLQSQNDRRGDIIRVKNGLRLIKPTITQQQEQTQDQYQQIQYHREQRSTSKYNGLDENFCAIRARLNIENPNHADTYNPRAGRITNLNSQKFSILNLVQMSATRVNLYQNAILSPFWNINAHSLVYTIQGRARVQVVSNHGKAVFNGVLRPGQLLIIPQNYVVMKKAELEGFQFIAFKTNPNAMVNHIAGKNSVLRAMPVDVIANAYRISRQEARSLKNNRGEEIGAFTPRYQQQKIHQEYSNPNESETQ[SEQ ID 528]

[0410] >gi|226510|prf||1515394A seed storage globulin MATTRFPSLLFYSCIFLLCNGSMAQLFGQSFTPWQSSRQGGLRGCRFDRLQAFEPLRQVRSQAGITEYFDEQNEQFRCAGVSVIRRVIEPQGLLLPQYHNAPGLVYILQGRGFTGLTFPGCPATFQQQFQ PFDQARFAQGQSKSQNLKDEHQRVHHIKQGDVVALPAGIVHWCYNDGDAPIVAVYVFDVNANQLEPRQKEFLLAGNNKREQQFGQNIFSGFSVQLLSEALGISQQAAQKIQSQNDQRGEIIRVSQGLQF LKPFVSQQGPVEHQAYQPIQSQQEQSTQYQVGQSPQYQEGQSTQYQSGQSWDQSFNGLEENFCSLEARQNIENPKRADTYNPRAGRITHLNSKNFPTNLVQMSATRVNLYQNAILSPYWNINAHSVMHM IQGRARVQVVNNHGQTVFNDILRRGQLLIIPQHYVVLKKAEREGCQYSFKTTPNSMVSYIAGKTSILRALPVDVLANAYRISRQESQNLKNNRGEEFGAFTPKFAQTGSQSYQDEGESSSTEKASE[SEQ ID 529]

[0411] P07730 (イネ) >gi|225959|prf||1404367A glutelin MASTNRPIVFFTVCLFLLCDGSLAQQLLGQSTSQWQSSRRGSPRGCRFDRLQAFEPIRSVRSQAGTTEFFDVSNELFQCTGVSVVRRVIEPRGLLLPHYTNGASLVYIIQGRGITGPTFPGCPETYQQQFQQSGQAGLTESQSQSHKFKDEHQKIHRFRQGDVIALPAGVAHWCYNDCEVPVVAIYVTDINNGANQLDPRQRDFLLAGNKRNPQAYRREVEEWSQNIFSGFSTELLSEAFGISNQVARQLQCQNDQKGEIVRVERGLSLLQPYASLQEQEQGQMQSREHYQEGGYQQSQYGSGCPNGLDETFCVNKVRQNIDNPNRADTYNPRAGRVTNLSQNFPILNLVQMSAVKVNLYQNTDTWISMGQEENALLSPFWNINAHSIVYITQGRAQVQVLRRGQLLIVPQHYVVVKKAQREGCAYIAFKTNPNSMVSHIAGKSSIFRALPTDVLANAYRISREEAQRLKHNRGDEFGAFTPLQYKSYQDVYNVAESS[SEQ ID 530] >gi|573943558|ref|XP_006654150.1| PREDICTED: glutelin type-A 3-like [Oryza brachyantha] MKSSIVFSTICLVLLCHGSLAQLLSQSTSQWQSSRRGSPRQCRFDQLQAFEPIRTVRSQAGVTEFYDVSNELFQCTGVSVVRRVIEPRGLLLPHYSNGATLVYIIQGRGITGPTFPGCPETYQQQFQQSGEAQPFEGQSHKFRDEHQKIHRFRQGDVVALPAGVAHWCYNDGEVPIVAIYVTDIYNSANQLDPRHRDFFLAGNNKVAQQLYRSEARENSKNIFGGFSVELLSEALGISRGVARQLQCQNDQRGEIVRVEHGLALLQPYASVQEQQQEQVQSRDYEQTQYQQKQPQGSCSNGLDETFCTMRLRQNIDNPNLADTYNPKAGRITYLNGQKFPILNLVQMSAVKVNLYQNAVLSPFWNINAHSVVYITQGRARVQVVNNNGKTVFDGELRQGQLLIIPQHHVVLKKAQREGCSYIALKTNPNSIVSHIAGKNSIFRALPGDVVTNAYRISREEAKRIKHNRGDESGVFAPSHAYRSYQDMSVAA[SEQ ID 531]

[0412] >gi|721641733|ref|XP_010231907.1| PREDICTED: 12S seed storage globulin 1-like [Brachypodium distachyon] MAHTSFSSFLSYFCLFLLFHGSMAQVLGQVSTWQSSRQGGSRDCSFDRLQAIEPVTQVRSQAGLTEYFDEQNEQFRCAGVFVIRRVIEPRGLLLPRYHNTPGLVYILQGNGFVGLTFPGCPETFREQFQQFRQTQSTLGQSQCQSQKLGDVHQRVHQFTQGDVVALPTGVAHWIYNGGDAPVVIVYVFDVNNNANQLEPRQKEFLLGGNYNGVLQYGQNIFSGFNAQLLSQAFGINEQTSQRIQNQNDGRGDIIRVDNGLQFLKPVVTQQQPEQPFMPIQHQTGQSSRNGLEENFCSLEPRQNIEDPNRADTYNPRAGSITRLNGQNFPILNLVQMSATRVNLQKNAILSPFWNINAHSVVYVIQGHALVQVVNNQGHNVFNGLLHRGQLLIIPQNYVVLKKAESEGYQYIAFKTNANSMVSHIAGKNSILRALPVDVIANAYRISRQEAQNLKNNRGEETGVLTPNFSQSTCQSYQTEDVQSLRPMSHWSE[SEQ ID 532]

[0413] Q0D7S0 (イネ) >gi|169244463|gb|ACA50505.1| seed allergenic protein RAG2 [Oryza sativa Japonica Group] MASNKVVFSALLLIIVSVLAATATMADHHKDQVVYSLGERCQPGMGYPMYSLPRCRAVVKRQCVGHGAPGGAVDEQLRQDCCRQLAAVDDSWCRCSALNHMVGGIYRELGATDVGHPMAXVFPGCRRGDLERAAASLPAFCNVDIPNGTGGVCYWLGYPRTPRTGH[SEQ ID 533]

[0414] >gi|5777592|emb|CAA44001.1| low molecular weight globulin [Oryza sativa] MASNKVVFSALLLIIVSVLRRDGTMADHHKDQVVYSLGERCQPGMGYPMYSLPRCRAVVKRQCVGHGAPGAVDEQLRQDCCRQLAAVDDSWCRCSALNHMVGGIYRELGATDVGHPMAEVFPGCRRGDLERAAASLPAFCNVDIPNGTGGVCYWLGYPRTPRTGH[SEQ ID 534]

[0415] >gi|115471175|ref|NP_001059186.1| Os07g0214600 [Oryza sativa Japonica Group] >gi|23616954|dbj|BAC20657.1| allergen RA16 [Oryza sativa Japonica Group] >gi|113610722|dbj|BAF21100.1| Os07g0214600 [Oryza sativa Japonica Group] >gi|125557687|gb|EAZ03223.1| hypothetical protein OsI_25372 [Oryza sativa Indica Group] SEQ ID 535

[0416] Q0DEV5 (イネ) >gi|83375868|gb|ABC17777.1| waxy [Oryza rufipogon] MSALTTSQLATSATGFGIADRSAPSSLLRHGFQGLKPRSPAGGDATSLSVTTSARATPKQQRSVQRGSRRFPSVVVYATGAGMNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRYDQYKDAWDTSVVAEIKVADRYERVRFFHCYKRGVDRVFVDHPSFLEKVWGKTGEKIYGPDTGVDYKDNQMRFSLLCQAPRILNLNNNPYFKGTYGEDVVFVCNDWHTGPLASYLKNNYQPNGIYRNAKVAFCIHNISYQGRFAFEDYPELNLSERFRSSFDFIDGYDTPVEGRKINWMKAGILEADRVLTVSPYYAEELISGIARGCELDNIMRLTGITGIVNGMDVSEWDPSKDKYITAKYDATTAIEAKALNKEALQAEAGLPVDRKIPLIAFIGRLEEQKGPDVMAAAIPELMQEDVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFHMGRLSVDCKVVEPSDVKKVAATLKRAIKVVGTPAYEEMVRNCMNQDLSWKGPAKNWENVLLGLGVAGSAPGIEGDEIAPLAKENVAAP[SEQ ID 536]

[0417] >gi|297614332|gb|ADI48504.1| glycogen synthetase [Oryza officinalis] MSALTTSQLATSATGFGIADRSAPSSLLRHGFQGLKPRSPAGGDASSLSVTTSARATPKQQRSVQRGSRRFPSVVVYATGAGMNVVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVISPRHDQYKDAWDTSVVAEIKVADRYERVRFFHCYKRGVDRVFIDHPSFLEKVWGKTGEKIYGPDTGVDYKDNQMRFSLLCQAALEAPRILNLNNNPYFKGTYGEDVVFVCNDWHTGPLPSYLKNNYQPNGIYRNAKVAFCIHNISYQGRFAFEDYPELNLSERFRSSFDFIDGYDTPVEGRKINWMKAGILESDRVLTVSPYYAEELISGIARGCELDNIMRLTGITGIVNGMDVSEWDPSKDKYIAAKYDATTAIEAKALNKEALQAEAGLPVDRKIPLIAFIGRLEEQKGPDVMAAAIPELMQENVQIVLLGTGKKKFEKLLKSMEEKYPGKVRAVVKFNAPLAHLIMAGADVLAVPSRFEPCGLIQLQGMRYGTPCACASTGGLVDTVIEGKTGFHMGRLSVDCKVVEPSDVQKVATTLKRAIKIVGTPAYNEMVRNCMNQDLSWKGPAKNWENVLLGLGVAGSAPGVEGEEIAPLAKENVAAP[SEQ ID 537]

[0418] >gi|389620054|gb|AFK93486.1| granule-bound starch synthase [Hordeum vulgare subsp. vulgare] [SEQ ID 538]

[0419] P14323 (イネ) >gi|573918992|ref|XP_006647120.1| PREDICTED: glutelin type-B 2-like [Oryza brachyantha] MATTVFSRFSTYFCVLLLCHGSMAQLFNPSTNPWHNPRQGSSRECRFDRLQPFEPLRKVRSEAGVTEYFDEKNELFQCTGTFVIRRVIQPQGLLVPRYTNAPGLVYIIQGRGSIGLTFPGCPATYQQQFQQFLPQEQSQSQKFRDEHQKIHQFRQGDIVALPAGVAHWFYNDGDAPVVAVYVYDVKNSANQLEPRQREFLLGGNNMRAQQVYGSSAEQHSRQNIFSGFGVEILSEALGISTVTTKRLQSQNDQRGEIIHVKNGLQFLKPTLTQQQEQAQAQYQEVQYSEQQQTSSRWNGLDENFCTIKARMNIENTSRADTYNPRAGRTTSLNSQKFPILNLVQMSATRVNLYQNAILSTFWNVNAHSLVYTIQGRARVQVVSNFGKTVFDGELRPGQLLIIPQHYVVLKKAQREGFRYIAIKTNANAFVSQLVGKNSVFRSLPVDVIANVYRISREQARSLKNNRGEEHGAFAPRSQQQSYPGFSNQSESETSE[SEQ ID 539]

[0420] >gi|573919041|ref|XP_006647142.1| PREDICTED: glutelin type-B 4-like [Oryza brachyantha] MATTTFSRFSIYFCVLLLCHGSMAQLFSPTLNPWHSSRRGGSRDCRFDRLQAFEPLRRVRSEAGVTEYFDERNEQFQCTGTFVIRRVIEPQGLLVPRYTNTPGVVYIMQGRGSMGLTFPGCPATYQQQFQQFLPEGQSQSQKFRDEHQKIHQFRQGDIVALPAGVAHWFYNEGDTPVVALYVFDINNSANQLEPRQKDFLLAGNNNREQQVYGRSIEKHSGQNIFSGFNHELLSEALGISTLAAKRLQGQNDHRGEIIRVRNGLQLLKPTFTQQQEQAQSQYQVQYSEKQQESTRCNGLDENFCTINARLNIENPSRADTYNPRAGRITHLNNQKFPILNLVQMSATRVNLYQNAILSPYWNVNAHSLVYMVQGHARVQVVSNLGKTVFNSVLRPGQLLIIPQHYVVLKKAEREGCQYIAFKTNANSIVSQLAGKNSILRAMPVDVVANAYRISREQARDLKNNRGEELGAFTPKFEQQSYPGLSNESESEASE[SEQ ID 540]

[0421] >gi|109894635|gb|ABG47337.1| glutelin precursor [Zizania latifolia] MNMATINGPTIFFTVCLFLLCHGSLAQLLGQSTSQWQSSHRGSSRQCRFDRLQAFEPVRSVRSQAGTTEFFDASNELFQCAGVSIVRRIIEPRGLLLPQYTNGATIMYIIQGRGITGQTFPGCPES YQQFQQSMQAQLTGSQSQSQKFKDEHQKINRQGDVIALPAGVAHWCYNDGEVPVVAIYVIDINNAANQLDPRQRDFLAGNMRSPQAYRREVENQSQNIFSGFSAELLSEALGISTGVARQLQ CQNDQRGEIVRVEHGLSLLQPYASLQEQEQQQPRERYQVTQHQQSQYGGGCSNGLDETFCAMRIWQNIDNPNLADTYNPRAGRVTNLNSQKFPILNLIQMSAVKVNLYQNALLSPFWNINSHSV VYVTQGCARVQVVNNNGKTVFNGELRRGQLLIIPQHYVVVKKAQREGCAYIAFKTNPNSMVSHIVGKSSIFRALPTDVLANAYRISREDAQRLKHNRGDELGAFTPLQYKSYQDVSSVAASS[SEQ ID 541]

[0422] P29835 (イネ) >gi|226508602|ref|NP_001152635.1| globulin precursor [Zea mays] >gi|195658363|gb|ACG48649.1| globulin precursor [Zea mays] MAKIAAAAAAAAALCFALVAVCQGEVERQRLRDLQCWQEVQESPLDACRQVLDRQLTGGGVGGPFRWGTGLRMRCCQQLQDVSRECRCAAIRSMVRG YEEAMPPLEKGWWPWGRQQQPPPQGGGGGQGGYYYPCSRAGEGYQTQMYPPCRPGTTGPRIGRVRLTKAREYAAGLPMMCRLSEPQECSIFSGGDQY[SEQ ID 542]

[0423] >gi|242090997|ref|XP_002441331.1| hypothetical protein SORBIDRAFT_09g024570 [Sorghum bicolor] >gi|241946616|gb|EES19761.1| hypothetical protein SORBIDRAFT_09g024570 [Sorghum bicolor] MAKIAAVAATAALCLAALVAVAVGQGVVERQRLKDLQCWQEVQENPLGACRQVLDRQLTGGMRYGIGPFRWGTGLRMRCCQQLQDVSRECRCAAIRSMVRGYEETMPPLEKGWWGQQPQPGYDYPCSQAGEGYGYGESGQQQMYPPCRPGTGQKIARVKLTKARQYAAGMPMMCRLSEPQECSVFSGGDQYY[SEQ ID 543]

[0424] >gi|514748428|ref|XP_004961615.1| PREDICTED: 19 kDa globulin-like [Setaria italica] MAKFVVAAATAALCLAALVAMAAGQSGFERQRLRDLRCQREVEENPLWACRQVLDRQLTGGMRYGVGPFRWGTGLRMRCCQQLQDVSRECRCSAVRRMVRGYEEAMPPLEEGPYGYGGEQGEGYYGGGEGGEGYLPFPPRRIGRVRLTKARQYAAGLPMMCRLEPQECSVFSGDQYK[SEQ ID 544]

[0425] P0C1U8 (Bacterial) GLUC (Staphylococcus aureus) >gi|446599182|ref|WP_000676528.1| glutamyl endopeptidase [Staphylococcus aureus] >gi|253729369|gb|EES98098.1| trypsin [Staphylococcus aureus subsp. aureus TCH130] >gi|341844549|gb|EGS85761.1| glutamyl endopeptidase [Staphylococcus aureus subsp. aureus 21259] >gi|537390486|gb|AGU61109.1| Glutamyl endopeptidase precursor [Staphylococcus aureus subsp. aureus CN1] >gi|564714561|gb|ETD14665.1| glutamyl endopeptidase [Staphylococcus aureus subsp. aureus KPL1845] >gi|577466329|gb|EUG79766.1| glutamyl endopeptidase [Staphylococcus aureus M0139] >gi|580560623|gb|EVF84961.1| glutamyl endopeptidase [Staphylococcus aureus COAS6020] >gi|580687002|gb|EVH10169.1| glutamyl endopeptidase [Staphylococcus aureus UCIM6080] >gi|751815683|gb|KIN24957.1| glutamyl endopeptidase [Staphylococcus aureus MRSA_CVM43477] >gi|781884797|dbj|BAR08486.1| glutamyl endopeptidase precursor [Staphylococcus aureus subsp. aureus] >gi|781887762|dbj|BAR11210.1| glutamyl endopeptidase precursor [Staphylococcus aureus subsp.aureus]. MKGKFLKVSSLFVATLTTATLVSSSPAANALSSKAMDNHPQQSQSSKQQTPKIQKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDNDNSDNPDAA[SEQ ID 545]

Claims

1. A peptide of the amino acid sequence of SEQ ID NO:

283.

2. A skin growth-promoting variant of the peptide of claim 1, which has 1 to 4 amino acid changes compared to the peptide consisting of the amino acid sequence of SEQ ID NO:

283.

3. The skin growth-promoting variant of claim 2, which has 1 to 3 amino acid changes compared to a peptide consisting of the amino acid sequence of SEQ ID NO:

283.

4. The skin growth-promoting variant of claim 2, which has 1 to 2 amino acid changes compared to a peptide consisting of the amino acid sequence of SEQ ID NO:

283.

5. The skin growth-promoting variant of claim 2, which has one amino acid change compared to the peptide consisting of the amino acid sequence of SEQ ID NO:

283.

6. The skin growth-promoting mutant according to any one of claims 2 to 5, wherein the alteration is a deletion.

7. The skin growth-promoting variant according to any one of claims 2 to 5, wherein the alteration is at a terminal position.

8. A chemically modified peptide according to claim 1 or a variant according to any one of claims 2 to 7, wherein said peptide is skin growth promoting.

9. 9. The peptide or variant of claim 8, wherein the peptide or variant is chemically modified by modifications to the side chains, incorporation of protecting groups, incorporation of unnatural amino acids and / or their derivatives during peptide synthesis, and use of cross-linking agents and other methods that impose conformational constraints on the peptide.

10. A conjugate comprising a peptide according to claim 1, a variant according to any one of claims 2 to 7, or a peptide or variant according to claim 8 or 9, conjugated, linked or fused with a binding partner optionally selected from a polyethylene glycol polymer, a compound that increases molecular weight, a lipophilic group, or an antibody molecule.

11. The peptide or composition according to claim 1.

12. A composition comprising the peptide of claim 1.

13. 13. The composition of claim 11 or 12, wherein the composition is a powder.

14. 13. The composition of claim 11 or 12, wherein the composition is formulated for topical administration to human skin.

15. 15. The composition of claim 14 in the form of a cream, multiple emulsion, anhydrous composition, aqueous dispersion, oil, milk, balsam, foam, lotion, gel, cream gel, hydroalcoholic solution, hydroglycolic solution, beauty product, personal care product, hydrogel, liniment, serum, soap, dusting powder, paste, semi-solid formulation, serums, shampoo, conditioner, ointment, optional rinse-off formulation, talc, mousse, powder, spray, aerosol, solution, suspension, emulsion, syrup, elixir, polysaccharide film, patch, gel patch, bandage, adhesive system, water-in-oil emulsion, oil-in-water emulsion and silicone emulsion.

16. 11. A food or beverage, a dietary supplement, a personal care composition, or a pharmaceutical composition comprising a peptide according to claim 1, a variant according to any one of claims 2 to 7, a peptide or variant according to claim 8 or 9, or a conjugate according to claim 10.

17. 16. A non-therapeutic method for preventing or inhibiting ageing of human skin, comprising topically administering a peptide according to claim 1, a variant according to any one of claims 2 to 7, a peptide or variant according to claim 8 or 9, a conjugate according to claim 10, or a composition according to claim 14.

18. 15. A peptide according to claim 1, a variant according to any one of claims 2 to 7, a peptide or variant according to claim 8 or 9, a conjugate according to claim 10, or a composition according to claim 14 for use in the treatment of a mammalian wound, wherein the composition is applied topically to the mammalian wound.

Images