JP2005531539A - ペプチド組成物 - Google Patents
ペプチド組成物 Download PDFInfo
- Publication number
- JP2005531539A JP2005531539A JP2003587832A JP2003587832A JP2005531539A JP 2005531539 A JP2005531539 A JP 2005531539A JP 2003587832 A JP2003587832 A JP 2003587832A JP 2003587832 A JP2003587832 A JP 2003587832A JP 2005531539 A JP2005531539 A JP 2005531539A
- Authority
- JP
- Japan
- Prior art keywords
- peptide
- lys
- glu
- use according
- casein
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
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- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 119
- 239000000203 mixture Substances 0.000 title description 7
- 108050001786 Alpha-s2 casein Proteins 0.000 claims abstract description 59
- 239000002243 precursor Substances 0.000 claims abstract description 45
- 230000000694 effects Effects 0.000 claims abstract description 40
- 150000001413 amino acids Chemical class 0.000 claims abstract description 39
- 102000013370 fibrillin Human genes 0.000 claims abstract description 30
- 108060002895 fibrillin Proteins 0.000 claims abstract description 30
- 238000004519 manufacturing process Methods 0.000 claims abstract description 27
- 239000003814 drug Substances 0.000 claims abstract description 23
- 229940079593 drug Drugs 0.000 claims abstract description 22
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical group NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 claims abstract description 21
- 210000002950 fibroblast Anatomy 0.000 claims abstract description 20
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 claims abstract description 9
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 4
- 210000003491 skin Anatomy 0.000 claims description 24
- 230000032683 aging Effects 0.000 claims description 13
- 208000028169 periodontal disease Diseases 0.000 claims description 12
- 230000004936 stimulating effect Effects 0.000 claims description 12
- 108010035532 Collagen Proteins 0.000 claims description 8
- 102000008186 Collagen Human genes 0.000 claims description 8
- 229920001436 collagen Polymers 0.000 claims description 8
- 241000283690 Bos taurus Species 0.000 claims description 7
- 210000002510 keratinocyte Anatomy 0.000 claims description 7
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- 230000008439 repair process Effects 0.000 claims description 5
- 241000283973 Oryctolagus cuniculus Species 0.000 claims description 4
- 241001494479 Pecora Species 0.000 claims description 4
- 241000124008 Mammalia Species 0.000 claims 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 26
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- 229940024606 amino acid Drugs 0.000 description 23
- 108010046377 Whey Proteins Proteins 0.000 description 21
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- 239000005862 Whey Substances 0.000 description 20
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- 210000004080 milk Anatomy 0.000 description 12
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- 101000741059 Bos taurus Alpha-S2-casein Proteins 0.000 description 7
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- WZQZUVWEPMGIMM-JYJNAYRXSA-N Tyr-Gln-Lys Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CCCCN)C(=O)O)N)O WZQZUVWEPMGIMM-JYJNAYRXSA-N 0.000 description 7
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- 101800003838 Epidermal growth factor Proteins 0.000 description 6
- 101000993347 Gallus gallus Ciliary neurotrophic factor Proteins 0.000 description 6
- KWTVLKBOQATPHJ-SRVKXCTJSA-N Leu-Ala-Lys Chemical compound C[C@@H](C(=O)N[C@@H](CCCCN)C(=O)O)NC(=O)[C@H](CC(C)C)N KWTVLKBOQATPHJ-SRVKXCTJSA-N 0.000 description 6
- BWTKUQPNOMMKMA-FIRPJDEBSA-N Phe-Ile-Phe Chemical compound C([C@H](N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=CC=C1 BWTKUQPNOMMKMA-FIRPJDEBSA-N 0.000 description 6
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- 239000000047 product Substances 0.000 description 6
- 238000012360 testing method Methods 0.000 description 6
- MAGNEQBFSBREJL-DCAQKATOSA-N Gln-Glu-Lys Chemical compound C(CCN)C[C@@H](C(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)N)N MAGNEQBFSBREJL-DCAQKATOSA-N 0.000 description 5
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- LNYOXPDEIZJDEI-NHCYSSNCSA-N Val-Asn-Leu Chemical compound CC(C)C[C@@H](C(=O)O)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](C(C)C)N LNYOXPDEIZJDEI-NHCYSSNCSA-N 0.000 description 1
- HZYOWMGWKKRMBZ-BYULHYEWSA-N Val-Asp-Asp Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)O)N HZYOWMGWKKRMBZ-BYULHYEWSA-N 0.000 description 1
- UEHRGZCNLSWGHK-DLOVCJGASA-N Val-Glu-Val Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C(C)C)C(O)=O UEHRGZCNLSWGHK-DLOVCJGASA-N 0.000 description 1
- SDSCOOZQQGUQFC-GVXVVHGQSA-N Val-His-Gln Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)N[C@@H](CCC(=O)N)C(=O)O)N SDSCOOZQQGUQFC-GVXVVHGQSA-N 0.000 description 1
- BZMIYHIJVVJPCK-QSFUFRPTSA-N Val-Ile-Asn Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)O)NC(=O)[C@H](C(C)C)N BZMIYHIJVVJPCK-QSFUFRPTSA-N 0.000 description 1
- WNZSAUMKZQXHNC-UKJIMTQDSA-N Val-Ile-Gln Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCC(=O)N)C(=O)O)NC(=O)[C@H](C(C)C)N WNZSAUMKZQXHNC-UKJIMTQDSA-N 0.000 description 1
- JZWZACGUZVCQPS-RNJOBUHISA-N Val-Ile-Pro Chemical compound CC[C@H](C)[C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@H](C(C)C)N JZWZACGUZVCQPS-RNJOBUHISA-N 0.000 description 1
- GVJUTBOZZBTBIG-AVGNSLFASA-N Val-Lys-Arg Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)N GVJUTBOZZBTBIG-AVGNSLFASA-N 0.000 description 1
- VPGCVZRRBYOGCD-AVGNSLFASA-N Val-Lys-Val Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(O)=O VPGCVZRRBYOGCD-AVGNSLFASA-N 0.000 description 1
- SVFRYKBZHUGKLP-QXEWZRGKSA-N Val-Met-Asn Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(=O)N)C(=O)O)N SVFRYKBZHUGKLP-QXEWZRGKSA-N 0.000 description 1
- OJOMXGVLFKYDKP-QXEWZRGKSA-N Val-Met-Asp Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(=O)O)C(=O)O)N OJOMXGVLFKYDKP-QXEWZRGKSA-N 0.000 description 1
- MIKHIIQMRFYVOR-RCWTZXSCSA-N Val-Pro-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](C(C)C)N)O MIKHIIQMRFYVOR-RCWTZXSCSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000003679 aging effect Effects 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 230000002009 allergenic effect Effects 0.000 description 1
- 230000037005 anaesthesia Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 235000020244 animal milk Nutrition 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 238000003491 array Methods 0.000 description 1
- 108010093581 aspartyl-proline Proteins 0.000 description 1
- 108010038633 aspartylglutamate Proteins 0.000 description 1
- 230000001680 brushing effect Effects 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 125000002057 carboxymethyl group Chemical group [H]OC(=O)C([H])([H])[*] 0.000 description 1
- 229940021722 caseins Drugs 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 229940112822 chewing gum Drugs 0.000 description 1
- 238000011210 chromatographic step Methods 0.000 description 1
- 108010031561 colostrum growth factor Proteins 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 235000013365 dairy product Nutrition 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 210000004207 dermis Anatomy 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 1
- 229920002549 elastin Polymers 0.000 description 1
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- 238000011156 evaluation Methods 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
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- 239000001963 growth medium Substances 0.000 description 1
- 230000036541 health Effects 0.000 description 1
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- 235000020256 human milk Nutrition 0.000 description 1
- 230000036571 hydration Effects 0.000 description 1
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- 229960002591 hydroxyproline Drugs 0.000 description 1
- 230000003810 hyperpigmentation Effects 0.000 description 1
- 208000000069 hyperpigmentation Diseases 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
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- 230000003993 interaction Effects 0.000 description 1
- 108010044374 isoleucyl-tyrosine Proteins 0.000 description 1
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- 229960004194 lidocaine Drugs 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000006210 lotion Substances 0.000 description 1
- 108010044348 lysyl-glutamyl-aspartic acid Proteins 0.000 description 1
- 108010045397 lysyl-tyrosyl-lysine Proteins 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
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- 238000013160 medical therapy Methods 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
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- 235000021239 milk protein Nutrition 0.000 description 1
- 230000001333 moisturizer Effects 0.000 description 1
- 239000005445 natural material Substances 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 229920002113 octoxynol Polymers 0.000 description 1
- 229920002866 paraformaldehyde Polymers 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 102000013415 peroxidase activity proteins Human genes 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- NTGBUUXKGAZMSE-UHFFFAOYSA-N phenyl n-[4-[4-(4-methoxyphenyl)piperazin-1-yl]phenyl]carbamate Chemical compound C1=CC(OC)=CC=C1N1CCN(C=2C=CC(NC(=O)OC=3C=CC=CC=3)=CC=2)CC1 NTGBUUXKGAZMSE-UHFFFAOYSA-N 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
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- 238000011321 prophylaxis Methods 0.000 description 1
- 239000003531 protein hydrolysate Substances 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 238000007388 punch biopsy Methods 0.000 description 1
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- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
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- 230000028327 secretion Effects 0.000 description 1
- 108010071207 serylmethionine Proteins 0.000 description 1
- 235000020183 skimmed milk Nutrition 0.000 description 1
- 210000001626 skin fibroblast Anatomy 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000008399 tap water Substances 0.000 description 1
- 235000020679 tap water Nutrition 0.000 description 1
- HWCKGOZZJDHMNC-UHFFFAOYSA-M tetraethylammonium bromide Chemical compound [Br-].CC[N+](CC)(CC)CC HWCKGOZZJDHMNC-UHFFFAOYSA-M 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 229940034610 toothpaste Drugs 0.000 description 1
- 239000003860 topical agent Substances 0.000 description 1
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 1
- 229960001727 tretinoin Drugs 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 108010084932 tryptophyl-proline Proteins 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 108010051110 tyrosyl-lysine Proteins 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
- 235000019155 vitamin A Nutrition 0.000 description 1
- 239000011719 vitamin A Substances 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
- 235000021119 whey protein Nutrition 0.000 description 1
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Classifications
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q11/00—Preparations for care of the teeth, of the oral cavity or of dentures; Dentifrices, e.g. toothpastes; Mouth rinses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- A61K38/1709—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/02—Stomatological preparations, e.g. drugs for caries, aphtae, periodontitis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/16—Emollients or protectives, e.g. against radiation
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
- A61Q19/08—Anti-ageing preparations
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
- A61K2800/70—Biological properties of the composition as a whole
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- General Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Chemical & Material Sciences (AREA)
- Medicinal Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Epidemiology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Dermatology (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Marine Sciences & Fisheries (AREA)
- Oral & Maxillofacial Surgery (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Birds (AREA)
- Toxicology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
Description
[CAS2_BOVIN] α−S2カゼイン前駆物質
配列:
MKFFIFTCLL AVALAKNTME HVSSSEESII SQETYKQEKN MAINPSKENL CSTFCKEVVR
NANEEEYSIG SSSEESAEVA TEEVKITVDD KHYQKALNEI NQFYQKFPQY LQYLYQGPIV
LNPWDQVKRN AVPITPTLNR EQLSTSEENS KKTVDMESTE VFTKKTKLTE EEKNRLNFLK
KISQRYQKFA LPQYLKTVYQ HQKAMKPWIQ PKTKVIPYVR YL
Met Lys Phe Phe Ile Phe Thr Cys Leu Leu
Ala Val Ala Leu Ala Lys Asn Thr Met Glu
His Val Ser Ser Ser Glu Glu Ser Ile Ile
Ser Gln Glu Thr Tyr Lys Gln Glu Lys Asn
Met Ala Ile Asn Pro Ser Lys Glu Asn Leu
Cys Ser Thr Phe Cys Lys Glu Val Val Arg
Asn Ala Asn Glu Glu Glu Tyr Ser Ile Gly
Ser Ser Ser Glu Glu Ser Ala Glu Val Ala
Thr Glu Glu Val Lys Ile Thr Val Asp Asp
Lys His Tyr Gln Lys Ala Leu Asn Glu Ile
Asn Gln Phe Tyr Gln Lys Phe Pro Gln Tyr
Leu Gln Tyr Leu Tyr Gln Gly Pro Ile Val
Leu Asn Pro Trp Asp Gln Val Lys Arg Asn
Ala Val Pro Ile Thr Pro Thr Leu Asn Arg
Glu Gln Leu Ser Thr Ser Glu Glu Asn Ser
Lys Lys Thr Val Asp Met Glu Ser Thr Glu
Val Phe Thr Lys Lys Thr Lys Leu Thr Glu
Glu Glu Lys Asn Arg Leu Asn Phe Leu Lys
Lys Ile Ser Gln Arg Tyr Gln Lys Phe Ala
Leu Pro Gln Tyr Leu Lys Thr Val Tyr Gln
His Gln Lys Ala Met Lys Pro Trp Ile Gln
Pro Lys Thr Lys Val Ile Pro Tyr Val Arg
Tyr Leu
となる。
LysValIleProTyrValArgTyrLeu;
ThrLysValIleProTyrValArgTyrLeu;
LysThrLysValIleProTyrValArgTyrLeu;
ProLysThrLysValIleProTyrValArgTyrLeu;
GlnProLysThrLysValIleProTyrValArgTyrLeu;
AlaMetLysProTrpIleGlnProLysThrLysValIleProTyrValArgTyrLeu;
ThrValTyrGlnHisGlnLysAlaMetLysProTrpIleGlnProLysThrLysValIleProTyrValArgTyrLeu;および
ProGlnTyrLeuLysThrValTyrGlnHisGlnLysAlaMetLysProTrpIleGlnProLysThrLysValIleProTyrValArgTyrLeu
から選択されるアミノ酸配列を含むことが好ましい。
LysValIleProTyr;
ThrLysValIleProTyr;
LysThrLysValIleProTyr;
ProLysThrLysValIleProTyr;
GlnProLysThrLysValIleProTyr;
AlaMetLysProTrpIleGlnProLysThrLysValIleProTyr;
ThrValTyrGlnHisGlnLysAlaMetLysProTrpIleGlnProLysThrLysValIleProTyr;
ProGlnTyrLeuLysThrValTyrGlnHisGlnLysAlaMetLysProTrpIleGlnProLysThrLysValIleProTyr.
もまた好ましい。
[CAS2 CAPH1] α−S2カゼイン前駆物質(α−S2−CN)
配列:
MKFFIFTCLL AVALAKHKME HVSSSEEPIN IFQEIYKQEK NMAIHPRKEK LCTTSCEEVV
RNANEEEYSI RSSSEESAEV APEEIKITVD DKHYQKALNE INQFYQKFPQ YLQYPYQGPI
VLNPWDQVKR NAGPFTPTVN REQLSTSEEN SKKTIDMEST EVFTKKTKLT EEEKNRLNFL
KKISQYYQKF AWPQYLKTVD QHQKAMKPWT QPKTNAIPYV RYL 223
>pir|S33881|S33881 α−S2カゼインE−ヤギ
配列:
MKFFIFTCLL AVALAKHKME HVSSSEEPIN IFQEIYKQEK NMAIHPRKEK LCTTSCEEVV
RNANEEEYSI RSSSEESAKV APEEIKITVD DKHYQKALNE INQFYQKFPQ YLQYPYQGPI
VLNPWDQVKR NAGPFTPTVN REQLSTSEEN SKKTIDMEST EVFTKKTKLT EEEKNRLNFL
KKISQYYQKF AWPQYLKTVD QHQKAMKPWT QPKTNAIPYV RYL 223
>gp|S74171|S74171_1 α−S2カゼインC−ヤギ属腋毛
配列:
MKFFIFTCLL AVALAKHKME HVSSSEEPIN IFQEIYKQEK NMAIHPRKEK LCTTSCEEVV
RNANEEEYSI RSSSEESAEV APEEIKITVD DKHYQKALNE INQFYQKFPQ YLQYPYQGPI
VLNPWDQVKR NAGPFTPTVN REQLSTSEEN SKKTIDMEST EVFTKKTKLT EEEKNRLNFL
KIISQYYQKF AWPQYLKTVD QHQKAMKPWT QPKTNAIPYV RYL 223
>pir|S39776|S39776 α−S2カゼインb型前駆物質−ウサギ
>gp|X76909|OCPAS2BCS_1 プレ−α−S2bカゼイン(AA−15〜167)アナウサギ属疥癬トンネル
配列:
MKFFIFTCLL AVALAKPKIE QSSEETIAV SQEVSPNLEN ICSTACEEPI KNINEVEYVE
VPTEIKDQEF YQKVNLLQYL QALYQYPTVM DPWTRAETKA IPFIRTMQYK QEKDATKHTS
QKTELTEEEK AFLKYLDEMK QYYQKFVFPQ YLKNAHHFQK TMNPWNHVKT IIYQVPTSL 179
[CAS2_SHEEP] α−S2カゼイン前駆物質−ヒツジ
配列:
MKFFIFTCLL AVALAKHKME HVSSSEEPIN ISQEIYKQEK NMAIHPRKEK LCTTSCEEVV
RNADEEEYSI RSSSEESAEV APEEVKITVD DKHYQKALNE INQFYQKFPQ YLQYLYQGPI
VLNPWDQVKR NAGPFTPTVN REQLSTSEEN SKKTIDMEST EVFTKKTKLT EEEKNRLNFL
KKISQYYQKF AWPQYLKTVD QHQKAMKPWT QPKTNAIPYV RYL 223
[CAS2_PIG] α−S2カゼイン前駆物質−ブタ
配列:
MKFFIFTCLL AVAFAKHEME HVSSSEESIN ISQEKYKQEK NVINHPSKED ICATSCEEAV
RNIKEVGYAS SSSSEESVDI PAENVKVTVE DKHYLKQLEK ISQFYQKFPQ YLQALYQAQI
VMNPWDQTKT SAYPFIPTVI QSGEELSTSE EPVSSSQEEN TKTVDESME EFTKKTELTE
EEKNRIKFLN KIKQYYQKFT WPQYIKTVHQ KQKAMKPWNH IKTNSYQIIP NLRYF 235
[CAS2 CAPH1] α−S2カゼイン前駆物質(α−S2−CN)
配列:
Met Lys Phe Ile Phe Phe Thr Cys Leu Leu
Ala Val Ala Leu Ala Lys His Lys Met Glu
His Val Ser Ser Ser Gly Gly Pro Ile Asn
Ile Phe Gln Glu Ile Tyr Lys Gln Glu Lys
Asn Met Ala Ile His Pro Arg Lys Glu Lys
Leu Cys Thr Thr Ser Cys Glu Glu Val Val
Arg Asn Ala Asn Glu Glu Glu Tyr Ser Ile
Arg Ser Ser Ser Glu Glu Ser Ala Glu Val
Ala Pro Glu Glu Ile Lys Ile Thr Val Asp
Asp Lys His Tyr Gln Lys Ala Leu Asn Glu
Ile Asn Gln Phe Tyr Gln Lys Phe Pro Gln
Tyr Leu Gln Tyr Pro Tyr Gln Gly Pro Ile
Val Leu Asn Pro Trp Asp Gln Val Lys Arg
Asn Ala Gly Pro Phe Thr Pro Thr Val Asn
Arg Glu Gln Leu Ser Thr Ser Glu Glu Asn
Ser Lys Lys Thr Ile Asp Met Glu Ser Thr
Glu Val Phe Thr Lys Lys Thr Lys Leu Thr
Glu Glu Glu Lys Asn Arg Leu Asn Phe Leu
Lys Lys Ile Ser Gln Tyr Tyr Gln Lys Phe
Ala Trp Pro Gln Tyr Leu Lys Thr Val Asp
Gln His Gln Lys Ala Met Lys Pro Trp Thr
Gln Pro Lys Thr Asn Ala Ile Pro Tyr Val
Arg Tyr Leu
>pir|S33881|S33881 α−S2カゼインE−ヤギ
配列:
Met Lys Phe Phe Ile Phe Thr Cys Leu Leu
Ala Val Ala Leu Ala Lys His Lys Met Glu
His Val Ser Ser Ser Glu Glu Pro Ile Asn
Ile Phe Gln Glu Ile Tyr Lys Gln Glu Lys
Asn Met Ala Ile His Pro Arg Lys Glu Lys
Leu Cys Thr Thr Ser Cys Glu Glu Val Val
Arg Asn Ala Asn Glu Glu Glu Tyr Ser Ile
Arg Ser Ser Ser Glu Glu Ser Ala Lys Val
Ala Pro Glu Glu Ile Lys Ile Thr Val Asp
Asp Lys His Tyr Gln Lys Ala Leu Asn Glu
Ile Asn Gln Phe Tyr Gln Lys Phe Pro Gln
Tyr Leu Gln Tyr Pro Tyr Gln Gly Pro Ile
Val Leu Asn Pro Trp Asp Gln Val Lys Arg
Asn Ala Gly Pro Phe Thr Pro Thr Val Asn
Arg Glu Gln Leu Ser Thr Ser Glu Glu Asn
Ser Lys Lys Thr Ile Asp Met Glu Ser Thr
Glu Val Phe Thr Lys Lys Thr Lys Leu Thr
Glu Glu Glu Lys Asn Arg Leu Asn Phe Leu
Lys Lys Ile Ser Gln Tyr Tyr Gln Lys Phe
Ala Trp Pro Gln Tyr Leu Lys Thr Val Asp
Gln His Gln Lys Ala Met Lys Pro Trp Thr
Gln Pro Lys Thr Asn Ala Ile Pro Tyr Val
Arg Tyr Leu
>gp|S74171|S74171_1 α−S2カゼインC−ヤギ属腋毛
配列:
Met Lys Phe Phe Ile Phe Thr Cys Leu Leu
Ala Val Ala Leu Ala Lys His Lys Met Glu
His Val Ser Ser Ser Glu Glu Pro Ile Asn
Ile Phe Gln Glu Ile Tyr Lys Gln Glu Lys
Asn Met Ala Ile His Pro Arg Lys Glu Lys
Leu Cys Thr Thr Ser Cys Glu Glu Val Val
Arg Asn Ala Asn Glu Glu Glu Tyr Ser Ile
Arg Ser Ser Ser Glu Glu Ser Ala Glu Val
Ala Pro Glu Glu Ile Lys Ile Thr Val Asp
Asp Lys His Tyr Gln Lys Ala Leu Asn Glu
Ile Asn Gln Phe Tyr Gln Lys Phe Pro Gln
Tyr Leu Gln Tyr Pro Tyr Gln Gly Pro Ile
Val Leu Asn Pro Trp Asp Gln Val Lys Arg
Asn Ala Gly Pro Phe Thr Pro Thr Val Asn
Arg Glu Gln Leu Ser Thr Ser Glu Glu Asn
Ser Lys Lys Thr Ile Asp Met Glu Ser Thr
Glu Val Phe Thr Lys Lys Thr Lys Leu Thr
Glu Glu Glu Lys Asn Arg Leu Asn Phe Leu
Lys Ile Ile Ser Gln Tyr Tyr Gln Lys Phe
Ala Trp Pro Gln Tyr Leu Lys Thr Val Asp
Gln His Gln Lys Ala Met Lys Pro Trp Thr
Gln Pro Lys Thr Asn Ala Ile Pro Tyr Val
Arg Tyr Leu
>pir|S39776|S39776 α−S2カゼインb型前駆物質−ウサギ
>gp|X76909|OCPAS2BCS_1 プレ−α−S2bカゼイン(AA−15〜167)アナウサギ属疥癬トンネル
配列:
Met Lys Phe Phe Ile Phe Thr Cys Leu Leu
Ala Val Ala Leu Ala Lys Pro Lys Ile Glu
Gln Ser Ser Ser Glu Glu Thr Ile Ala Val
Ser Gln Glu Val Ser Pro Asn Leu Glu Asn
Ile Cys Ser Thr Ala Cys Glu Glu Pro Ile
Lys Asn Ile Asn Glu Val Glu Tyr Val Glu
Val Pro Thr Glu Ile Lys Asp Gln Glu Phe
Tyr Gln Lys Val Asn Leu Leu Gln Tyr Leu
Gln Ala Leu Tyr Gln Tyr Pro Thr Val Met
Asp Pro Trp Thr Arg Ala Glu Thr Lys Ala
Ile Pro Phe Ile Arg Thr Met Gln Tyr Lys
Gln Glu Lys Asp Ala Thr Lys His Thr Ser
Gln Lys Thr Glu Leu Thr Glu Glu Glu Lys
Ala Phe Leu Lys Tyr Leu Asp Glu Met Lys
Gln Tyr Tyr Gln Lys Phe Val Phe Pro Gln
Tyr Leu Lys Asn Ala His His Phe Gln Lys
Thr Met Asn Pro Trp Asn His Val Lys Thr
Ile Ile Tyr Gln Ser Val Pro Thr Leu
[CAS2_SHEEP] α−S2カゼイン前駆物質−ヒツジ
配列:
Met Lys Phe Phe Ile Phe Thr Cys Leu Leu
Ala Val Ala Leu Ala Lys His Lys Met Glu
His Val Ser Ser Ser Glu Glu Pro Ile Asn
Ile Ser Gln Glu Ile Tyr Lys Gln Glu Lys
Asn Met Ala Ile His Pro Arg Lys Glu Lys
Leu Cys Thr Thr Ser Cys Glu Glu Val Val
Arg Asn Ala Asp Glu Glu Glu Tyr Ser Ile
Arg Ser Ser Ser Glu Glu Ser Ala Glu Val
Ala Pro Glu Glu Val Lys Ile Thr Val Asp
Asp Lys His Tyr Gln Lys Ala Leu Asn Glu
Ile Asn Gln Phe Tyr Gln Lys Phe Pro Gln
Tyr Leu Gln Tyr Leu Tyr Gln Gly Pro Ile
Val Leu Asn Pro Trp Asp Gln Val Lys Arg
Asn Ala Gly Pro Phe Thr Pro Thr Val Asn
Arg Glu Gln Leu Ser Thr Ser Glu Glu Asn
Ser Lys Lys Thr Ile Asp Met Glu Ser Thr
Glu Val Phe Thr Lys Lys Thr Lys Leu Thr
Glu Glu Glu Lys Asn Arg Leu Asn Phe Leu
Lys Lys Ile Ser Gln Tyr Tyr Gln Lys Phe
Ala Trp Pro Gln Tyr Leu Lys Thr Val Asp
Gln His Gln Lys Ala Met Lys Pro Trp Thr
Gln Pro Lys Thr Asn Ala Ile Pro Tyr Val
Arg Tyr Leu
[CAS2_PIG] α−S2カゼイン前駆物質−ブタ
配列:
Met Lys Phe Phe Ile Phe Thr Cys Leu Leu
Ala Val Ala Phe Ala Lys His Glu Met Glu
His Val Ser Ser Ser Glu Glu Ser Ile Asp
Ile Ser Gln Glu Lys Tyr Lys Gln Glu Lys
Asn Val Ile Asn His Pro Ser Lys Glu Asp
Ile Cys Ala Thr Ser Cys Glu Glu Ala Val
Arg Asn Ile Lys Glu Val Glu Tyr Ala Ser
Ser Ser Ser Ser Glu Glu Ser Val Asp Ile
Pro Ala Glu Asn Val Lys Val Thr Val Glu
Asp Lys His Tyr Leu Lys Gln Leu Glu Lys
Ile Ser Gln Phe Tyr Gln Lys Phe Pro Gln
Tyr Leu Gln Ala Leu Tyr Gln Ala Gln Ile
Val Met Asn Pro Trp Asp Gln Thr Lys Thr
Ser Ala Tyr Pro Phe Ile Pro Thr Val Ile
Gln Ser Gly Glu Glu Leu Ser Thr Ser Glu
Glu Pro Val Ser Ser Ser Gln Glu Glu Asn
Thr Lys Thr Val Asp Met Glu Ser Met Glu
Glu Phe Thr Lys Lys Thr Glu Leu Thr Glu
Glu Glu Lys Asn Arg Ile Lys Phe Leu Asn
Lys Ile Lys Gln Tyr Tyr Gln Lys Phe Thr
Trp Pro Gln Tyr Ile Lys Thr Val His Gln
Lys Gln Lys Ala Met Lys Pro Trp Asn His
Ile Lys Thr Asn Ser Tyr Gln Ile Ile Pro
Asn Leu Arg Tyr Phe
この手順は、チーズホエイから標準化天然製品(Standardised Natural Product)(SNP)の回収、製造および保存の方法に関するものである。通常、この手順は、SNPの小規模製造に、例えば研究および開発の目的に用いられる。しかしながら、その手順は、公知の技術に従って商業生産に望ましいようにスケールアップすることができる。
チーズホエイの回収および保存
約40リットルの新鮮な清澄化チーズホエイをDewLayチーズ製造工場(ガースタング、ランカシャー)から入手した。そのホエイは、清潔な容器内に回収され、直ちにPepsyn Central Manufacturing Facility(リバプール)に輸送された。
プラスチック製バッグに2リットルブロックのホエイを入れ、流れる熱水中にそれを浸漬することによって、凍結したホエイを解凍した。解凍は10分未満で終了し、融解したホエイの温度を10℃未満に維持した。
濃HClを用いて、ホエイのpHを3.0に調整した。ホエイ1リットルにつき、攪拌しながら、(NH4)2S04(BDH,AnalaRグレード)220gを攪拌しながら30分間かけてゆっくりと添加した。攪拌せず、さらに1時間30分平衡化し、次いで、操作温度4〜10℃に予め平衡化させておいた、SorvallRC−SB遠心機およびそれに付随するGS−3ローター(DuPont Instruments社)を使用して、9000rpmで40分間遠心した。回収した上清1リットルごとに、(NH4)2S04130gを添加し、平衡化させ、上述のように遠心した。上清を廃棄し、ペレットを蒸留水に再溶解した(最初のホエイ1リットルごとに400ml)。流れる水道水に対して、分画分子量(MWCO)12,000〜14,000ダルトンの透析チューブ(Medicell Int.Ltd,英国)を用いて、これを一晩透析し、次いで、緩衝液を1回装入して、pH6.0の20mMリン酸ナトリウム緩衝液で7時間透析した。透析されたソルトカット(salt-cut)を回収し、翌日に加工するために冷蔵するか、または必要となるまで凍結した(−20℃)。
透析されたチーズホエイ・ソルトカット(cheese whey salt cut)を、20mMリン酸ナトリウム緩衝液(pH6.0)の移動相を有する陽イオン交換クロマトグラフィーに4℃でかけた。グラディエントミキサー(Pharmacia gradient mixer GM−1)によって提供される100〜700mM NaClの直線塩勾配を用いて、タンパク質を溶出した。UVモニター(Uvicord S II,Pharmacia社)を使用して280nmで作業の進行状況をモニターした。
陽イオン交換クロマトグラフィーからの活性画分を疎水性相互作用クロマトグラフィー(HIC)にかけた。20mMリン酸ナトリウム緩衝液(pH6.5)の移動相を用いて、これを室温で行った。グラディエントミキサー(Pharmacia gradient mixer GM−1)によって提供される4〜0M NaClの直線塩勾配を用いて、タンパク質を溶出した。UVモニター(Uvicord S II,Pharmacia社)を使用して280nmで作業の進行状況をモニターした。
この実施例によって、本発明で用いられるペプチドが、in vivoでフィブリリンの交換を刺激し、光老化した皮膚の修復を助けることが示されている。したがって、このペプチドは臨床的有効性を有する。
健康ではあるが、光老化したボランティア10名を募集した(男性:7名;女性:3名;年齢範囲37〜77歳)。直径6mmの標準フィンチャンバーの下で、前腕の伸筋側に、試験物質を別々に適用した:これらはカゼインペプチド(SNP36μg/水1ml)および閉塞(occluded)基準対照であった。4日間処置した後、フィンチャンバーを除去し、リグノカイン麻酔1体積%下にて、各試験部位から、3mmパンチバイオプシーを採取した。各バイオプシーを液体窒素中で急速凍結させ、組織学的評価のために処理した。バイオプシー部位を1×4/oエチロンで縫合し、縫合を除去するために、7日後に戻ってくるように対象に指示した。
凍結切片を厚さ10μmに作製した(OTFクリオスタット、Bright Instruments Ltd.)。患者1名当たり、1部分につき3つの切片を以下のように処理し、光学顕微鏡によってフィブリリン豊富なミクロフィブリル網状構造を同定した。
Rama27ラット乳細胞をコンフルエンスに成長させ、それらのコラーゲン合成の速度をM.J.Warburton,S.A.Ferns,およびP.S.Rudland,Experimental Cell Research,137,373−380(1982)の方法を用いて測定した。ヒドロキシプロリンへの[3H]プロリンの取り込みによって推定されるコラーゲン合成速度は、以下の表2に示す。
ケラチノサイト成長培地(TCS Cellworks Ltd.)において、ヒトケラチノサイト(HatKat)を20%コンフルエンスになるまで成長させた。次いで、同じ培地中で、ケラチノサイトを0.5%ウシ胎児血清(FCS)と共に3日間成長させた。その時点で、細胞をコールター(登録商標)カウンターで計数した。得られた細胞数を以下の表3に示す。
Claims (20)
- フィブリリンを産生するように線維芽細胞を刺激するのに有効な薬物の製造におけるペプチド、またはペプチドの誘導体の使用であって、そのペプチドが、α−S2カゼイン前駆物質中に存在するアミノ酸配列を含み、前記配列が3個以上のアミノ酸を含み、全長α−S2カゼイン前駆物質のN末端アミノ酸をそのN末端に含まないことを特徴とする使用。
- フィブリリンを産生するように線維芽細胞を刺激するのに有効な薬物の製造におけるペプチド、またはペプチドの誘導体の使用であって、そのペプチドがα−S2カゼイン断片活性を有することを特徴とする使用。
- 前記薬物が、歯周病を緩和または予防するのに有効である請求項1または2に記載の使用。
- 前記薬物が、皮膚における老化の影響を緩和または防止するのに有効である請求項1または2に記載の使用。
- 前記ペプチドが、9個以上のアミノ酸を含む請求項1から4のいずれかに記載の使用。
- 前記ペプチドが、9〜31個のアミノ酸を含む請求項1から5のいずれかに記載の使用。
- 前記ペプチドが、全長α−S2カゼイン前駆物質のC末端を含む請求項1から6のいずれかに記載の使用。
- 前記ペプチドが、ウシ、ヤギ、ヒツジ、ウサギまたはブタのα−S2カゼイン由来のペプチドであるか、または合成されたその等価物または相同体である請求項1から7のいずれかに記載の使用。
- 前記ペプチドが、以下の配列:
LysValIleProTyrValArgTyrLeu;
ThrLysValIleProTyrValArgTyrLeu;
LysThrLysValIleProTyrValArgTyrLeu;
ProLysThrLysValIleProTyrValArgTyrLeu
GlnProLysThrLysValIleProTyrValArgTyrLeu
AlaMetLysProTrpIleGlnProLysThrLysValIleProTyrValArgTyrLeu;
ThrValTyrGlnHisGlnLysAlaMetLysProTrpIleGlnProLysThrLysValIleProTyrValArgTyrLeu;および
ProGlnTyrLeuLysThrValTyrGlnHisGlnLysAlaMetLysProTrpIleGlnProLysThrLysValIleProTyrValArgTyrLeu
から選択されるアミノ酸配列を含む、請求項1から8のいずれかに記載の使用。 - 前記ペプチドが、以下の配列:
LysValIleProTyr;
ThrLysValIleProTyr;
LysThrLysValIleProTyr;
ProLysThrLysValIleProTyr;
GlnProLysThrLysValIleProTyr;
AlaMetLysProTrpIleGlnProLysThrLysValIleProTyr;
ThrValTyrGlnHisGlnLysAlaMetLysProTrpIleGlnProLysThrLysValIleProTyr;および
ProGlnTyrLeuLysThrValTyrGlnHisGlnLysAlaMetLysProTrpIleGlnProLysThrLysValIleProTyr
から選択されるアミノ酸配列を含む請求項1から9のいずれかに記載の使用。 - 前記ペプチドが:
(a)そのアミノ酸Leu、IleおよびValのうちの1つまたは複数が互いに置換され;および/または
(b)そのアミノ酸TyrおよびPheのうちの1つまたは複数が互いに置換され;および/または
(c)そのアミノ酸ArgおよびLysのうちの1つまたは複数が互いに置換された;
ペプチド相同体を含む、請求項1から10のいずれかに記載の使用。 - 老化の前記影響が、皮膚の皺ができることである請求項4から11のいずれかに記載の使用。
- 前記ペプチドが、線維芽細胞の成長を刺激することができる請求項1から12のいずれかに記載の使用。
- 前記ペプチドが、コラーゲンを産生するように線維芽細胞を刺激することができる請求項1から13のいずれかに記載の使用。
- 前記ペプチドが、ケラチノサイトの成長を刺激することができる請求項1から14のいずれかに記載の使用。
- 哺乳動物の皮膚の基底膜域を修復および/または維持するのに有効な薬物の製造におけるペプチド、またはペプチドの誘導体の使用であって、そのペプチドが、α−S2カゼイン前駆物質中に存在するアミノ酸配列を含み、前記配列が3個以上のアミノ酸を含み、全長α−S2カゼイン前駆物質のN末端アミノ酸をそのN末端に含まないことを特徴とする使用。
- 哺乳動物の皮膚の基底膜域を修復および/または維持するのに有効な薬物の製造におけるペプチド、またはペプチドの誘導体の使用であって、そのペプチドがα−S2カゼイン断片活性を有することを特徴とする使用。
- 前記薬物が、歯周病を緩和または予防するのに有効である請求項16または17に記載の使用。
- 前記薬物が、皮膚における老化の影響を緩和または防止するのに有効である請求項16または17に記載の使用。
- 前記哺乳動物がヒトである請求項16から19のいずれかに記載の使用。
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
GBGB0209384.7A GB0209384D0 (en) | 2002-04-24 | 2002-04-24 | Peptide composition |
PCT/GB2003/001439 WO2003091274A2 (en) | 2002-04-24 | 2003-04-02 | Use of alpha-s2 casein precursor-derived peptided |
Publications (1)
Publication Number | Publication Date |
---|---|
JP2005531539A true JP2005531539A (ja) | 2005-10-20 |
Family
ID=9935427
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2003587832A Pending JP2005531539A (ja) | 2002-04-24 | 2003-04-02 | ペプチド組成物 |
Country Status (8)
Country | Link |
---|---|
US (2) | US20060019884A1 (ja) |
EP (1) | EP1501538B1 (ja) |
JP (1) | JP2005531539A (ja) |
AT (1) | ATE446766T1 (ja) |
AU (1) | AU2003222959A1 (ja) |
DE (1) | DE60329838D1 (ja) |
GB (1) | GB0209384D0 (ja) |
WO (1) | WO2003091274A2 (ja) |
Families Citing this family (2)
Publication number | Priority date | Publication date | Assignee | Title |
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GB0209384D0 (en) | 2002-04-24 | 2002-06-05 | Pepsyn Ltd | Peptide composition |
JP5653759B2 (ja) * | 2008-12-15 | 2015-01-14 | カルピス株式会社 | 皮膚老化抑制ペプチド |
Family Cites Families (19)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US3558770A (en) | 1967-09-01 | 1971-01-26 | Kraftco Corp | Wound treating composition employing an enzyme modified casein |
US5086164A (en) | 1989-01-10 | 1992-02-04 | Repligen Corporation | Novel methods and compositions for treatment of angiogenic diseases |
JPH03255095A (ja) | 1990-03-02 | 1991-11-13 | Kanebo Ltd | カゼインペプチド |
EP0457565B1 (en) | 1990-05-18 | 1997-07-30 | Morinaga Milk Industry Co., Ltd. | Milk-protein hydrolyzates and compositions for use as hair and skin treating agent |
DE69133442T2 (de) | 1990-07-13 | 2006-01-12 | Gropep Ltd., Thebarton | Wachstumsfördernder wirkstoff |
AUPN271295A0 (en) | 1995-05-02 | 1995-05-25 | Gropep Pty Ltd | Method of treatment |
FR2673374A1 (fr) | 1991-03-01 | 1992-09-04 | Oreal | Composition cosmetique contenant comme ingredient actif un peptide a activite opiouide. |
CH684773A5 (fr) * | 1992-12-28 | 1994-12-30 | Nestle Sa | Composition alimentaire anti-cariogène. |
JPH06211689A (ja) | 1993-01-19 | 1994-08-02 | Kanebo Ltd | 鎮静剤及び精神安定用食品 |
US5965536A (en) | 1993-12-15 | 1999-10-12 | Board Of Regents, The University Of Texas System | Methods of inhibiting CXC intercrine molecules |
AUPM534794A0 (en) | 1994-04-28 | 1994-05-19 | Gropep Pty Ltd | Modified milk growth factor |
US5948763A (en) * | 1995-06-07 | 1999-09-07 | New York University | Peptides and pharmaceutical compositions thereof for treatment of disorders or diseases associated with abnormal protein folding into amyloid or amyloid-like deposits |
GB9522302D0 (en) * | 1995-10-31 | 1996-01-03 | Univ Liverpool | Growth promoters |
EP0983042B1 (en) | 1997-05-19 | 2004-12-08 | Colgate-Palmolive Company (a Delaware corporation) | Fluoride free dental remineralization |
JP3255095B2 (ja) | 1997-09-30 | 2002-02-12 | 日本電気株式会社 | 研磨液および研磨方法 |
AUPP494798A0 (en) | 1998-07-29 | 1998-08-20 | Pacific Biolink Pty Limited | Protective protein formulation |
CA2296311A1 (en) | 1999-01-28 | 2000-07-28 | Universite Laval | Enzymatic hydrolysate of milk proteins |
GB0016189D0 (en) * | 2000-06-30 | 2000-08-23 | Pepsyn Ltd | Cosmetic composition |
GB0209384D0 (en) | 2002-04-24 | 2002-06-05 | Pepsyn Ltd | Peptide composition |
-
2002
- 2002-04-24 GB GBGB0209384.7A patent/GB0209384D0/en not_active Ceased
-
2003
- 2003-04-02 EP EP03718925A patent/EP1501538B1/en not_active Expired - Lifetime
- 2003-04-02 US US10/512,512 patent/US20060019884A1/en not_active Abandoned
- 2003-04-02 WO PCT/GB2003/001439 patent/WO2003091274A2/en active Application Filing
- 2003-04-02 AT AT03718925T patent/ATE446766T1/de not_active IP Right Cessation
- 2003-04-02 JP JP2003587832A patent/JP2005531539A/ja active Pending
- 2003-04-02 AU AU2003222959A patent/AU2003222959A1/en not_active Abandoned
- 2003-04-02 DE DE60329838T patent/DE60329838D1/de not_active Expired - Lifetime
-
2006
- 2006-08-09 US US11/502,345 patent/US7786081B2/en not_active Expired - Fee Related
Also Published As
Publication number | Publication date |
---|---|
GB0209384D0 (en) | 2002-06-05 |
EP1501538A2 (en) | 2005-02-02 |
US7786081B2 (en) | 2010-08-31 |
EP1501538B1 (en) | 2009-10-28 |
US20070160558A1 (en) | 2007-07-12 |
AU2003222959A1 (en) | 2003-11-10 |
WO2003091274A2 (en) | 2003-11-06 |
US20060019884A1 (en) | 2006-01-26 |
WO2003091274A3 (en) | 2003-12-24 |
DE60329838D1 (de) | 2009-12-10 |
AU2003222959A8 (en) | 2003-11-10 |
ATE446766T1 (de) | 2009-11-15 |
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