CN109160945A - A kind of biologically active polypeptide DKLAQ and its preparation method and application - Google Patents
A kind of biologically active polypeptide DKLAQ and its preparation method and application Download PDFInfo
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- CN109160945A CN109160945A CN201811003878.5A CN201811003878A CN109160945A CN 109160945 A CN109160945 A CN 109160945A CN 201811003878 A CN201811003878 A CN 201811003878A CN 109160945 A CN109160945 A CN 109160945A
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- China
- Prior art keywords
- dklaq
- biologically active
- active polypeptide
- polypeptide
- derivative
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- AAZOYLQUEQRUMZ-GSSVUCPTSA-N Thr-Thr-Asn Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@H](C(O)=O)CC(N)=O AAZOYLQUEQRUMZ-GSSVUCPTSA-N 0.000 description 1
- MFMGPEKYBXFIRF-SUSMZKCASA-N Thr-Thr-Gln Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(N)=O)C(O)=O MFMGPEKYBXFIRF-SUSMZKCASA-N 0.000 description 1
- COYHRQWNJDJCNA-NUJDXYNKSA-N Thr-Thr-Thr Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O COYHRQWNJDJCNA-NUJDXYNKSA-N 0.000 description 1
- XVHAUVJXBFGUPC-RPTUDFQQSA-N Thr-Tyr-Phe Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O XVHAUVJXBFGUPC-RPTUDFQQSA-N 0.000 description 1
- KZTLZZQTJMCGIP-ZJDVBMNYSA-N Thr-Val-Thr Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)O)C(O)=O KZTLZZQTJMCGIP-ZJDVBMNYSA-N 0.000 description 1
- ATJFFYVFTNAWJD-UHFFFAOYSA-N Tin Chemical compound [Sn] ATJFFYVFTNAWJD-UHFFFAOYSA-N 0.000 description 1
- DANHCMVVXDXOHN-SRVKXCTJSA-N Tyr-Asp-Asn Chemical compound NC(=O)C[C@@H](C(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 DANHCMVVXDXOHN-SRVKXCTJSA-N 0.000 description 1
- 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 1
- WAPFQMXRSDEGOE-IHRRRGAJSA-N Tyr-Glu-Gln Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(N)=O)C(O)=O WAPFQMXRSDEGOE-IHRRRGAJSA-N 0.000 description 1
- WURLIFOWSMBUAR-SLFFLAALSA-N Tyr-Phe-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CC2=CC=CC=C2)NC(=O)[C@H](CC3=CC=C(C=C3)O)N)C(=O)O WURLIFOWSMBUAR-SLFFLAALSA-N 0.000 description 1
- VKYDVKAKGDNZED-STECZYCISA-N Tyr-Val-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC1=CC=C(C=C1)O)N VKYDVKAKGDNZED-STECZYCISA-N 0.000 description 1
- COSLEEOIYRPTHD-YDHLFZDLSA-N Val-Asp-Tyr Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 COSLEEOIYRPTHD-YDHLFZDLSA-N 0.000 description 1
- VLDMQVZZWDOKQF-AUTRQRHGSA-N Val-Glu-Gln Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)N)C(=O)O)N VLDMQVZZWDOKQF-AUTRQRHGSA-N 0.000 description 1
- AEMPCGRFEZTWIF-IHRRRGAJSA-N Val-Leu-Lys Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(O)=O AEMPCGRFEZTWIF-IHRRRGAJSA-N 0.000 description 1
- BTWMICVCQLKKNR-DCAQKATOSA-N Val-Leu-Ser Chemical compound CC(C)[C@H]([NH3+])C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C([O-])=O BTWMICVCQLKKNR-DCAQKATOSA-N 0.000 description 1
- USLVEJAHTBLSIL-CYDGBPFRSA-N Val-Pro-Ile Chemical compound CC[C@H](C)[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](N)C(C)C USLVEJAHTBLSIL-CYDGBPFRSA-N 0.000 description 1
- GUIYPEKUEMQBIK-JSGCOSHPSA-N Val-Tyr-Gly Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)NCC(O)=O GUIYPEKUEMQBIK-JSGCOSHPSA-N 0.000 description 1
- 229930003427 Vitamin E Natural products 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
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- 230000003679 aging effect Effects 0.000 description 1
- 108010044940 alanylglutamine Proteins 0.000 description 1
- 230000002605 anti-dotal effect Effects 0.000 description 1
- 108010084758 arginyl-tyrosyl-aspartic acid Proteins 0.000 description 1
- 210000001367 artery Anatomy 0.000 description 1
- 108010010430 asparagine-proline-alanine Proteins 0.000 description 1
- 108010077245 asparaginyl-proline Proteins 0.000 description 1
- 108010069205 aspartyl-phenylalanine Proteins 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 238000005842 biochemical reaction Methods 0.000 description 1
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- 239000004305 biphenyl Substances 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 235000019282 butylated hydroxyanisole Nutrition 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound 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 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000005352 clarification Methods 0.000 description 1
- 210000003022 colostrum Anatomy 0.000 description 1
- 235000021277 colostrum Nutrition 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 229910021641 deionized water Inorganic materials 0.000 description 1
- 230000001934 delay Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
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- 235000021245 dietary protein Nutrition 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
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- 108010054812 diprotin A Proteins 0.000 description 1
- 230000007071 enzymatic hydrolysis Effects 0.000 description 1
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- 238000000605 extraction Methods 0.000 description 1
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- 230000004151 fermentation Effects 0.000 description 1
- 125000002485 formyl group Chemical class [H]C(*)=O 0.000 description 1
- WIGCFUFOHFEKBI-UHFFFAOYSA-N gamma-tocopherol Natural products CC(C)CCCC(C)CCCC(C)CCCC1CCC2C(C)C(O)C(C)C(C)C2O1 WIGCFUFOHFEKBI-UHFFFAOYSA-N 0.000 description 1
- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- XBGGUPMXALFZOT-UHFFFAOYSA-N glycyl-L-tyrosine hemihydrate Natural products NCC(=O)NC(C(O)=O)CC1=CC=C(O)C=C1 XBGGUPMXALFZOT-UHFFFAOYSA-N 0.000 description 1
- 108010066198 glycyl-leucyl-phenylalanine Proteins 0.000 description 1
- 108010089804 glycyl-threonine Proteins 0.000 description 1
- 108010087823 glycyltyrosine Proteins 0.000 description 1
- 230000008642 heat stress Effects 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 229940088592 immunologic factor Drugs 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 210000002490 intestinal epithelial cell Anatomy 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- JEIPFZHSYJVQDO-UHFFFAOYSA-N iron(III) oxide Inorganic materials O=[Fe]O[Fe]=O JEIPFZHSYJVQDO-UHFFFAOYSA-N 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 108010044311 leucyl-glycyl-glycine Proteins 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 108010025153 lysyl-alanyl-alanine Proteins 0.000 description 1
- 108010043322 lysyl-tryptophyl-alpha-lysine Proteins 0.000 description 1
- 108010009298 lysylglutamic acid Proteins 0.000 description 1
- 108010064235 lysylglycine Proteins 0.000 description 1
- 108010054155 lysyllysine Proteins 0.000 description 1
- 108010017391 lysylvaline Proteins 0.000 description 1
- 230000003050 macronutrient Effects 0.000 description 1
- 235000021073 macronutrients Nutrition 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 238000001819 mass spectrum Methods 0.000 description 1
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- 230000002503 metabolic effect Effects 0.000 description 1
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- 230000000813 microbial effect Effects 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 230000004783 oxidative metabolism Effects 0.000 description 1
- 230000000737 periodic effect Effects 0.000 description 1
- 108010024607 phenylalanylalanine Proteins 0.000 description 1
- ZUOUZKKEUPVFJK-UHFFFAOYSA-N phenylbenzene Natural products C1=CC=CC=C1C1=CC=CC=C1 ZUOUZKKEUPVFJK-UHFFFAOYSA-N 0.000 description 1
- 230000000770 proinflammatory effect Effects 0.000 description 1
- 125000006239 protecting group Chemical group 0.000 description 1
- 239000003642 reactive oxygen metabolite Substances 0.000 description 1
- 230000001850 reproductive effect Effects 0.000 description 1
- 230000011506 response to oxidative stress Effects 0.000 description 1
- 201000003068 rheumatic fever Diseases 0.000 description 1
- 239000011435 rock Substances 0.000 description 1
- 238000005070 sampling Methods 0.000 description 1
- 230000002000 scavenging effect Effects 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 229910000077 silane Inorganic materials 0.000 description 1
- 230000037380 skin damage Effects 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
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- 108010078580 tyrosylleucine Proteins 0.000 description 1
- 238000002525 ultrasonication Methods 0.000 description 1
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- 235000019165 vitamin E Nutrition 0.000 description 1
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/335—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Lactobacillus (G)
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
-
- 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
- A61P39/00—General protective or antinoxious agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P39/00—General protective or antinoxious agents
- A61P39/06—Free radical scavengers or antioxidants
-
- 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
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Abstract
The present invention relates to albumen fields, and in particular to a kind of biologically active polypeptide DKLAQ and its preparation method and application, its amino acid sequence of biologically active polypeptide DKLAQ are Asp-Lys-Leu-Ala-Gln.By antioxidation in vitro experiment, internal Antisenility Experiment, demonstrating polypeptide DKLAQ has preferable antioxidation biology activity and activity of fighting against senium, on the one hand, biologically active polypeptide DKLAQ of the invention has preferable antioxidant activity, can the intracorporal free radical of removing machine, improve the quality of life；On the other hand, it can be improved the vigor of internal anti-peroxidation enzyme system, enhance body and resist the function of external source sexual stimulus, to reduce organism aging process, aging and sick probability, there is anti-oxidation function, the food of anti-senescence function, health care product and drug to have a very important significance exploitation.
Description
Technical field
The present invention relates to albumen fields, more particularly, to a kind of biologically active polypeptide DKLAQ and its preparation method and application.
Background technique
During cow's milk is through lactobacillus-fermented, a part of protein in cow's milk is metabolized by lactic acid bacteria to be utilized, concurrently
A series of biochemical reactions have been given birth to, so that protein is become polypeptide or free amino acid, is digested or passes through
The absorption and transport of intestinal epithelial cell is directly entered the blood circulation of human body.There is also the eggs of itself some synthesis for lactic acid bacteria thallus
White matter polypeptide fragment is utilized for bacterial growth.In these polypeptides, some is referred to as " raw with special physiological function
Object active peptide ".
It is particularly important that safe biologically active peptide is found in natural food source.In recent years, it has been found that some foods
The polypeptides matter in object source has good bioactivity, such as corn small peptide, soybean peptide, cow's milk polypeptide.These polypeptides can
To be obtained by number of ways such as microbial fermentation, digestion enzymatic hydrolysis, and biologically active polypeptide is by 2~20 mostly
Amino acid residue composition, molecular weight are less than 6000Da, contain a certain amount of hydrophobic amino acid, aromatic amino acid.
Oxidation reaction and oxidative metabolism be all for food and human body it is vital, free radical and active oxygen cause
A series of oxidation reaction.When excessive free radical is formed, they can be more than protective enzyme such as superoxide dismutase, peroxide
Change the protective effect of hydrogen enzyme, is generated so as to cause a series of side effect such as lipid oxidation, Apoptosis.This kind of oxidations is anti-
It answers, not only influences the shelf-life of the food containing rouge, certain harm is also caused to the health of human body, such as rheumatic arthritis, sugar
Urinate disease, artery sclerosis etc..In addition, the generation of Collins et al. 2005 research discovery cancers also has with the oxidative damage of DNA
It closes.
Artificial synthesized antioxidants some in early days such as butylated hydroxy anisole (BHA), 2,6- di-t-butyl -4- methylbenzene
Phenol (BHT) is applied in food, as the antioxidant of lipid, but these artificial synthesized additives have for human body it is latent
Risk.In the research process of natural, from the anti-oxidation peptide of food proteins become popular research it
One.It is not only highly-safe, is easier to be absorbed and used than macro-nutrients such as protein, such as calcium, iron can be promoted micro-
The absorption of nutrient is measured, also there is preferable antioxidant activity, have a extensive future.
Aging is a natural phenomena, and process is often accompanied by the variation of antioxidant levels, organ-tissue, immune factor,
Complicated variation, such as the trend that proinflammatory cytokine IL-6, IL-4, TNF-α presentation increase, IL-6 occur for middle cell factor
It is all considered to play an important role in the generating process of geriatric disease with TNF-a.With science of heredity and molecular biology
Development, the research of biological decay mechanism achieve gratifying progress.Researcher pass through utilize some model organisms, as mouse,
The term single gene mutating experiment of drosophila and caenorhabditis elegan etc. finds that some genes can dramatically increase service life of these organisms and reach
As many as 6 times.
Anti-aging peptide in terms of physiological function there is amino acid cannot compare excellent as a kind of emerging antidotal agent
Gesture can generate promotion or inhibiting effect to the intracorporal enzyme of biology, improve absorption and benefit to minerals and other nutrients
With removing interior free yl enhances the resistance to oxidation of body itself, to delay senescence.Therefore, the nutrition and health care of biologically active peptide
Effect has become the emphasis of domestic and foreign scholars' subject study.Qiu Juan et al. warp experimental studies have found that, milk-derived bioactive micro peptide
Life span of drosophila melanogaster can effectively be extended, delay its aging, and also there is preferable antioxidation, thus it is speculated that may be wherein rich in coloured glaze
Base peptides.SOD vigor in serum, reduces its lipid in discovery bovine colostrum extract energy conspicuousness raising the elderly's body such as the brightness in week
Peroxide and enhancing body resistance to oxidation, have certain anti-senescence function.
Have much about the research of biologically active polypeptide at present, for example Chinese patent CN105254738A discloses one kind and comes
Derived from the milk-derived biologically active polypeptide DELQDKIH of beta-casein, Chinese patent CN105254739A discloses one kind and derives from
Milk-derived the biologically active polypeptide GTQYTD, Chinese patent CN105254740A of α s1- casein disclose a kind of from α s2-
The milk-derived biologically active polypeptide NQFYQKF of casein.
Summary of the invention
The purpose of the present invention is to provide a kind of biologically active polypeptide DKLAQ and its preparation method and application.
The purpose of the present invention can be achieved through the following technical solutions:
First aspect present invention provides a kind of biologically active polypeptide DKLAQ, amino acid sequence Asp-Lys-Leu-
Ala-Gln, as shown in SEQ ID NO:1.
Preferably, the biologically active polypeptide derives from Lactobacillus helveticus mycoprotein.It is derive specifically from LBH_0445 |
m.412LBH_0445|g.412ORF LBH_0445|g.412LBH_0445|m.412type:5prime_partial len:
383 (+) LBH_0445:1-1149 (+) albumen, and the 311st~315, albumen amino acid residue thus.LBH_0445|
m.412LBH_0445|g.412ORF LBH_0445|g.412LBH_0445|m.412type:5prime_partial len:
383 (+) LBH_0445:1-1149 (+) protein amino acid sequences are as shown in SEQ ID NO:3.
LBH_0445|m.412LBH_0445|g.412ORF LBH_0445|g.412LBH_0445|m.412type:
The amino acid sequence and corresponding nucleotides sequence of 5prime_partial len:383 (+) LBH_0445:1-1149 (+) albumen
It is classified as existing technology, encodes the bioactivity of the nucleotide fragments energy encoding mature of this 311st~315 amino acids residue of albumen
Polypeptide DKLAQ.
Preferably, the biologically active polypeptide has anti-oxidation function and anti-senescence function.
Second aspect of the present invention provides the nucleotide fragments for encoding the biologically active polypeptide DKLAQ, sequence are as follows:
5 '-aca agc ttg ctc aag-3 ', as shown in SEQ ID NO:2.
Third aspect present invention provides the preparation method of the biologically active polypeptide DKLAQ, can pass through genetic engineering
Method it is artificial synthesized, can be directly obtained from Lactobacillus helveticus thallus by the method that clasmatosis isolates and purifies, Ke Yizhi
Connected chemical synthesis preparation.
Fourth aspect present invention, provide the biologically active polypeptide DKLAQ preparation have anti-oxidation function food,
Application in health care product, drug or cosmetics.
Fifth aspect present invention, provide the biologically active polypeptide DKLAQ preparation have anti-senescence function food,
Application in health care product or drug.
Sixth aspect present invention, provide the biologically active polypeptide DKLAQ preparation and meanwhile have anti-oxidation function with
Application in the food of anti-senescence function, health care product or drug.
Specifically, biologically active polypeptide DKLAQ of the invention, which can be used for preparing, reduces free radical to skin damage
Cosmetics, preparation have anti-oxidant and/or anti-aging drug；And since biologically active polypeptide DKLAQ of the invention passes through
Product after gastrointestinal tract degradation still has bioactivity, therefore can be also used for preparing the food such as Yoghourt, oxidation-resisting health-care
Product, and what is taken orally are used to prepare with anti-oxidant and/or anti-aging drug.
Seventh aspect present invention provides a kind of oxidation resistant product, including the biologically active polypeptide DKLAQ or the life
The derivative of object active peptides DKLAQ；The oxidation resistant product includes antioxidant food, antioxidant health-care product, antioxidant drug
Object or antioxidation cosmetic product；The derivative of the biologically active polypeptide DKLAQ, refers to the amino in biologically active polypeptide DKLAQ
On sour side-chain radical, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonylation, methylation, acetylation, phosphorylation, esterification
Or the modification such as glycosylation, obtained polypeptide derivative.
Eighth aspect present invention provides a kind of anti-aging product, including the biologically active polypeptide DKLAQ or the life
The derivative of object active peptides DKLAQ；The anti-aging product includes antisenility cistanche food, antisenescence health product or Kangshuaining mixture
Object；The derivative of the biologically active polypeptide DKLAQ, refers on the amino acid side groups of biologically active polypeptide DKLAQ, ammonia
Cardinal extremity or c-terminus carry out the modification such as hydroxylating, carboxylated, carbonylation, methylation, acetylation, phosphorylation, esterification or glycosylation,
Obtained polypeptide derivative.
Ninth aspect present invention provides product that is a kind of while having anti-oxidation function and anti-senescence function, including institute
State the derivative of biologically active polypeptide DKLAQ or the biologically active polypeptide DKLAQ；With anti-oxidation function and anti-senescence function
Product include food, health care product or drug；The derivative of the biologically active polypeptide DKLAQ, refers in biologically active polypeptide
On the amino acid side groups of DKLAQ, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonylation, methylation, acetylation,
The modification such as phosphorylation, esterification or glycosylation, obtained polypeptide derivative.
Biologically active polypeptide DKLAQ's of the present invention has the beneficial effect that biologically active polypeptide DKLAQ of the invention has preferably
Antioxidant activity and activity of fighting against senium；On the one hand, biologically active polypeptide DKLAQ of the invention has preferable anti-oxidant work
Property, can the intracorporal free radical of removing machine, improve the quality of life；On the other hand, it can be improved internal anti-peroxidation enzyme system
Vigor, enhancing body resists the function of external source sexual stimulus, to reduce organism aging process, aging and sick probability, has to exploitation
There are anti-oxidation function, the food of anti-senescence function, health care product and drug to have a very important significance.
Detailed description of the invention
Fig. 1: mass chromatography extracts figure (m/z=575.3201)；
Fig. 2: the second order ms figure for the segment that mass-to-charge ratio is 575.3201；
Fig. 3: polypeptide az, by crack conditions that mass-to-charge ratio is 575.3201；
Fig. 4: [DPPH] methanol standard curve；
Fig. 5: FeSO4Standard curve；
Fig. 6: the biologically active polypeptide DKLAQ influence to the caenorhabditis elegan service life；
Fig. 7: the biologically active polypeptide DKLAQ influence to caenorhabditis elegan under oxidative stress.
Specific embodiment
Before further describing specific embodiments of the present invention, it should be appreciated that protection scope of the present invention is not limited to down
State specific specific embodiment；It is also understood that term used in the embodiment of the present invention is specific specific in order to describe
Embodiment, rather than limiting the scope of protection of the present invention.
When embodiment provides numberical range, it should be appreciated that except non-present invention is otherwise noted, two ends of each numberical range
Any one numerical value can be selected between point and two endpoints.Unless otherwise defined, the present invention used in all technologies and
Scientific term is identical as the normally understood meaning of those skilled in the art of the present technique.Except specific method, equipment used in embodiment,
Outside material, grasp and record of the invention according to those skilled in the art to the prior art can also be used and this
Any method, equipment and the material of the similar or equivalent prior art of method described in inventive embodiments, equipment, material come real
The existing present invention.
Unless otherwise stated, disclosed in this invention experimental method, detection method, preparation method be all made of this technology neck
Molecular biology, biochemistry, chromatin Structure and the analysis of domain routine, analytical chemistry, cell culture, recombinant DNA technology and
The routine techniques of related fields.These technologies have perfect explanation in the prior art, and for details, reference can be made to Sambrook etc.
MOLECULAR CLONING:ALABORATORY MANUAL, Second edition, Cold Spring Harbor
Laboratory Press, 1989and Third edition, 2001；Ausubel etc., CURRENT PROTOCOLS IN
MOLECULAR BIOLOGY, John Wiley&Sons, New York, 1987and periodic updates；the
Series METHODS INENZYMOLOGY, Academic Press, San Diego；Wolffe, CHROMATIN
STRUCTUREAND FUNCTION, Third edition, Academic Press, San Diego, 1998；METHODSIN
ENZYMOLOGY, Vol.304, Chromatin (P.M.Wassarman and A.P.Wolffe, eds.), Academic
Press, San Diego, 1999；With METHODS IN MOLECULAR BIOLOGY, Vol.119, Chromatin
Protocols (P.B.Becker, ed.) Humana Press, Totowa, 1999 etc..
The present invention is described in detail with specific embodiment below in conjunction with the accompanying drawings.
1 active peptide DKLAQ's of embodiment is artificial synthesized
One, the synthesis of biologically active peptide
1. RINK resin 3g (degree of substitution 0.3mmol/g) is weighed in the reactor of 150ml, with the methylene chloride of 50ml
(DCM) it impregnates.
After 2.2 hours, resin is washed with nitrogen-dimethylformamide (DMF) of 3 times of resin volumes, is then drained, so weight
It is four times multiple, it is stand-by after resin is drained.
3. a certain amount of 20% piperidines (piperidines/DMF=1:4, v:v) is added into reactor, it is placed on decolorization swinging table and shakes
20min is shaken, the Fmoc blocking group on resin is sloughed with this.It is washed four times after having taken off protection with the DMF of 3 times of resin volumes,
Then it drains.
4. taking the detection of a small amount of resin ninhydrin (nine well ninhydrins) method (each two drop of inspection A, inspection B, 100 DEG C of reactions
1min), resin has color, illustrates to be deprotected successfully.
5. it weighs amino acid Asp in right amount and 1- hydroxyl-benzene a pair of horses going side by side triazole (HOBT) is in right amount in the centrifuge tube of 50ml, addition
The DMF of 20ml is dissolved, and the N of 3ml is then added, N diisopropylcarbodiimide (DIC) oscillation shakes up 1min, clear to solution
It is added in reactor after clear, then reactor is placed in 30 DEG C of shaking table and is reacted.
After 6.2 hours, with a certain amount of acetic anhydride end socket (acetic anhydride: DIEA:DCM=1:1:2, v:v:v) half an hour, so
It is washed four times, is drained stand-by with the DMF of 3 times of resin volumes afterwards.
7. a certain amount of 20% piperidines (piperidines/DMF=1:4, v:v) is added into reactor, it is placed on decolorization swinging table and shakes
20min is shaken, the Fmoc blocking group on resin is sloughed with this.It is washed four times after having taken off protection with DMF, is then drained.
8. taking the detection of a small amount of resin ninhydrin (nine well ninhydrins) method (each two drop of inspection A, inspection B, 100 DEG C of reactions
1min), resin has color, illustrates to be deprotected successfully.
9. weighing second amino acid next in right amount and HOBT being in right amount in the centrifuge tube of 50ml, the DMF general of 25ml is added
It is dissolved, and the DIC oscillation that 2.5ml is then added shakes up 1min, is added in reactor after solution clarification, then by reactor
It is placed in 30 DEG C of shaking table and reacts.
After 10.1 hours, a small amount of resin is taken to detect, with ninhydrin method detection (each two drop of inspection A, inspection B, 100 DEG C of reactions
1min), if resin be it is colourless, illustrate fully reacting；If resin has color, illustrate condensation not exclusively, the reaction was continued.
11. after complete reaction, being washed resin four times with DMF, then drains, a certain amount of 20% is added into reactor
Piperidines (piperidines/DMF=1:4, v:v), be placed on decolorization swinging table and rock 20min, sloughs the Fmoc protecting group on resin with this
Group.It is washed four times after having taken off protection with DMF, then drains whether detection protection sloughs.
12. successively connecting amino acid Lys, Leu, Ala and Gln according to step 9-11.
13. sloughing protection after connecting the last one amino acid, is washed four times with DMF, then taken out resin with methanol
It is dry.Then with 95 cutting liquids (trifluoroacetic acid: 1,2 dithioglycol: 3, isopropyl base silane: water=95:2:2:1, v:v:v) by polypeptide
It is cut down from resin (every gram of resin adds 10ml cutting liquid), and is centrifuged and is sunk with ice ether (cutting liquid: ether=1:9, v:v)
Drop four times.
So far, artificial synthesized biologically active peptide DKLAQ.
Two, the confirmation of biologically active peptide
1) UPLC is analyzed
UPLC condition is as follows:
Instrument: Waters ACQUITY UPLC ultra high efficiency liquid phase-electron spray-level four bars-time of-flight mass spectrometer
Chromatographic column specification: BEH C18 chromatographic column
Flow velocity: 0.4mL/min
Temperature: 50 DEG C
Ultraviolet detection wavelength: 210nm
Sample volume: 2 μ L
Gradient condition: A liquid: contain the water of 0.1% formic acid (v/v), B liquid: containing the acetonitrile of 0.1% formic acid (v/v)
2) mass spectral analysis
Mass Spectrometry Conditions are as follows:
Ionic means: ES+
Mass range (m/z): 100-1000
Capillary voltage (Capillary) (kV): 3.0
Sampling spiroid (V): 35.0
Ion source temperature (DEG C): 115
It goes solvent temperature (DEG C): 350
It goes solvent stream (L/hr): 700.0
Collision energy (eV): 4.0
Sweep time (sec): 0.25
Interior sweep time (sec): 0.02
According to the above analysis method, using ultra high efficiency liquid phase-electron spray-level four bars-flight time mass spectrum, to bioactivity
Peptide D KLAQ carries out chromatography and mass spectral analysis, and mass chromatography extraction figure is as shown in Figure 1, extract the second order ms figure at this peak
As shown in Figures 2 and 3 with az, by crack conditions, the polypeptide mass-to-charge ratio that can obtain this peak is 575.3201Da, and retention time is
37.8min。
3) result
From the figure 3, it may be seen that the case where being broken according to az, by, by Mascot software analytical calculation, obtains mass-to-charge ratio
The fragment sequence of 575.3201Da is Asp-Lys-Leu-Ala-Gln (DKLAQ), is denoted as SEQ ID NO:1.The segment and LBH_
0445|m.412LBH_0445|g.412ORF LBH_0445|g.412LBH_0445|m.412type:5prime_partial
The residue sequence that len:383 (+) LBH_0445:1-1149 (+) is the 311st~315, albumen is corresponding, and sequence is shown in SEQ ID NO:
3。
The antioxidant activity of 2 biologically active peptide of embodiment is tested
One, the antioxidation activity in vitro of [DPPH] method measurement biologically active peptide DKLAQ
1. experiment reagent and instrument:
Reagent: 1,1- diphenyl -2- trinitrophenyl-hydrazine (1,1-Diphenyl-2-picrylhydrazyl [DPPH]),
Japanese Wako company production；Methanol, Shanghai traditional Chinese medicines company provide；The biologically active polypeptide DKLAQ that embodiment 1 obtains.
Key instrument: Sunrise microplate reader, Austrian Tecan Products；96 porocyte culture plates, the U.S.
The manufacture of Millipore company；Assay balance, Meitelei-tolido Products.
2. experimental method:
(1) 1mmol/L [DPPH] methanol solution
It weighs 0.349mg [DPPH] with assay balance to be dissolved in 1mL methanol solution, the 1mmol/L prepared
[DPPH] methanol solution, tinfoil are kept in dark place, i.e., with i.e. use.
(2) measurement of [DPPH] methanol standard curve
100 μ L [DPPH] methanol standard curve samples are separately added by table 1 in 96 orifice plates, are stored at room temperature 90min, are used
Microplate reader detects light absorption value at 517nm.
Table 1 [DPPH] methanol calibration curve solution is prepared
According to experimental result, using Excel matched curve and regression equation is calculated, as a result sees Fig. 4 (regression equation: y=-
0.192x+0.2271, R2=0.9991).The linear relationship of [DPPH] methanol standard curve is good, related coefficient 0.999,
Show that [DPPH] methanol standard curve preci-sion and accuracy meets testing requirements.In terms of result, absorbance value with
[DPPH] content is in inverse relation, and [DPPH] content is fewer, and light absorption value is higher, i.e., the ability that sample removes free radical is got over
By force.
(3) antioxidant activity of [DPPH] method measurement biologically active peptide DKLAQ
1) sample sets: 80 μ L concentration are added in 96 orifice plates and add respectively for 1mmol/L [DPPH] methanol solution, by table 2
Enter sample to be tested (DKLAQ), the positive control 1 (Trolox of 2.5mg/mL), positive control 2 of 20 μ L various concentrations
(Trolox of 0.025mg/mL) and negative control (phytic acid)；
2) blank group: being 1mmol/L [DPPH] methanol solution and 20 μ L so that 80 μ L concentration are added on same 96 orifice plate
The sample of deionized water does blank control.
After sample to be tested is loaded, it is stored at room temperature 90min, detects light absorption value at 517nm with microplate reader.Under
Formula calculates free radical scavenging activity, and experimental result is shown in Table 2.
Formula:
The antioxidant activity result of [DPPH] method of table 2 measurement biologically active polypeptide
From table 2 it can be seen that the Trolox of the 2.5mg/mL as positive control have under the same conditions it is strongest clear
Except the ability of free radical, free radical all in solution can be almost removed, is secondly Trolox, the phytic acid, work of 0.025mg/mL
Property polypeptide.It is 29.89% that polypeptide DKLAQ, which removes [DPPH] free radical rate, and with the reduction of DKLAQ concentration, is removed certainly
By base reduced capability.
2, FARP method measures biologically active peptide DKLAQ antioxidant activity in vitro
1) experiment reagent and instrument
Total antioxidant capacity detection kit (Ferric Reducing Ability of Plasma FRAP method), is purchased from
Shanghai green skies biotechnology company；FeSO4Solution (10mmol/L), watermiscible vitamin E (Trolox solution) (10mmol/
L), the biologically active polypeptide DKLAQ that embodiment 1 obtains.
Key instrument: Sunrise microplate reader, Austrian Tecan Products；96 porocyte culture plates, the U.S.
The manufacture of Millipore company；Assay balance, Meitelei-tolido Products；HWS26 type electric-heated thermostatic water bath, Shanghai
One permanent Science and Technology Ltd.'s manufacture.
2) experimental method
(1) preparation of FRAP working solution
According to total antioxidant capacity detection kit, TPTZ 7.5mL dilution, 750 μ L solution of TPTZ, detection are buffered
750 μ L of liquid is uniformly mixed, and is incubated in 37 DEG C of water-baths, is finished in 2 hours h.
(2)FeSO4The production of standard curve curve measures
180 μ LFRAP working solutions are first added in 96 orifice plates, 5 μ L FeSO are added by table 34Calibration curve solution is gently mixed
It is even, after 37 DEG C of incubation 3-5min, light absorption value is measured at 593nm with microplate reader.
3 FeSO of table4The solution of standard curve determination is prepared
FeSO4Concentration and light absorption value are in good proportional relation, FeSO4Concentration is higher, and light absorption value is higher.FeSO of the present invention4
Standard curve result is shown in Fig. 5, and the linear relationship of standard curve is good, related coefficient 0.998, FeSO4The precision of standard curve
Degree and accuracy meet testing requirements, can be used for subsequent calculating.
(3) oxidation resistance of FRAP method measurement biologically active polypeptide DKLAQ
180 μ L FRAP working solutions are first added in 96 orifice plates, 5 μ L ddH are added in blank control wells2O, sample detection hole
5 μ L phytic acid are added in 5 μ L samples to be tested of interior addition, positive control, mixes gently, after 37 DEG C of incubation 3-5min, is existed with microplate reader
Light absorption value is measured at 593nm.Total antioxidant capacity representation is with FeSO4The concentration of standard solution indicates.It counts according to the following formula
Free radical scavenging activity is calculated, experimental result is shown in Table 4.
The total antioxidant capacity result of 4 FARP method of table measurement biologically active polypeptide DKLAQ
By total antioxidant capacity method (Ferric Reducing Ability Power FRAP method) to polypeptide DKLAQ's
External total antioxidant activity is determined, and discovery biologically active polypeptide DKLAQ has the ability of preferable reduction-oxidation substance；
When concentration is 4mg/mL, the total antioxidation level of polypeptide DKLAQ reaches 0.0238mmol/g；Illustrate biologically active polypeptide
The total antioxidant capacity of DKLAQ has conspicuousness (p > 0.05) higher than the phytic acid with weak antioxidant activity under comparable sodium
Difference.Therefore, it can assert that the biologically active polypeptide DKLAQ of invention has significant oxidation resistance.
The activity of fighting against senium of 3 biologically active peptide of embodiment is tested
One, experiment of the biologically active polypeptide DKLAQ to caenorhabditis elegan aging effects
1. experiment reagent and instrument:
Reagent: caenorhabditis elegan (Caenorhabditis elegans), attached Chinese and Western binding institute of Fudan University；Large intestine
Bacterial strain E.coli OP50, attached Chinese and Western binding institute of Fudan University；Agar powder, Sinopharm Chemical Reagent Co., Ltd.；Ferment
Female powder, Sinopharm Chemical Reagent Co., Ltd.；5-fluor-uracil, Sigma Co., USA；The bioactivity that embodiment 1 obtains
Polypeptide DKLAQ.
Instrument and equipment: power health RO15 pure water system, Li Kang biologic medical Science and Technology Ltd.；G136T type Zealway intelligence
High-temperature sterilization pot, Xiamen Zhi Wei instrument Science and Technology Ltd.；THZ-32 type Desk type constant-temperatureoscillator oscillator, Shanghai precision experimental facilities have
Limit company；TDL-40B centrifuge, Anting Scientific Instrument Factory, Shanghai；Lu Xiang instrument GL-22M high speed freezing centrifuge, Shanghai Lu Xiang instrument
Instrument Ltd.；Win fast BJ-CD SERIES Biohazard Safety Equipment, Shanghai Bo Xun Industrial Co., Ltd.；Nikko is inverted electronic display
Micro mirror, Nikon Corp..
2. experimental method:
(1) prepared by NGM plate
Take strain Escherichia coli in LB plate streaking, picking single bacterium is fallen in 10ml LB liquid medium, and 37 DEG C,
200rpm, shaken cultivation for 24 hours, until OD600=0.4 for be inoculated with NGM plate feed nematode.100 μ L bacterium solutions are taken to be applied to 60mm
NGM plate notices that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM plate having been coated with is in room temperature (21-25 DEG C) mistake
It can be used after night.
(2) nematode culture
Nematode used in this experiment is hermaphroditic, Standard culture conditions (20 DEG C of temperature, humidity 40%~
60%) growth is cultivated under.
(3) the synchronization processing of nematode
1) sodium perchlorate bleaching
Prepare pregnant worm growth plate (80% or more insect is in reproduction period i.e. in plate) 2-3 plate, 5ml M9 buffer is taken to rinse 2
It is secondary, buffer is sucked in 15ml centrifuge tube, 1000r/min is centrifuged 3min, discards supernatant.5ml is added and newly matches synchronization bleaching
Liquid acutely vibrates 2.5min at room temperature, adult polypide is corroded.Centrifugation, discards supernatant.Guarantee total processing time no more than
5min prevents damage worm's ovum.It adds M9 buffer precipitating is resuspended, is centrifuged, discards supernatant after mixing, repeat this process 3 times.
2) it prescribes a time limit oviposition method
The picking several nematodes in the egg-laying season are in same plate, and the particular number of picking is with required synchronization nematode
Number is foundation.Under general condition, an egg-laying season nematode can lay eggs 6 or so within 1h.After cultivating 0.5h in plate,
Choose nematode in plate, then the ovum in plate is in same growth period.
(4) index determining
Experimental group: blank group and polypeptide group.Several of L4 phase nematode is chosen, after synchronization processing, is respectively placed in corresponding
In NGM plate；Every group of nematode population is no less than 60, is denoted as 0 day, is transferred in new plate daily at this time, arrives the reproduction later period
It does not retransfer.Record nematode is dead daily and eliminates the item number of experiment.Wherein contain in each NGM plate of life experiment
12.5mg/L 5-fluor-uracil is to inhibit nematode reproduction.Nematode death judgment criteria: without mobile and swallowing act, after touching still
Without any reaction.Rejecting standard: it 1. flees to plate wall or covers and thirst；2. worm's ovum is hatched in vivo into bag sample worm: 3.
It pierces in agar.
3. experimental result and analysis:
Influence of the 5 biologically active polypeptide DKLAQ of table to the nematode service life
It can be seen from table 5 and Fig. 6 when the mass concentration of feeding polypeptide DKLAQ is 300mg/L, nematode in experimental group
Average life span extend about 9.67% respectively, meanwhile, the half death time has even more obtained conspicuousness raising (P <
0.05), the MaLS time also extends 4 days respectively compared to blank group.It is even more that can be intuitive to see in Fig. 6, same time
Point, nematode survival rate is apparently higher than blank group in experimental group, and the nematode service life is extended.It is demonstrated experimentally that the polypeptide that experiment uses
Mass concentration is suitable.It can effectively delay nematode aging, improve survival rate, and also further demonstrate that polypeptide simultaneously
DKLAQ extends the effect in service life not by inhibiting nematode reproductive capacity to realize, because its with good anti-oxidation function and compared with
Strong Scavenging ability.
Two, the Acute oxidative of biologically active polypeptide DKLAQ stress survival experiment
1. experiment reagent and instrument:
Reagent: caenorhabditis elegan (Caenorhabditis elegans), attached Chinese and Western binding institute of Fudan University；Large intestine
Bacterial strain E.coli OP50, attached Chinese and Western binding institute of Fudan University；Agar powder, Sinopharm Chemical Reagent Co., Ltd.；Ferment
Female powder, Sinopharm Chemical Reagent Co., Ltd.；30% hydrogenperoxide steam generator, Sinopharm Chemical Reagent Co., Ltd.；Implement
The biologically active polypeptide DKLAQ that example 1 obtains.
Instrument and equipment: power health RO15 pure water system, Li Kang biologic medical Science and Technology Ltd.；G136T type Zealway intelligence
High-temperature sterilization pot, Xiamen Zhi Wei instrument Science and Technology Ltd.；THZ-32 type Desk type constant-temperatureoscillator oscillator, Shanghai precision experimental facilities have
Limit company；TDL-40B centrifuge, Anting Scientific Instrument Factory, Shanghai；Lu Xiang instrument GL-22M high speed freezing centrifuge, Shanghai Lu Xiang instrument
Instrument Ltd.；Win fast BJ-CD SERIES Biohazard Safety Equipment, Shanghai Bo Xun Industrial Co., Ltd.；Nikko is inverted electronic display
Micro mirror, Nikon Corp..
2. experimental method:
(1) prepared by NGM plate
Take strain Escherichia coli in LB plate streaking, picking single bacterium is fallen in 10ml LB liquid medium, and 37 DEG C,
200rpm, shaken cultivation for 24 hours, until OD600=0.4 for be inoculated with NGM plate feed nematode.100 μ L bacterium solutions are taken to be applied to 60mm
NGM plate notices that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM plate having been coated with is in room temperature (21-25 DEG C) mistake
It can be used after night.
(2) nematode culture
Nematode used in this experiment is hermaphroditic, Standard culture conditions (20 DEG C of temperature, humidity 40%~
60%) growth is cultivated under.
(3) the synchronization processing of nematode
1) sodium perchlorate bleaching
Prepare pregnant worm growth plate (80% or more insect is in reproduction period i.e. in plate) 2-3 plate, 5ml M9 buffer is taken to rinse 2
It is secondary, buffer is sucked in 15ml centrifuge tube, 1000r/min is centrifuged 3min, discards supernatant.5ml is added and newly matches synchronization bleaching
Liquid acutely vibrates 2.5min at room temperature, adult polypide is corroded.Centrifugation, discards supernatant.Guarantee total processing time no more than
5min prevents damage worm's ovum.It adds M9 buffer precipitating is resuspended, is centrifuged, discards supernatant after mixing, repeat this process 3 times.
2) it prescribes a time limit oviposition method
The picking several nematodes in the egg-laying season are in same plate, and the particular number of picking is with required synchronization nematode
Number is foundation.Under general condition, an egg-laying season nematode can lay eggs 6 or so within 1h.After cultivating 0.5h in plate,
Choose nematode in plate, then the ovum in plate is in same growth period.
(4) index determining
Experimental group: blank group and polypeptide group.By synchronization, treated that L4 phase nematode is placed in corresponding NGM plate, experiment
In H containing 20mM2O2NGM plate in carry out, every plate quantity is no less than 10, count that nematode is dead, viable count per half an hour,
Nematode death judgment criteria: without mobile and swallowing act, still without any reaction after touching.Rejecting standard: it 1. flees to plate wall
Or it covers and thirst；2. worm's ovum is hatched in vivo into bag sample worm: 3. piercing in agar.
3. experimental result and analysis:
Influence of the 6 biologically active polypeptide DKLAQ of table to nematode under oxidative stress
As can be seen from Table 6, there is conspicuousness to improve (P < 0.05) for experimental group nematode average life span under oxidative stress,
Extremely significant difference (P < 0.05) is presented in polypeptide DKLAQ group.The each group half death time also it is corresponding to a certain extent
Extend, hybrid peptide group is presented conspicuousness and improves (P < 0.05) compared with other experimental groups.As shown in fig. 7, in oxidative stress condition
Under, experimental group survival rate is obviously higher than blank group survival rate.Under the conditions of oxidative stress, the survival rate of nematode obtains this explanation
It significantly improves, it may be possible to since polypeptide DKLAQ can effectively help nematode to resist oxidative damage, remove the free radical generated in vivo
And the accumulation of peroxide is reduced, rather than realized by enhancing its heat hardiness.The extension of organism life-span is to a certain extent
It is the resistance due to improving cell to stress conditions, thus delays senescence and exist very with the survival rate under pressure stressed condition
Important Relations.This results show polypeptide DKLAQ can increase the oxidative stress ability of nematode significantly, improve the survival of nematode
Rate illustrates that certain density polypeptide DKLAQ has anti-aging function for nematode.
Three, the pressure acute stress experiment in vivo of biologically active polypeptide DKLAQ
1. experiment reagent and instrument:
Reagent: caenorhabditis elegan (Caenorhabditis elegans), attached Chinese and Western binding institute of Fudan University；Large intestine
Bacterial strain E.coli OP50, attached Chinese and Western binding institute of Fudan University；Agar powder, Sinopharm Chemical Reagent Co., Ltd.；Ferment
Female powder, Sinopharm Chemical Reagent Co., Ltd.；30% hydrogenperoxide steam generator, Sinopharm Chemical Reagent Co., Ltd.；The third two
Aldehyde (MDA) assay kit, Biotechnology Co., Ltd is built up in Nanjing；Active oxygen (ROS) assay kit, biology is built up in Nanjing
Science and Technology Ltd.；Superoxide dismutase (SOD) kit, Biotechnology Co., Ltd is built up in Nanjing；What embodiment 1 obtained
Biologically active polypeptide DKLAQ.
Instrument and equipment: power health RO15 pure water system, Li Kang biologic medical Science and Technology Ltd.；G136T type Zealway intelligence
High-temperature sterilization pot, Xiamen Zhi Wei instrument Science and Technology Ltd.；THZ-32 type Desk type constant-temperatureoscillator oscillator, Shanghai precision experimental facilities have
Limit company；TDL-40B centrifuge, Anting Scientific Instrument Factory, Shanghai；Lu Xiang instrument GL-22M high speed freezing centrifuge, Shanghai Lu Xiang instrument
Instrument Ltd.；Win fast BJ-CD SERIES Biohazard Safety Equipment, Shanghai Bo Xun Industrial Co., Ltd.；Nikko is inverted electronic display
Micro mirror, Nikon Corp.；II D ultrasonic cell disruptor of JY92-, Shanghai is than bright Instrument Ltd..
2. experimental method:
(1) prepared by NGM plate
Take strain Escherichia coli in LB plate streaking, picking single bacterium is fallen in 10ml LB liquid medium, and 37 DEG C,
200rpm, shaken cultivation for 24 hours, until OD600=0.4 for be inoculated with NGM plate feed nematode.100 μ L bacterium solutions are taken to be applied to 60mm
NGM plate notices that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM plate having been coated with is in room temperature (21-25 DEG C) mistake
It can be used after night.
(2) nematode culture
Nematode used in this experiment is hermaphroditic, Standard culture conditions (20 DEG C of temperature, humidity 40%~
60%) growth is cultivated under.
(3) the synchronization processing of nematode
1) sodium perchlorate bleaching
Prepare pregnant worm growth plate (80% or more insect is in reproduction period i.e. in plate) 2-3 plate, 5ml M9 buffer is taken to rinse 2
It is secondary, buffer is sucked in 15ml centrifuge tube, 1000r/min is centrifuged 3min, discards supernatant.5ml is added and newly matches synchronization bleaching
Liquid acutely vibrates 2.5min at room temperature, adult polypide is corroded.Centrifugation, discards supernatant.Guarantee total processing time no more than
5min prevents damage worm's ovum.It adds M9 buffer precipitating is resuspended, is centrifuged, discards supernatant after mixing, repeat this process 3 times.
2) it prescribes a time limit oviposition method
The picking several nematodes in the egg-laying season are in same plate, and the particular number of picking is with required synchronization nematode
Number is foundation.Under general condition, an egg-laying season nematode can lay eggs 6 or so within 1h.After cultivating 0.5h in plate,
Choose nematode in plate, then the ovum in plate is in same growth period.
(4) index determining
Experiment is divided into non-treated experimental group, heat treatment experimental group and oxidation processes experimental group.
Wherein, non-treated experimental group is divided into non-treated group of blank and non-treated group of polypeptide again.Several of L4 phase nematode is chosen,
After synchronization processing, is rinsed and be centrifuged with M9 buffer, removal supernatant, addition PBS buffer solution, ultrasonication 2min,
Centrifugation obtains its tissue homogenate supernatant, and illustrates the measurement of progress SOD, MDA and ROS index according to kit immediately.
Heat treatment experimental group is divided into blank heat treatment group and polypeptide heat treatment group again.By synchronization treated L4 phase line
Worm is placed in corresponding NGM plate, and every plate is no less than 40, and experiment is placed in 35 DEG C of progress.After cultivating 2h, its indices is measured, is examined
Survey method is identical as non-treated experimental group.
Oxidation processes experimental group is divided into blank oxidation processes group and polypeptide oxidation processes group again.By synchronization treated L4
Phase nematode is placed in corresponding NGM plate, tests in H containing 20mM2O2NGM plate in carry out, every plate quantity is no less than 10.Culture
After 1h, its indices is measured, measuring method is identical as non-treated experimental group.
3. experimental result and analysis:
Influence of the 7 biologically active polypeptide DKLAQ of table to nematode SOD, MDA and ROS
As can be seen from Table 7, with the non-treated experimental group ratio of blank, blank heat treatment experiment group and blank oxidation processes are real
It tests the equal conspicuousness of MDA and ROS value in group to increase, SOD is substantially reduced (P < 0.05), this explanation either heat stress, or oxidation
Nematode body can stress be caused to damage.From in table it is also found that MDA and SOD is and blank group in non-treated group of polypeptide
Compared to presentation significant difference.
Under 35 DEG C for the treatment of conditions, only MDA reduces (P < 0.05) to polypeptide group, and ROS is unchanged with SOD.This is further
Its temperature capacity under stressed condition can not be improved by having proved milk-derived small peptide.Under 20mMH2O2 treatment conditions, polypeptide
There is conspicuousness variation (P < 0.05) in SOD and ROS value in group, and wherein the MDA value of polypeptide group is even more that extremely significant reduction (P is presented
<0.01).SOD content can be effectively improved by thinking in the online polypide of biologically active peptide DKLAQ, reduce lipid peroxide with
And the generation of active oxygen, show good anti-oxidant, removing free radical function.
The induced enzymes such as SOD can remove itself excessive free radical in time, keep the metabolic balance of interior free yl, be to measure
The index of body health situation；MDA can reflect body inner lipid peroxide reactions degree, reflect that body is damaged journey indirectly
Degree；Reactive oxygen species ROS is that aerobic cell generates in the metabolic process, can lead to Apoptosis by response to oxidative stress.Cause
This, three indexs are used in combination the oxidation resistance that can be well reflected out body and are damaged degree.According to this experiment
As a result, biologically active peptide DKLAQ can improve the intracorporal Antioxidant Enzymes activity of nematode to a certain extent, and in oxidative stress item
Under part, effective protection body resists oxidative damage, removes free radical, but can not significantly improve its heat hardiness.
The above description of the embodiments is intended to facilitate ordinary skill in the art to understand and use the invention.
Person skilled in the art obviously easily can make various modifications to these embodiments, and described herein general
Principle is applied in other embodiments without having to go through creative labor.Therefore, the present invention is not limited to the above embodiments, ability
Field technique personnel announcement according to the present invention, improvement and modification made without departing from the scope of the present invention all should be of the invention
Within protection scope.
Sequence table
<110>Shanghai Communications University；Zhejiang Hui Tai life and health Science and Technology Ltd.
<120>a kind of biologically active polypeptide DKLAQ and its preparation method and application
<160> 3
<170> SIPOSequenceListing 1.0
<210> 1
<211> 5
<212> PRT
<213>artificial sequence (Artificial Sequence)
<400> 1
Asp Lys Leu Ala Gln
1 5
<210> 2
<211> 15
<212> DNA
<213>artificial sequence (Artificial Sequence)
<400> 2
acaagcttgc tcaag 15
<210> 3
<211> 382
<212> PRT
<213>artificial sequence (Artificial Sequence)
<400> 3
Val Arg Lys Tyr Leu Gln Ile Met Ala Leu Ala Gly Ala Met Leu Thr
1 5 10 15
Leu Ser Gly Cys Gly Lys Leu Lys Asp Ser Ser Leu Ala Asn Asn Ala
20 25 30
Thr Thr Thr Ser Thr Ala Lys Lys Lys Ser Tyr Gln Thr Thr Asn Thr
35 40 45
Gly Lys Asn Gly Tyr Thr Val Leu Met Lys Asn Gly Arg Tyr Val Ile
50 55 60
Ser Pro Ile Ala Gly Leu Thr Ala Thr Asn Asn Asp Asn Ser Val Asp
65 70 75 80
Thr Arg Glu Leu Glu Arg Gly Leu Ile Gln Ile Ser Lys Asn Gln Phe
85 90 95
Ser Pro Asn Gln Tyr Val Phe Gln Glu Gly Gln Tyr Leu Asp Thr Ser
100 105 110
Thr Val Thr Asp Trp Leu Thr Arg Lys Ser Lys Ser Asn Pro Lys Gly
115 120 125
Leu Asn Pro Ala Asn Asn Gly Lys Thr Gly Pro Asp Thr Arg Asn Pro
130 135 140
Ile Tyr Leu Glu Glu Ile Val Glu Gln Asp Tyr Leu Thr Gly Ser Gly
145 150 155 160
Ser Lys Tyr Gln Leu Gly Gly Met Ser Leu Gly Leu Ala Met Asn Ser
165 170 175
Val Asp Tyr Tyr Gln Lys Lys Arg Asn Gly Ala Glu Phe Lys Thr Glu
180 185 190
Ile Ser Arg Ala Glu Gln Lys Ala Gln Gly Glu Lys Ile Ala Asn Glu
195 200 205
Ile Ile Ala Arg Leu Arg Lys Lys Lys Val Leu Lys Asn Ile Pro Ile
210 215 220
Thr Ile Gly Leu Phe Ser Lys Thr Glu Lys Asp Ser Leu Val Gly Gly
225 230 235 240
Thr Tyr Phe Ala Tyr Gly Thr Ala Ala Ala Asn Ser Ser Lys Ile Thr
245 250 255
Lys Trp Lys Ser Val Ser Glu Lys Met Gln Val Leu Pro Thr Thr Gly
260 265 270
Asn Glu Lys Ala Ile Asn Ser Asp Asp Ala Ser His Phe Asn Asp Phe
275 280 285
Lys Ala Ala Ile Gln Asn Tyr Phe Pro Asn Ile Ser Gly Val Thr Ala
290 295 300
Thr Leu Arg Tyr Asp Asn Asp Lys Leu Ala Gln Glu Asn Ile Ser Ile
305 310 315 320
Thr Thr Gln Phe Tyr Gly Tyr Glu Gln Ile Gln Ser Phe Thr Arg Leu
325 330 335
Val Leu Ser Ser Ala Lys Lys Tyr Leu Pro Asn Asn Val Pro Ile Glu
340 345 350
Ile Lys Ile Gly Ser Val Asn Asp Val Gln Ala Leu Ile Ala Lys Glu
355 360 365
Thr Gly Asp Ser Asp Tyr Gln Val His Val Tyr Gly Gly Glu
370 375 380
Claims (10)
1. a kind of biologically active polypeptide DKLAQ, which is characterized in that its amino acid sequence is Asp-Lys-Leu-Ala-Gln.
2. a kind of biologically active polypeptide DKLAQ according to claim 1, which is characterized in that the biologically active polypeptide comes
Derived from Lactobacillus helveticus mycoprotein.
3. encoding the nucleotide fragments of biologically active polypeptide DKLAQ described in claim 1, which is characterized in that the nucleotide piece
The sequence of section is as shown in SEQ ID NO:2.
4. the preparation method of biologically active polypeptide DKLAQ as described in claim 1, which is characterized in that pass through the side of genetic engineering
Method is artificial synthesized or Lactobacillus helveticus thallus is directly obtained by the method that clasmatosis isolates and purifies, or directly passes through chemistry
It is synthetically prepared.
5. the application of biologically active polypeptide DKLAQ as described in claim 1, which is characterized in that the biologically active polypeptide DKLAQ
Application in food, health care product, drug or the cosmetics that preparation has anti-oxidation function.
6. the application of biologically active polypeptide DKLAQ as described in claim 1, which is characterized in that the biologically active polypeptide DKLAQ
Application in the food, health care product or drug that preparation has anti-senescence function.
7. the application of biologically active polypeptide DKLAQ as described in claim 1, which is characterized in that the biologically active polypeptide DKLAQ
Application in the food, health care product or drug that preparation has anti-oxidation function and anti-senescence function.
8. a kind of oxidation resistant product, which is characterized in that including biologically active polypeptide DKLAQ as described in claim 1 or the life
The derivative of object active peptides DKLAQ；The oxidation resistant product includes antioxidant food, antioxidant health-care product, antioxidant drug
Object or antioxidation cosmetic product；The derivative of the biologically active polypeptide DKLAQ, refers to the amino in biologically active polypeptide DKLAQ
On sour side-chain radical, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonylation, methylation, acetylation, phosphorylation, esterification
Or glycosylation modified, obtained polypeptide derivative.
9. a kind of anti-aging product, which is characterized in that including biologically active polypeptide DKLAQ as described in claim 1 or the life
The derivative of object active peptides DKLAQ；The anti-aging product includes antisenility cistanche food, antisenescence health product or Kangshuaining mixture
Object；The derivative of the biologically active polypeptide DKLAQ, refers on the amino acid side groups of biologically active polypeptide DKLAQ, ammonia
Cardinal extremity or c-terminus carry out hydroxylating, carboxylated, carbonylation, methylation, acetylation, phosphorylation, esterification or glycosylation modified, obtain
The polypeptide derivative arrived.
10. a kind of product with anti-oxidation function and anti-senescence function, which is characterized in that including giving birth to as described in claim 1
The derivative of object active peptides DKLAQ or the biologically active polypeptide DKLAQ；Production with anti-oxidation function and anti-senescence function
Product include food, health care product or drug；The derivative of the biologically active polypeptide DKLAQ, refers in biologically active polypeptide DKLAQ
Amino acid side groups on, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonylation, methylation, acetylation, phosphoric acid
Change, esterification or glycosylation modified, obtained polypeptide derivative.
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| CN201811003878.5A CN109160945B (en) | 2018-08-30 | 2018-08-30 | Bioactive polypeptide DKLAQ and preparation method and application thereof |
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN111100196A (en) * | 2019-11-08 | 2020-05-05 | 上海交通大学 | Bioactive polypeptide QILSVPGWTYSR, and preparation method and application thereof |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2009121176A1 (en) * | 2008-03-31 | 2009-10-08 | The University Of British Columbia | Insulin-induced gene (insig) peptide compositions and methods for cytoprotection |
| CN105254750A (en) * | 2015-10-16 | 2016-01-20 | 上海交通大学 | Bioactive polypeptide FGYSGAFKCL as well as preparation and application thereof |
-
2018
- 2018-08-30 CN CN201811003878.5A patent/CN109160945B/en active Active
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2009121176A1 (en) * | 2008-03-31 | 2009-10-08 | The University Of British Columbia | Insulin-induced gene (insig) peptide compositions and methods for cytoprotection |
| CN105254750A (en) * | 2015-10-16 | 2016-01-20 | 上海交通大学 | Bioactive polypeptide FGYSGAFKCL as well as preparation and application thereof |
Non-Patent Citations (2)
| Title |
|---|
| 20161231: "瑞士乳杆菌胞内生物活性肽的分离鉴定", 《中国乳品工业》 * |
| JIEHUI,ZHOU 等: "Immunomodulating effects of casein-derived peptides QEPVL and QEPV on lymphocytes in vitro and in vivo", 《FOOD & FUNCTION》 * |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN111100196A (en) * | 2019-11-08 | 2020-05-05 | 上海交通大学 | Bioactive polypeptide QILSVPGWTYSR, and preparation method and application thereof |
| CN111100196B (en) * | 2019-11-08 | 2021-07-13 | 上海交通大学 | Bioactive polypeptide QILSVPGWTYSR, and preparation method and application thereof |
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| Publication number | Publication date |
|---|---|
| CN109160945B (en) | 2021-03-23 |
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