CN108794605A - A kind of biologically active polypeptide SRPETSG and its preparation method and application - Google Patents
A kind of biologically active polypeptide SRPETSG and its preparation method and application Download PDFInfo
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- CN108794605A CN108794605A CN201810718874.9A CN201810718874A CN108794605A CN 108794605 A CN108794605 A CN 108794605A CN 201810718874 A CN201810718874 A CN 201810718874A CN 108794605 A CN108794605 A CN 108794605A
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- Prior art keywords
- srpetsg
- biologically active
- active polypeptide
- polypeptide
- derivative
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- AUMNPAUHKUNHHN-BYULHYEWSA-N Val-Asn-Asp Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CC(=O)O)C(=O)O)N AUMNPAUHKUNHHN-BYULHYEWSA-N 0.000 description 1
- PTFPUAXGIKTVNN-ONGXEEELSA-N Val-His-Gly Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)NCC(=O)O)N PTFPUAXGIKTVNN-ONGXEEELSA-N 0.000 description 1
- HGJRMXOWUWVUOA-GVXVVHGQSA-N Val-Leu-Gln Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CCC(=O)N)C(=O)O)NC(=O)[C@H](C(C)C)N HGJRMXOWUWVUOA-GVXVVHGQSA-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
- IJGPOONOTBNTFS-GVXVVHGQSA-N Val-Lys-Glu Chemical compound [H]N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(O)=O IJGPOONOTBNTFS-GVXVVHGQSA-N 0.000 description 1
- NZGOVKLVQNOEKP-YDHLFZDLSA-N Val-Phe-Asn Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC(=O)N)C(=O)O)N NZGOVKLVQNOEKP-YDHLFZDLSA-N 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
- 238000009825 accumulation Methods 0.000 description 1
- 229960000583 acetic acid Drugs 0.000 description 1
- 239000011149 active material Substances 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 230000001464 adherent effect Effects 0.000 description 1
- 108010044940 alanylglutamine Proteins 0.000 description 1
- 108010047495 alanylglycine Proteins 0.000 description 1
- 230000002605 anti-dotal effect Effects 0.000 description 1
- 230000003064 anti-oxidating effect Effects 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 230000003078 antioxidant effect Effects 0.000 description 1
- 108010008355 arginyl-glutamine Proteins 0.000 description 1
- 108010060035 arginylproline Proteins 0.000 description 1
- 108010040443 aspartyl-aspartic acid Proteins 0.000 description 1
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- 229940098773 bovine serum albumin Drugs 0.000 description 1
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- 229940021722 caseins Drugs 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 239000012930 cell culture fluid Substances 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
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- 210000003022 colostrum Anatomy 0.000 description 1
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- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- 239000012362 glacial acetic acid Substances 0.000 description 1
- 108010049041 glutamylalanine Proteins 0.000 description 1
- XKUKSGPZAADMRA-UHFFFAOYSA-N glycyl-glycyl-glycine Natural products NCC(=O)NCC(=O)NCC(O)=O XKUKSGPZAADMRA-UHFFFAOYSA-N 0.000 description 1
- 108010026364 glycyl-glycyl-leucine Proteins 0.000 description 1
- 108010082286 glycyl-seryl-alanine Proteins 0.000 description 1
- 108010089804 glycyl-threonine Proteins 0.000 description 1
- 108010050848 glycylleucine Proteins 0.000 description 1
- 108010015792 glycyllysine Proteins 0.000 description 1
- 229960002163 hydrogen peroxide Drugs 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
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- 229940088592 immunologic factor Drugs 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
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- 150000002500 ions Chemical class 0.000 description 1
- 108010044374 isoleucyl-tyrosine Proteins 0.000 description 1
- 108010078274 isoleucylvaline Proteins 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 238000009533 lab test Methods 0.000 description 1
- 108010091871 leucylmethionine Proteins 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
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- 108010003700 lysyl aspartic acid Proteins 0.000 description 1
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- 238000010369 molecular cloning Methods 0.000 description 1
- PGSADBUBUOPOJS-UHFFFAOYSA-N neutral red Chemical compound Cl.C1=C(C)C(N)=CC2=NC3=CC(N(C)C)=CC=C3N=C21 PGSADBUBUOPOJS-UHFFFAOYSA-N 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 239000003399 opiate peptide Substances 0.000 description 1
- 229940126701 oral medication Drugs 0.000 description 1
- 230000004792 oxidative damage Effects 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 230000000242 pagocytic effect Effects 0.000 description 1
- 229940055695 pancreatin Drugs 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 230000000737 periodic effect Effects 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 230000000770 proinflammatory effect Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 125000006239 protecting group Chemical group 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000000197 pyrolysis Methods 0.000 description 1
- 150000003254 radicals Chemical class 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 239000011435 rock Substances 0.000 description 1
- 238000005070 sampling Methods 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
- 210000000952 spleen Anatomy 0.000 description 1
- 239000012192 staining solution Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000009747 swallowing Effects 0.000 description 1
- 230000035922 thirst Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 150000003852 triazoles Chemical class 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
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- 108010003137 tyrosyltyrosine Proteins 0.000 description 1
- 238000000825 ultraviolet detection Methods 0.000 description 1
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- 238000005303 weighing Methods 0.000 description 1
- 210000004885 white matter Anatomy 0.000 description 1
- 235000013618 yogurt Nutrition 0.000 description 1
- 235000021247 β-casein Nutrition 0.000 description 1
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
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
-
- 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
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Organic Chemistry (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Molecular Biology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Pharmacology & Pharmacy (AREA)
- Food Science & Technology (AREA)
- Toxicology (AREA)
- Mycology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Dermatology (AREA)
- Polymers & Plastics (AREA)
- Nutrition Science (AREA)
- Birds (AREA)
- Epidemiology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The present invention relates to albumen fields, and in particular to its amino acid sequence of a kind of biologically active polypeptide SRPETSG and its preparation method and application, biologically active polypeptide SRPETSG is Ser-Arg-Pro-Glu-Thr-Ser-Gly.By the experiment of ion vitro immunization function point analysis, internal Antisenility Experiment, demonstrating polypeptide SRPETSG has preferable immunoloregulation function and activity of fighting against senium, on the one hand, the biologically active polypeptide SRPETSG of the present invention can enhance the in-vitro multiplication ability of lymphocyte and macrophage, the ability that body resists extraneous pathogenic infection is improved, body incidence is reduced；On the other hand, the vigor of internal anti-peroxidation enzyme system can be improved, enhance the function that body resists external source sexual stimulus, to reduce organism aging process, aging and sick probability, there is immunoloregulation function, the food of anti-senescence function, health products 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 SRPETSG and preparation method thereof and answer
With.
Background technology
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 some itself synthesis for lactic acid bacteria thalline
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 enzymolysis, and biologically active polypeptide is by 2~20 mostly
Amino acid residue forms, and molecular weight is less than 6000Da, contains a certain amount of hydrophobic amino acid, aromatic amino acid.
Immune-active peptides are to obtain and prove that one kind biology of its physiological activity is living from breast for the first time after opioid peptides discovery
Property polypeptide.Jolles in 1981 et al. has found for the first time, using trypsin hydrolysis people lactoprotein, can obtain an amino acid sequence
It is classified as the hexapeptide of Val-Glu-Pro-Ile-Pro-Tyr, experiment in vitro proves that the peptide can enhance Turnover of Mouse Peritoneal Macrophages pair
The phagocytosis of sheep red blood cell (SRBC).Migliore-Samour et al. has found the hexapeptide Thr-Thr-Met-Pro- from casein
Leu-Trp can stimulate sheep erythrocyte to the phagocytosis of mouse peritoneal macrophages and enhancing for kerekou pneumonia primary
The resistance of bacterium.Newborn source immunomodulatory peptides (PGPIPN) the feeding rat of Li Su duckweeds et al. synthesis finds rat peritoneal macrophages
Phagocytosis and the relevant immunoloregulation function of red blood cell have significant enhancing.
Studies have shown that immune-active peptides can not only enhance immunity of organisms, the proliferation of body lymphocyte, enhancing are stimulated
The phagocytic function of macrophage promotes the release of cell factor, improves the ability that body resists extraneous pathogenic infection, reduces machine
Body incidence, and the immunological rejection of body will not be caused.
Aging is a natural phenomena, and process is often accompanied by the variation of antioxidant levels, organ-tissue, immune factor,
Complicated variation occurs for middle cell factor, such as the trend that proinflammatory cytokine IL-6, IL-4, TNF-α presentation increase, IL-6
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 by using 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 as a kind of emerging antidotal agent, in terms of physiological function have amino acid cannot compare it is excellent
Gesture can generate promotion or inhibiting effect to the enzyme in organism, improve the absorption to minerals and other nutrients and profit
With removing interior free yl enhances the resistance to oxidation of body itself, to slow down aging.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. pass through 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 to be 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- caseins disclose a kind of from α s2-
The milk-derived biologically active polypeptide NQFYQKF of casein.
Invention content
The purpose of the present invention is to provide a kind of biologically active polypeptide SRPETSG 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 SRPETSG, amino acid sequence Ser-Arg-Pro-
Glu-Thr-Ser-Gly, such as SEQ ID NO：Shown in 1.
Preferably, the biologically active polypeptide derives from Lactobacillus helveticus mycoprotein.It is derive specifically from LBH_1278 |
m.1190 LBH_1278|g.1190 ORF LBH_1278|g.1190 LBH_1278|m.1190 type:complete len:
350(+)LBH_1278:1-1050 (+), and the amino acid residue of the 29th~35, albumen thus.LBH_1278|m.1190
LBH_1278|g.1190 ORF LBH_1278|g.1190 LBH_1278|m.1190 type:complete len:350(+)
LBH_1278:1-1050 (+) amino acid sequence such as SEQ ID NO：Shown in 3.
LBH_1278|m.1190 LBH_1278|g.1190 ORF LBH_1278|g.1190 LBH_1278|m.1190
type:complete len:350(+)LBH_1278:The amino acid sequence and corresponding nucleotides sequence of 1-1050 (+) albumen
It is classified as existing technology, the bioactivity for encoding the nucleotide fragments energy encoding mature of this 29th~35 amino acids residue of albumen is more
Peptide SRPETSG.
Preferably, the biologically active polypeptide has immunoloregulation function and anti-senescence function.
Second aspect of the present invention provides the nucleotide fragments for encoding the biologically active polypeptide SRPETSG, sequence
For：5 '-tag tcg tcc aga aac cag tgg-3 ', such as SEQ ID NO：Shown in 2.
Third aspect present invention provides the preparation method of the biologically active polypeptide SRPETSG, can pass through gene work
The method of journey is artificial synthesized, can be directly obtained from Lactobacillus helveticus thalline by the method that clasmatosis isolates and purifies, can be with
Directly prepared by chemical synthesis.
Fourth aspect present invention provides the biologically active polypeptide SRPETSG and is preparing with immunoloregulation function
Application in food, health products, drug or cosmetics.
Fifth aspect present invention provides the biologically active polypeptide SRPETSG and is preparing the food with anti-senescence function
Application in product, health products or drug.
Sixth aspect present invention provides the biologically active polypeptide SRPETSG and is preparing while having immunological regulation work(
It can be with the application in the food, health products or drug of anti-senescence function.
Specifically, the biologically active polypeptide SRPETSG of the present invention, which can be used for preparing, reduces free radical to skin damage
Cosmetics, prepare the drug with immunological regulation and/or anti-aging；And due to the biologically active polypeptide of the present invention
Product after SRPETSG is degraded by gastrointestinal tract still has bioactivity, therefore can be also used for preparing the food such as Yoghourt, adjust
Save the health products of immunity, and the oral drug being used to prepare with immunological regulation and/or anti-aging.
Seventh aspect present invention provides a kind of immunological regulation product, including the biologically active polypeptide SRPETSG or institute
State the derivative of biologically active polypeptide SRPETSG；The immunological regulation product includes immunological regulation food, immunological regulation health care
Product, immunoregulation medicament or immunological regulation cosmetics；The derivative of the biologically active polypeptide SRPETSG refers to living in biology
Property polypeptide SRPETSG amino acid side groups on, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonylation, methyl
The modifications such as change, acetylation, phosphorylation, esterification or glycosylation, obtained polypeptide derivative.
Eighth aspect present invention provides a kind of anti-aging product, including the biologically active polypeptide SRPETSG or described
The derivative of biologically active polypeptide SRPETSG；The anti-aging product includes antisenility cistanche food, antisenescence health product or anti-ageing
Old drug；The derivative of the biologically active polypeptide SRPETSG refers to the amino acid side chain in biologically active polypeptide SRPETSG
On group, aminoterminal or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate, acetylation, phosphorylation, esterification or glycosyl
The modifications such as change, obtained polypeptide derivative.
Ninth aspect present invention provides product that is a kind of while having immunoloregulation function and anti-senescence function, including
The derivative of the biologically active polypeptide SRPETSG or described biologically active polypeptides SRPETSG；With immunoloregulation function and resist
The product of aging function includes food, health products or drug；The derivative of the biologically active polypeptide SRPETSG, refers in life
On the amino acid side groups of object active peptides SRPETSG, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonylation, first
The modifications such as base, acetylation, phosphorylation, esterification or glycosylation, obtained polypeptide derivative.
Biologically active polypeptide SRPETSG's of the present invention has the beneficial effect that：The biologically active polypeptide SRPETSG of the present invention has
It is preferable to adjust immunity of organisms activity and activity of fighting against senium；On the one hand, biologically active polypeptide SRPETSG of the invention can increase
The in-vitro multiplication ability of strong lymphocyte and macrophage improves the ability that body resists extraneous pathogenic infection, reduces body
Incidence；On the other hand, the vigor of internal anti-peroxidation enzyme system can be improved, enhancing body resists the function of external source sexual stimulus,
To reduce organism aging process, aging and sick probability, to developing the dairy products with immunoloregulation function and anti-senescence function
It is had a very important significance with health products.
Description of the drawings
Fig. 1：Mass chromatography extraction figure (m/z=734.3551)；
Fig. 2：The second order ms figure for the segment that mass-to-charge ratio is 734.3551；
Fig. 3：Influences of the various concentration SRPETSG to caenorhabditis elegan fecundity；
Fig. 4：Nematode growth conditions in the L4 phases under different condition of culture；
Fig. 5：The influence that biologically active polypeptide SRPETSG grows caenorhabditis elegan body；
Fig. 6：Influences of the biologically active polypeptide SRPETSG to caenorhabditis elegan under oxidative stress.
Specific implementation mode
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 the term used in the embodiment of the present invention is specific specific in order to describe
Embodiment, the protection domain being not intended to be limiting of the 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, in the present invention all technologies for using and
Scientific terminology is identical as the normally understood meaning of those skilled in the art of the present technique.Except used in embodiment specific method, equipment,
Outside material, the record according to those skilled in the art to the grasp of the prior art and the present invention can also use and this
Any method, equipment and the material of the similar or equivalent prior art of method, equipment described in inventive embodiments, 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 field.These technologies existing perfect explanation in the prior art, for details, reference can be made to Sambrook etc.
MOLECULAR CLONING：A LABORATORY MANUAL, Second edition, Cold Spring Harbor
Laboratory Press, 1989and Third edition, 2001；Ausubel etc., CURRENT PROTOCOLS IN
MOLECULAR BIOLOGY, John Wiley&Sons, New York, 1987 and periodic updates；the
Series METHODS IN ENZYMOLOGY, Academic Press, San Diego；Wolffe, CHROMATIN
STRUCTURE AND FUNCTION, Third edition, Academic Press, San Diego, 1998；METHODS IN
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 SRPETSG's of embodiment is artificial synthesized
One, the synthesis of biologically active peptide
1. RINK resin 3g (degree of substitution 0.3mmol/g) are weighed in the reactor of 150ml, with the dichloromethane 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 for use after resin is drained.
3. a certain amount of 20% piperidines (piperidines/DMF=1 is added into reactor:4,v:V), it is placed on decolorization swinging table and shakes
20min is shaken, the Fmoc blocking groups on resin are sloughed with this.It is washed four times with the DMF of 3 times of resin volumes after having taken off protection,
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 Ser in right amount and 1- hydroxyls-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, and N diisopropylcarbodiimide (DIC) oscillation shakes up 1min, waits for that solution is clear
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 for use with the DMF of 3 times of resin volumes afterwards.
7. a certain amount of 20% piperidines (piperidines/DMF=1 is added into reactor:4, v:V), it is placed on decolorization swinging table and shakes
20min is shaken, the Fmoc blocking groups on resin are sloughed with this.It is washed four times with DMF after having taken off protection, 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 generals of 25ml are added
It is dissolved, and the DIC oscillations that 2.5ml is then added shake up 1min, are 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 is colourless, illustrate that the reaction was complete；If resin has color, illustrate that condensation is incomplete, the reaction was continued.
11. after complete reaction, washing resin four times with DMF, then drains, a certain amount of 20% is added into reactor
Piperidines (piperidines/DMF=1:4,v:V), it is placed on decolorization swinging table and rocks 20min, the Fmoc protecting groups on resin are sloughed with this
Group.It is washed four times with DMF after having taken off protection, then drains whether detection protection sloughs.
12. connecting amino acid Arg, Pro, Glu, Thr, Ser and Gly successively according to step 9-11.
13. after connecting the last one amino acid, protection is sloughed, is washed four times with DMF, is then taken out resin with methanol
It is dry.Then with 95 cutting liquid (trifluoroacetic acids:1,2 dithioglycols:3, isopropyl base silane:Water=95:2:2:1, v:v:V) by polypeptide
(every gram of resin adds 10ml cutting liquids) is cut down from resin, and ice ether (cutting liquid is used in combination：Ether=1:9,v:V) centrifugation is heavy
Drop four times.
So far, artificial synthesized biologically active peptide SRPETSG.
Two, the confirmation of biologically active peptide
1) UPLC is analyzed
UPLC conditions are as follows：
Instrument：Waters ACQUITY UPLC ultra high efficiencies liquid phase-electron spray-level four bars-time of-flight mass spectrometer
Chromatographic column specification：BEH C18 chromatographic columns
Flow velocity：0.4mL/min
Temperature：50℃
Ultraviolet detection wavelength：210nm
Sample size：2μL
Gradient condition：A liquid：Water containing 0.1% formic acid (v/v), B liquid：Acetonitrile containing 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
Remove solvent temperature (DEG C)：350
Go 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 SRPETSG carries out chromatography and mass spectral analysis, and mass chromatography extraction figure is as shown in Figure 1, extract the second order ms at this peak
Figure and az, by crack conditions are as shown in Figures 2 and 3, and the polypeptide mass-to-charge ratio that can obtain this peak is 734.3551Da, and retention time is
32.6min。
3) result
From the figure 3, it may be seen that the case where being broken according to az, by, analyzes by Mascot softwares and calculates, obtain mass-to-charge ratio
The fragment sequence of 734.3551Da is Ser-Arg-Pro-Glu-Thr-Ser-Gly (SRPETSG), is denoted as SEQ ID NO：1.It should
Segment and LBH_1278 | m.1190 LBH_1278 | g.1190 ORF LBH_1278 | g.1190 LBH_1278 | m.1190
type:complete len:350(+)LBH_1278:The residue sequence of 1-1050 (+) 29-35 is corresponding, and sequence is shown in SEQ
ID NO：3.
The adjusting immunity of organisms activity experiment of 2 biologically active peptide of embodiment
One, mtt assay measures the vitro lymphocyte proliferation capacity experimental of biologically active polypeptide SRPETSG
1. experiment material and instrument：
Reagent and material：Experimental animal balb/c mouse (male 6-8 week old, Shanghai Communications University's agricultural and biological institute
Animal experimental center)；The biologically active polypeptide SRPETSG that embodiment 1 obtains；Mouse lymphocyte extracting solution (is purchased from Suo Laibao
Company)；RPMI1640 culture mediums (are purchased from GIBCO companies)；3- (4,5- dimethylthiazole -2) -2,5- diphenyltetrazolium bromide bromides
(MTT is purchased from Amresco companies)；ConA (ConA is purchased from Sigma companies)；(BSA is purchased from bovine serum albumin(BSA)
Genebase companies)；Pepsin (is purchased from Sigma companies)；Pancreatin (Corolase PP are purchased from AB companies).
Instrument and equipment：LRH-250F biochemical cultivation cases, Shanghai perseverance Science and Technology Ltd.；GL-22M high speed freezing centrifuges,
Shanghai Lu Xiang instrument centrifuges Instrument Ltd.；150 CO2 incubators of Hera cell, Heraeus companies；Dragon
Wellscan MK3 microplate reader, Labsystems companies；ALPHA 1-2-LD vacuum freeze driers, Christ companies；Superelevation
Effect liquid phase chromatogram-quadrupole rod time of-flight mass spectrometer, waters companies.
2. experimental method：
Mouse spleen is taken under aseptic condition, mouse lymphocyte is extracted with lymphocyte extracting solution, carries out Yuan Dynasty's culture.With
Cell density is adjusted to 2.5 × 10 by complete RPMI1640 culture solutions6A/mL.It is sequentially added in 96 porocyte culture plates：
100 μ L mouse lymphocyte suspensions, 100 μ L RPMI1640 complete culture solutions, 20 μ L ConAs, 100 μ L samples.In addition,
Blank control group (PBS of pH7.2~7.4,3mol/L) and negative control group (500 μ g/mL BSA) are set, research shows that its is right
It is not influenced in vitro lymphocyte proliferation.Every group of 3 parallel laboratory test samples.In 5%CO2After 68h being cultivated in 37 DEG C of incubators,
20 μ L MTT are added under aseptic condition per hole, continues to cultivate 4h, carefully discards supernatant liquid, 100 μ L dimethyl sulfoxide (DMSO)s are added per hole,
37 DEG C of biochemical cultivation cases hatch 10min, shake up, light absorption value is measured at 570nm with microplate reader.
Vitro lymphocyte proliferation ability indicates that computational methods are as follows with stimulus index：
In formula：A1For blank control at the 570nm under light absorption value；A2For negative control group at the 570nm under extinction
Value, A3For experimental group at the 570nm under light absorption value.
3. experimental result and analysis：
Influences of the 1 biologically active polypeptide SRPETSG of table to vitro lymphocyte proliferation
| Experiment packet | Stimulus index SI |
| Negative control group | 1 |
| SRPETSG | 1.212±0.221* |
Note：* labelled notation is the significant difference (P < 0.05) compared with negative control.
Experimental result is shown in Table 1.As shown in Table 1, in the condition that the mass concentration of biologically active peptide SRPETSG is 100 μ g/mL
Under, the stimulus index of biologically active peptide SRPETSG is more than BSA, illustrates that SRPETSG can stimulate external mouse lymph to a certain extent
The proliferation of cell.And the stimulus index of SRPETSG reached 1.212 and negative control group have significant difference (P<0.05).
Therefore, it can be assumed that active peptides SRPETSG has the ability for remarkably promoting mouse lymphocyte proliferation, one kind can be used as
Health products or additive are edible, can improve the immunity of animal and human body.
Two, the rush macrophage of biologically active polypeptide SRPETSG swallows dimethyl diaminophenazine chloride capacity experimental
1. experiment reagent and instrument：
Reagent：Experimental animal balb/c mouse (male 6-8 week old) Shanghai Communications University's agricultural and biological institute animal reality
Test center；The biologically active polypeptide SRPETSG that embodiment 1 obtains；LPS is purchased from Sigma companies；Neutral red staining solution, the green skies
Biotechnology research institute produces.
Instrument and equipment：LRH-250F biochemical cultivation cases Shanghai perseverance Science and Technology Ltd.；On GL-22M high speed freezing centrifuges
Hai Luxiang instrument centrifuges Instrument Ltd.；150 CO2 incubator Heraeus companies of Hera cell；Dragon Wellscan
MK3 microplate reader Labsystems companies.
2. experimental method：
It is 2 × 10 that number of cells, which is added,6100 holes μ l/ of cell suspension of/ml, adherent be added after purification contain active peptide
200 holes μ l/ of RPMI1640 complete culture solutions (10%FBS) of SRPETSG (1mg/ml) are experimental group, and addition is free of active peptide
What 200 holes μ l/ of RPMI1640 complete culture solutions (10%FBS) were cultivated is set as blank group；And experimental group and blank group exist
LPS to 10 μ g/ml of final concentration is added when cultivating for 24 hours；After continuing culture to 48h, cell culture fluid is abandoned in suction.PBS cleans bottom hole
37 DEG C of 80 holes μ l/ of dimethyl diaminophenazine chloride dye liquor are added afterwards, inhales abandon dye liquor after ten minutes, after being cleaned twice with PBS, 150 μ l are added per hole
Cell pyrolysis liquid (glacial acetic acid：Absolute ethyl alcohol=1:1, v/v).After 4 DEG C of dissolvings overnight, absorbance value is measured at wavelength 540nm
(OD540)。
3. experimental result and analysis：
2 biologically active polypeptide SRPETSG of table promotees the measurement of macrophage phagocytosis dimethyl diaminophenazine chloride ability
| Experiment packet | Inflammation group absorbance value (OD540) |
| Blank group | 0.1072±0.0236 |
| Experimental group | 0.1512±0.0432** |
Note：*, compared with negative control, significant difference (P < 0.05)
*, compared with negative control group, significant difference (P < 0.01)
Experimental result is shown in Table 2, compared with cell blank, the inflammation group of addition 1mg/ml biologically active polypeptides SRPETSG
Macrophage phagocytosis dimethyl diaminophenazine chloride ability obviously increases, and compared with cell blank group, has significant difference (P < 0.01).
It is aobvious to illustrate that biologically active polypeptide SRPETSG has macrophages in vitro phagocytosis dimethyl diaminophenazine chloride ability in the case where there is inflammation generation
The facilitation of work.
The activity of fighting against senium of 3 biologically active peptide of embodiment is tested
One, the experiment that biologically active polypeptide SRPETSG influences caenorhabditis elegan fecundity
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.；The biologically active polypeptide SRPETSG that embodiment 1 obtains.
Instrument and equipment：Power health RO15 pure water systems, Li Kang biologic medicals Science and Technology Ltd.；G136T types Zealway intelligence
High-temperature sterilization pot, Xiamen Zhi Wei instruments Science and Technology Ltd.；THZ-32 type Desk type constant-temperatureoscillator oscillators, Shanghai precision experimental facilities have
Limit company；TDL-40B centrifuges, Anting Scientific Instrument Factory, Shanghai；Lu Xiang instrument GL-22M high speed freezing centrifuges, Shanghai Lu Xiang instrument
Instrument Ltd.；Win fast BJ-CD SERIES Biohazard Safety Equipments, Shanghai Bo Xun Industrial Co., Ltd.s；Nikko is inverted electronic display
Micro mirror, Nikon Corp..
2. experimental method：
(1) prepared by NGM tablets
Take strain Escherichia coli in LB plate streakings, picking single bacterium is fallen in 10ml LB liquid mediums, 37 DEG C,
200rpm, shaken cultivation for 24 hours, until OD600=0.4 for be inoculated with NGM tablets feed nematode.100 μ L bacterium solutions are taken to be applied to 60mm
NGM tablets notice that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM tablets having been coated with are 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 plates, takes 5ml M9 wash buffers 2
It is secondary, buffer solution is sucked in 15ml centrifuge tubes, 1000r/min centrifuges 3min, discards supernatant.5ml is added and newly matches synchronization bleaching
Liquid acutely vibrates 2.5min, adult polypide is corroded at room temperature.Centrifugation, discards supernatant.Ensure total processing time no more than
5min prevents damage worm's ovum.It adds M9 buffer solutions precipitation is resuspended, centrifuges, discard supernatant after mixing, repeat this process 3 times.
2) it prescribes a time limit oviposition method
Several nematodes in the egg-laying season of picking are in same tablet, 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 0.5h being cultivated in tablet,
Choose nematode in tablet, then the ovum in tablet is in same growth period.
(4) index determining
This experiment is using caenorhabditis elegan as animal model, and treated that L4 phase nematodes arrive respective concentration for picking synchronization
In NGM plates.Each concentration at least 8 nematodes, each NGM plates are transferred to one, are denoted as 0 day, move to daily later in new plate until
Nematode reproduction is no longer laid eggs substantially, is counted to the total laying of nematode before it enters the egg-laying season.
3. experimental result and analysis：
Experimental result is as shown in figure 3, compared with the not blank group of feeding polypeptide SRPETSG, feeding different quality concentration
Experimental group in, eggs on average number has different degrees of increase.When a concentration of 300mg/L of the polypeptide SRPETSG of feeding, line
Worm eggs on average number has highly significant difference (P compared with blank group<0.01), and in its a concentration of 400mg/L, 500mg/
When L, significant difference (P is but only presented compared with blank group<0.05), this has also further demonstrated that 300mg/L is that hybrid peptide is more
Peptide SRPETSG acts on optium concentration, and as the raising of peptide concentration can't inhibit nematode reproduction, but its function and effect weakens.
In conclusion polypeptide SRPETSG can be obviously improved the fecundity of nematode under a certain concentration.Meanwhile this experimental results showed that,
Polypeptide SRPETSG300mg/L is optimum concentration.But with the increase of concentration, obviously carrying but no longer occurs in the fecundity of nematode
It is high.
Two, the experiment that biologically active polypeptide SRPETSG influences caenorhabditis elegan body length
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.；The biologically active polypeptide SRPETSG that embodiment 1 obtains.
Instrument and equipment：Power health RO15 pure water systems, Li Kang biologic medicals Science and Technology Ltd.；G136T types Zealway intelligence
High-temperature sterilization pot, Xiamen Zhi Wei instruments Science and Technology Ltd.；THZ-32 type Desk type constant-temperatureoscillator oscillators, Shanghai precision experimental facilities have
Limit company；TDL-40B centrifuges, Anting Scientific Instrument Factory, Shanghai；Lu Xiang instrument GL-22M high speed freezing centrifuges, Shanghai Lu Xiang instrument
Instrument Ltd.；Win fast BJ-CD SERIES Biohazard Safety Equipments, Shanghai Bo Xun Industrial Co., Ltd.s；Nikko is inverted electronic display
Micro mirror, Nikon Corp..
2. experimental method：
(1) prepared by NGM tablets
Take strain Escherichia coli in LB plate streakings, picking single bacterium is fallen in 10ml LB liquid mediums, 37 DEG C,
200rpm, shaken cultivation for 24 hours, until OD600=0.4 for be inoculated with NGM tablets feed nematode.100 μ L bacterium solutions are taken to be applied to 60mm
NGM tablets notice that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM tablets having been coated with are 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 plates, takes 5ml M9 wash buffers 2
It is secondary, buffer solution is sucked in 15ml centrifuge tubes, 1000r/min centrifuges 3min, discards supernatant.5ml is added and newly matches synchronization bleaching
Liquid acutely vibrates 2.5min, adult polypide is corroded at room temperature.Centrifugation, discards supernatant.Ensure total processing time no more than
5min prevents damage worm's ovum.It adds M9 buffer solutions precipitation is resuspended, centrifuges, discard supernatant after mixing, repeat this process 3 times.
2) it prescribes a time limit oviposition method
Several nematodes in the egg-laying season of picking are in same tablet, 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 0.5h being cultivated in tablet,
Choose nematode in tablet, then the ovum in tablet is in same growth period.
(4) index determining
Experiment packet：Blank group and polypeptide group.Difference group nematode, the difference between in the same period lower body is grown, Ke Yi
Reflect the influence that the active material develops nematode growth to a certain extent.The nematode of each group synchronization culture is growing to
When L2 phases (culture 2 days or so), 40 nematodes of picking to respective NGM tablets respectively, continuous 2 days, 3 days, 4 days, 5 days, 6 days, 8
It, observe growth state with inverted microscope within 10 days, measure and record that its body is long, and every group takes its average value.
3. experimental result and analysis：
Under 20 DEG C of condition of culture, since the L2 phases (the 2nd day) of nematode growth from, L3 phases (the 3rd day), L4 phases
It in (the 4th day), the adult stage (the 6th day), is observed continuously 8 days, until the 10th day of nematode growth, measure nematode under each time point
Body is long.Can be seen that each group nematode its body length in the L4 phases in conjunction with Fig. 4 and Fig. 5 is 1000 μm or so, no significant difference.Together
When, from the long change curve of nematode body it can also be seen that, the long change curve of experimental group body also almost with the long change curve of blank group body
It coincides, at nematode L3 phases (the 3rd day), although nematode is averaged, slightly different for body length, does not present statistically aobvious
Write sex differernce.Experiment shows that the concentration of polypeptide SRPETSG can't influence the growth of nematode.Meanwhile it is also seen that nematode in L3
Phase (the 3rd day) is growth stage the most quick to L4 phases (the 4th day).
Three, the Acute oxidative of biologically active polypeptide SRPETSG 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 SRPETSG that example 1 obtains.
Instrument and equipment：Power health RO15 pure water systems, Li Kang biologic medicals Science and Technology Ltd.；G136T types Zealway intelligence
High-temperature sterilization pot, Xiamen Zhi Wei instruments Science and Technology Ltd.；THZ-32 type Desk type constant-temperatureoscillator oscillators, Shanghai precision experimental facilities have
Limit company；TDL-40B centrifuges, Anting Scientific Instrument Factory, Shanghai；Lu Xiang instrument GL-22M high speed freezing centrifuges, Shanghai Lu Xiang instrument
Instrument Ltd.；Win fast BJ-CD SERIES Biohazard Safety Equipments, Shanghai Bo Xun Industrial Co., Ltd.s；Nikko is inverted electronic display
Micro mirror, Nikon Corp..
2. experimental method：
(1) prepared by NGM tablets
Take strain Escherichia coli in LB plate streakings, picking single bacterium is fallen in 10ml LB liquid mediums, 37 DEG C,
200rpm, shaken cultivation for 24 hours, until OD600=0.4 for be inoculated with NGM tablets feed nematode.100 μ L bacterium solutions are taken to be applied to 60mm
NGM tablets notice that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM tablets having been coated with are 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 plates, takes 5ml M9 wash buffers 2
It is secondary, buffer solution is sucked in 15ml centrifuge tubes, 1000r/min centrifuges 3min, discards supernatant.5ml is added and newly matches synchronization bleaching
Liquid acutely vibrates 2.5min, adult polypide is corroded at room temperature.Centrifugation, discards supernatant.Ensure total processing time no more than
5min prevents damage worm's ovum.It adds M9 buffer solutions precipitation is resuspended, centrifuges, discard supernatant after mixing, repeat this process 3 times.
2) it prescribes a time limit oviposition method
Several nematodes in the egg-laying season of picking are in same tablet, 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 0.5h being cultivated in tablet,
Choose nematode in tablet, then the ovum in tablet is in same growth period.
(4) index determining
Experiment packet：Blank group and polypeptide group.By synchronization, treated that L4 phase nematodes are placed in corresponding NGM plates, experiment
In H containing 20mM2O2NGM tablets in carry out, be no less than 10 per plate quantity, count that nematode is dead, viable count per half an hour,
Nematode death criterion：Without mobile and swallowing act, still without any reaction after touching.Rejecting standard：1. fleeing to tablet wall
Or it covers and thirst；2. worm's ovum is hatched in vivo forms bag sample worm：3. piercing in agar.
3. experimental result and analysis：
Influences of the 3 biologically active polypeptide SRPETSG of table to nematode under oxidative stress
As can be seen from Table 3, there is conspicuousness to improve (P < 0.05) for experimental group nematode average life span under oxidative stress,
Extremely significant difference (P is presented in polypeptide SRPETSG groups<0.05).The each group half death time also accordingly has to a certain extent
Extended, hybrid peptide group is presented conspicuousness and improves (P compared with other experimental groups<0.05).As shown in fig. 6, in oxidative stress item
Under part, 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
To significantly improving, it may be possible to since polypeptide SRPETSG can effectively help nematode to resist oxidative damage, remove generate in vivo from
By the accumulation of base and reduction peroxide, rather than by enhancing the realization of its heat hardiness.The extension of organism life-span is in certain journey
It is the resistance due to improving cell to stress conditions on degree, thus slows down aging and deposited with the survival rate under pressure stressed condition
In much relations.This results show polypeptide SRPETSG can significantly increase nematode pressure stress with oxidative stress ability,
The survival rate for improving nematode illustrates that certain density polypeptide SRPETSG has anti-aging function for nematode.
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 embodiment 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 the present invention's
Within protection domain.
Sequence table
<110>Zhejiang Hui Tai life and healths Science and Technology Ltd.；The Shanghai bio tech ltd Bo Hui
<120>A kind of biologically active polypeptide SRPETSG and its preparation method and application
<160> 3
<170> SIPOSequenceListing 1.0
<210> 1
<211> 7
<212> PRT
<213>Artificial sequence (Artificial Sequence)
<400> 1
Ser Arg Pro Glu Thr Ser Gly
1 5
<210> 2
<211> 21
<212> DNA
<213>Artificial sequence (Artificial Sequence)
<400> 2
tagtcgtcca gaaaccagtg g 21
<210> 3
<211> 349
<212> PRT
<213>Artificial sequence (Artificial Sequence)
<400> 3
Met Asn Arg Tyr Lys Asp Ala Gly Val Asp Val Glu Ala Gly Tyr Asp
1 5 10 15
Leu Val Lys Arg Ile Lys Lys Asp Ile Ala Ala Thr Ser Arg Pro Glu
20 25 30
Thr Ser Gly Thr Ile Gly Ser Phe Gly Gly Met Phe Asp Leu Glu Lys
35 40 45
Leu Gly Tyr Gln His Pro Val Leu Val Ser Gly Thr Asp Gly Val Gly
50 55 60
Thr Lys Leu Met Ile Ala Gln Glu Met Gly Ile Asn Asp Thr Ile Gly
65 70 75 80
Ile Asp Cys Val Ala Met Cys Val Asn Asp Val Leu Ala Gln Gly Ala
85 90 95
Glu Pro Leu Phe Phe Leu Asp Tyr Ile Ala Thr Gly His Asn Asp Pro
100 105 110
Ala Lys Leu Ala Gln Val Val His Gly Val Ala Glu Gly Cys Arg Gln
115 120 125
Ser Gly Ser Ala Leu Ile Gly Gly Glu Thr Ala Glu Met Pro Asp Met
130 135 140
Tyr Pro Lys Asn Glu Tyr Asp Leu Ala Gly Phe Ser Thr Gly Ile Ala
145 150 155 160
Asn Lys Glu Asp Ile Leu Thr Gln Asp Leu Ala Lys Glu Gly Asp Ile
165 170 175
Leu Ile Gly Leu Pro Ser Ser Gly Val His Ser Asn Gly Phe Ser Leu
180 185 190
Ile Arg Gln Val Leu Phe Lys Asp His His Leu Lys Val Thr Asp Arg
195 200 205
Pro Glu Ala Leu Glu Gly Lys Ser Ile Gly Glu Ile Leu Leu Thr Pro
210 215 220
Thr Lys Ile Tyr Val Gln Ala Val Leu Ser Leu Val Lys Arg His Leu
225 230 235 240
Leu His Gly Ile Ala His Ile Thr Gly Gly Gly Leu Ile Glu Asn Leu
245 250 255
Pro Arg Thr Tyr Asn Asp Asp Leu Gln Ala Glu Val Asn Leu Gly Ala
260 265 270
Trp Pro Val Gln Ala Ile Phe Arg Tyr Leu Gln Asn Lys Gly Gln Leu
275 280 285
Lys Glu Gln Asp Cys Leu Asn Thr Phe Asn Met Gly Ile Gly Leu Val
290 295 300
Leu Leu Val Pro Lys Ala Asn Val Leu Gln Val Lys Glu Gln Leu Lys
305 310 315 320
Gln Lys Asn Glu Gln Tyr Tyr Glu Ile Gly Lys Leu Arg Lys Arg Pro
325 330 335
Ile Gly Glu Lys Lys Ile Val Phe Asn Gly Ser Phe Lys
340 345
Claims (10)
1. a kind of biologically active polypeptide SRPETSG, which is characterized in that its amino acid sequence is Ser-Arg-Pro-Glu-Thr-
Ser-Gly。
2. a kind of biologically active polypeptide SRPETSG according to claim 1, which is characterized in that the biologically active polypeptide
From Lactobacillus helveticus mycoprotein.
3. encoding the nucleotide fragments of biologically active polypeptide SRPETSG described in claim 1, which is characterized in that the nucleotide
The sequence of segment such as SEQ ID NO：Shown in 2.
4. the preparation method of biologically active polypeptide SRPETSG as described in claim 1, which is characterized in that pass through genetic engineering
Method is artificial synthesized or Lactobacillus helveticus thalline is directly obtained by the method that clasmatosis isolates and purifies, or directly passing through
Be synthetically prepared.
5. the application of biologically active polypeptide SRPETSG as described in claim 1, which is characterized in that the biologically active polypeptide
Applications of the SRPETSG in preparing the food with immunoloregulation function, health products, drug or cosmetics.
6. the application of biologically active polypeptide SRPETSG as described in claim 1, which is characterized in that the biologically active polypeptide
Applications of the SRPETSG in preparing the food with anti-senescence function, health products or drug.
7. the application of biologically active polypeptide SRPETSG as described in claim 1, which is characterized in that the biologically active polypeptide
Applications of the SRPETSG in preparing the food with immunoloregulation function and anti-senescence function, health products or drug.
8. a kind of immunological regulation product, which is characterized in that including biologically active polypeptide SRPETSG as described in claim 1 or institute
State the derivative of biologically active polypeptide SRPETSG；The immunological regulation product includes immunological regulation food, immunological regulation health care
Product, immunoregulation medicament or immunological regulation cosmetics；The derivative of the biologically active polypeptide SRPETSG refers to living in biology
Property polypeptide SRPETSG amino acid side groups on, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonylation, methyl
Change, 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 SRPETSG or described as described in claim 1
The derivative of biologically active polypeptide SRPETSG；The anti-aging product includes antisenility cistanche food, antisenescence health product or anti-ageing
Old drug；The derivative of the biologically active polypeptide SRPETSG refers to the amino acid side chain in biologically active polypeptide SRPETSG
On group, aminoterminal or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate, acetylation, phosphorylation, esterification or glycosyl
Change modification, obtained polypeptide derivative.
10. a kind of product with immunoloregulation function and anti-senescence function, which is characterized in that including as described in claim 1
The derivative of biologically active polypeptide SRPETSG or described biologically active polypeptides SRPETSG；With immunoloregulation function and anti-aging
The product of function includes food, health products or drug；The derivative of the biologically active polypeptide SRPETSG refers to living in biology
Property polypeptide SRPETSG amino acid side groups on, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonylation, methyl
Change, acetylation, phosphorylation, esterification or glycosylation modified, obtained polypeptide derivative.
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| CN201810718874.9A CN108794605B (en) | 2018-06-29 | 2018-06-29 | Bioactive polypeptide SRPETSG, and preparation method and application thereof |
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| CN201810718874.9A CN108794605B (en) | 2018-06-29 | 2018-06-29 | Bioactive polypeptide SRPETSG, and preparation method and application thereof |
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| CN108794605A true CN108794605A (en) | 2018-11-13 |
| CN108794605B CN108794605B (en) | 2021-03-05 |
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Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
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| CN112679598A (en) * | 2021-01-19 | 2021-04-20 | 浙江辉肽生命健康科技有限公司 | Bioactive peptide SGVSLAALKKALAAAGYDVEK, and preparation method and application thereof |
| CN112745379A (en) * | 2021-01-22 | 2021-05-04 | 浙江辉肽生命健康科技有限公司 | Bioactive peptide with amino acid structure RDNKKTRIIPR, and preparation method and application thereof |
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| 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 |
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| WO2009121176A1 (en) * | 2008-03-31 | 2009-10-08 | The University Of British Columbia | Insulin-induced gene (insig) peptide compositions and methods for cytoprotection |
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| CN112679598A (en) * | 2021-01-19 | 2021-04-20 | 浙江辉肽生命健康科技有限公司 | Bioactive peptide SGVSLAALKKALAAAGYDVEK, and preparation method and application thereof |
| CN112745379A (en) * | 2021-01-22 | 2021-05-04 | 浙江辉肽生命健康科技有限公司 | Bioactive peptide with amino acid structure RDNKKTRIIPR, and preparation method and application thereof |
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| CN108794605B (en) | 2021-03-05 |
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