CN107840880A - A kind of biologically active polypeptide GLNYYQQKPVA and its preparation method and application - Google Patents
A kind of biologically active polypeptide GLNYYQQKPVA and its preparation method and application Download PDFInfo
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- CN107840880A CN107840880A CN201711125040.9A CN201711125040A CN107840880A CN 107840880 A CN107840880 A CN 107840880A CN 201711125040 A CN201711125040 A CN 201711125040A CN 107840880 A CN107840880 A CN 107840880A
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- Prior art keywords
- glnyyqqkpva
- biologically active
- active polypeptide
- polypeptide
- inflammatory
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- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical class OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 1
- JLTQXEOXIJMCLZ-ZVZYQTTQSA-N Trp-Gln-Val Chemical compound C1=CC=C2C(C[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C(C)C)C(O)=O)=CNC2=C1 JLTQXEOXIJMCLZ-ZVZYQTTQSA-N 0.000 description 1
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4732—Casein
-
- 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
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Organic Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Mycology (AREA)
- Nutrition Science (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Medicinal Chemistry (AREA)
- Dermatology (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Birds (AREA)
- Epidemiology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
The present invention relates to albumen field, and in particular to its amino acid sequence of a kind of biologically active polypeptide GLNYYQQKPVA and its preparation method and application, biologically active polypeptide GLNYYQQKPVA is Gly Leu Asn Tyr Tyr Gln Gln Lys Pro Val Ala.By extracorporeal anti-inflammatory activity experiment, internal Antisenility Experiment, demonstrating polypeptide GLNYYQQKPVA has preferable anti-inflammatory activity and activity of fighting against senium, on the one hand, the biologically active polypeptide GLNYYQQKPVA of the present invention can promote Factor of Macrophage, promote the increase of the macrophage nitric oxide amount of inducing, the ability that body resists extraneous pathogenic infection is improved, reduces the body incidence of disease；On the other hand, the vigor of internal anti-peroxidation enzyme system can be improved, strengthen the function of body resistance external source sexual stimulus, so as to reduce organism aging process, aging and sick probability, exploitation is of great significance with anti-inflammatory properties, the food of anti-senescence function, health products and medicine tool.
Description
Technical field
The present invention relates to albumen field, more particularly, to a kind of biologically active polypeptide GLNYYQQKPVA and preparation method thereof
And application.
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, protein is changed into 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.In these polypeptides, some has special
Physiological function, it is referred to as " biologically active peptide ".
It is particularly important that safe biologically active peptide is found in natural food source.In the last few years, it has been found that some foods
The polypeptides matter in thing 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 the polypeptide with bioactivity 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 physiologically active is living from breast first after opioid peptides discovery
Property polypeptide.Jolles in 1981 et al. has found first, using trypsin hydrolysis people lactoprotein, can obtain an amino acid sequence
Val-Glu-Pro-Ile-Pro-Tyr hexapeptide is classified as, experiment in vitro proves that the peptide can strengthen 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 phagocytosis and enhancing of the sheep erythrocyte to mouse peritoneal macrophages for kerekou pneumonia primary
The resistance of bacterium, there are anti-inflammatory properties.Li Su duckweeds et al. find that rat abdominal cavity is huge with newborn source peptide (PGPIPN) the feeding rat of synthesis
The anti-inflammatory properties that the phagocytosis of phagocyte is related to red blood cell have significant enhancing.
Research shows that immune-active peptides can not only strengthen immunity of organisms, stimulates the propagation of body lymphocyte, enhancing
The phagocytic function of macrophage, promote the release of cell factor, the increase for promoting the macrophage nitric oxide amount of inducing, raising machine
Body resists the ability of extraneous pathogenic infection, reduces the body incidence of disease, and will not cause the immunological rejection of body.
Aging is a natural phenomena, and process is often accompanied by the change of antioxidant levels, organ-tissue, immune factor, its
The change of complexity, the trend that such as 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 by using some model organisms, as mouse,
The term single gene mutating experiment of drosophila and C. Elegans Automatic Screening etc., it is found that some genes can dramatically increase life-spans of these organisms and reach
As many as 6 times.
Anti-aging peptide in terms of physiological function there is amino acid can not compare excellent as a kind of emerging antidotal agent
Gesture, it can produce promotion or inhibitory action to the enzyme in organism, improve absorption and the profit to mineral matter and other nutrients
With, removing interior free yl, the resistance to oxidation of enhancing body itself, with anti-aging.Therefore, the nutrition and health care of biologically active peptide
Effect has turned into 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 be probably 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.
The research on biologically active polypeptide has much at present, for example Chinese patent CN105254738A discloses one kind and come
The milk-derived biologically active polypeptide DELQDKIH of beta-casein is come from, Chinese patent CN105254739A discloses one kind and derived from
The milk-derived biologically active polypeptide GTQYTD of α s1- caseins, Chinese patent CN105254740A, which are disclosed, a kind of derives from α s2-
The milk-derived biologically active polypeptide NQFYQKF of casein.
The content of the invention
It is an object of the invention to provide a kind of biologically active polypeptide GLNYYQQKPVA and its preparation method and application.
The purpose of the present invention can be achieved through the following technical solutions：
First aspect present invention, there is provided a kind of biologically active polypeptide GLNYYQQKPVA, its amino acid sequence are Gly-Leu-
Asn-Tyr-Tyr-Gln-Gln-Lys-Pro-Val-Ala, such as SEQ ID NO：Shown in 1.
Preferably, the biologically active polypeptide is milk-derived.κ-casein is derive specifically from, and is κ-ss-casein variants
The amino acid residue that A is the 60th~70.κ-ss-casein variants A amino acid sequences such as SEQ ID NO：Shown in 3.
The amino acid sequence of κ-casein and corresponding nucleotides sequence are classified as existing technology, encode κ-ss-casein variants A
The biologically active polypeptide GLNYYQQKPVA of the nucleotide fragments energy encoding mature of 60th~70 amino acids residue.
Preferably, the biologically active polypeptide has anti-inflammatory properties and anti-senescence function.
Second aspect of the present invention, there is provided encode the nucleotide fragments of the biologically active polypeptide GLNYYQQKPVA, its sequence
It is classified as：5 '-gga ctc aat tac tac caa cag aaa cca gtt gca-3 ', such as SEQ ID NO：Shown in 2.
Third aspect present invention, there is provided the preparation method of the biologically active polypeptide GLNYYQQKPVA, base can be passed through
Because the method for engineering is artificial synthesized, can be directly obtained from dairy products by the method isolated and purified, can direct passing through
Learn synthetically prepared.
Fourth aspect present invention, there is provided the biologically active polypeptide GLNYYQQKPVA is being prepared with anti-inflammatory properties
Application in food, health products, medicine or cosmetics.
Fifth aspect present invention, there is provided the biologically active polypeptide GLNYYQQKPVA has anti-senescence function in preparation
Food, the application in health products or medicine.
Sixth aspect present invention, there is provided the biologically active polypeptide GLNYYQQKPVA is being prepared while had anti-inflammatory work(
Can be with the application in the food, health products or medicine of anti-senescence function.
Specifically, biologically active polypeptide GLNYYQQKPVA of the invention, which can be used for preparing, reduces free radical to skin
The cosmetics of injury, prepare the medicine with anti-inflammatory and/or anti-aging；And due to the biologically active polypeptide of the present invention
Product after GLNYYQQKPVA is degraded by intestines and stomach still has bioactivity, therefore can be also used for preparing the food such as Yoghourt
Product, the health products for adjusting immunity, and the oral medicine being used to prepare with anti-inflammatory and/or anti-aging.
Seventh aspect present invention, there is provided a kind of anti-inflammatory products, including the biologically active polypeptide GLNYYQQKPVA or institute
State biologically active polypeptide GLNYYQQKPVA derivative；Described anti-inflammatory products include anti-inflammatory food, anti-inflammatory health product, anti-inflammatory
Medicine or anti-inflammatory cosmetics；The derivative of the biologically active polypeptide GLNYYQQKPVA, refers in biologically active polypeptide
On GLNYYQQKPVA amino acid side groups, aminoterminal or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate,
Acetylation, phosphorylation, esterification or glycosylation etc. are modified, obtained polypeptide derivative.
Eighth aspect present invention, there is provided a kind of anti-aging product, including the biologically active polypeptide GLNYYQQKPVA or
The derivative of the biologically active polypeptide GLNYYQQKPVA；Described anti-aging product includes antisenility cistanche food, anti-ageing healthcare
Product or antiaging agent；The derivative of the biologically active polypeptide GLNYYQQKPVA, refers in biologically active polypeptide
On GLNYYQQKPVA amino acid side groups, aminoterminal or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate,
Acetylation, phosphorylation, esterification or glycosylation etc. are modified, obtained polypeptide derivative.
Ninth aspect present invention, there is provided product a kind of while that there is anti-inflammatory properties and anti-senescence function, including it is described
Biologically active polypeptide GLNYYQQKPVA or described biologically active polypeptides GLNYYQQKPVA derivative；With anti-inflammatory properties and resist
The product of aging function includes food, health products or medicine；The derivative of the biologically active polypeptide GLNYYQQKPVA, refers to
On biologically active polypeptide GLNYYQQKPVA amino acid side groups, aminoterminal or c-terminus carry out hydroxylating, carboxylated,
Be carbonylated, methylate, acetylation, phosphorylation, the modification such as esterification or glycosylation, obtained polypeptide derivative.
Biologically active polypeptide GLNYYQQKPVA's of the present invention has the beneficial effect that：The milk-derived biologically active polypeptide of the present invention
GLNYYQQKPVA has preferable anti-inflammatory activity and activity of fighting against senium；On the one hand, biologically active polypeptide of the invention
GLNYYQQKPVA can promote Factor of Macrophage, promote the increase of the macrophage nitric oxide amount of inducing, and improve
Body resists the ability of extraneous pathogenic infection, reduces the body incidence of disease；On the other hand, it is possible to increase internal anti-peroxidation enzyme system
Vigor, enhancing body resistance external source sexual stimulus function, so as to reduce organism aging process, aging and sick probability, to exploitation
It is of great significance with anti-inflammatory properties, the food of anti-senescence function, health products and medicine tool.
Brief description of the drawings
Fig. 1：Mass chromatography extraction figure (m/z=641.3308)；
Fig. 2：Mass-to-charge ratio is the second order mses figure of 641.3308 fragment；
Fig. 3：Mass-to-charge ratio is 641.3308 polypeptide az, by crack conditions；
Fig. 4：Influence situations of the biologically active polypeptide GLNYYQQKPVA to drosophila survival rate；
Fig. 5：Hydrogen peroxide (H2O2) acute experiment.
Embodiment
Before specific embodiments of the present invention are further described, 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 number range, it should be appreciated that except non-invention is otherwise noted, two ends of each number range
Any one numerical value can be selected between point and two end points.Unless otherwise defined, in the present invention all technologies for using and
Scientific terminology is identical with the meaning that those skilled in the art of the present technique are generally understood that.Except used in embodiment specific method, equipment,
Outside material, according to grasp of the those skilled in the art to prior art and the record of the present invention, it 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 indicated, disclosed in this invention experimental method, detection method, preparation method using this technology lead
Domain conventional molecular biology, biochemistry, chromatin Structure and analysis, analytical chemistry, cell culture, recombinant DNA technology and
The routine techniques of association area.These technologies existing perfect explanation in the prior art, 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 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.
The active peptide GLNYYQQKPVA's of embodiment 1 is artificial synthesized
First, the synthesis of biologically active peptide
1. RINK resin 3g (substitution value 0.3mmol/g) are weighed in 150ml reactor, with 50ml dichloromethane
(DCM) soak.
After 2.2 hours, resin is washed with nitrogen-dimethylformamide (DMF) of 3 times of resin volumes, is then drained, so weight
It is multiple four times, resin is drained rear stand-by.
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.Washed four times with the DMF of 3 times of resin volumes after having taken off protection,
Then drain.
4. take 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. weigh amino acid Gly in right amount and 1- hydroxyls-benzene a pair of horses going side by side triazole (HOBT) is in right amount in 50ml centrifuge tube, addition
20ml DMF is dissolved, and then adds 3ml N, and N DICs (DIC) vibration shakes up 1min, treats that solution is clear
It is added to after clear in reactor, then reactor is placed in 30 DEG C of shaking table and 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
Washed four times, drained stand-by 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.Washed four times with DMF after having taken off protection, then drained.
8. take 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 50ml centrifuge tube, 25ml DMF generals are added
It dissolves, and the DIC vibrations for then adding 2.5ml shake up 1min, are added to after solution clarification in reactor, then by reactor
It is placed in 30 DEG C of shaking table and reacts.
After 10.1 hours, take a small amount of resin to detect, (each two drop of inspection A, inspection B, 100 DEG C of reactions are detected with ninhydrin method
1min), if resin is colourless, illustrate that reaction is complete；If resin has color, illustrate that condensation is incomplete, continue to react.
After 11. question response is complete, washs resin four times with DMF, then drain, 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 protection groups on resin is sloughed with this
Group.Washed four times with DMF after having taken off protection, then drain whether detection protection sloughs.
12. according to step 9-11 connect successively amino acid Leu, Asn, Tyr, Tyr, Gln, Gln, Lys, Pro, Val and
Ala。
13. after last amino acid is connected, 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
Cut down from resin (every gram of resin adds 10ml cutting liquids), and with ice ether (cutting liquid：Ether=1:9,v:V) centrifugation is heavy
Drop four times.
So far, artificial synthesized biologically active peptide GLNYYQQKPVA.
2nd, the confirmation of biologically active peptide
1) UPLC is analyzed
UPLC conditions are as follows：
Instrument：Waters ACQUITY UPLC ultra high efficiency liquid phase-electron spray-level Four bar-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 above analysis method, using ultra high efficiency liquid phase-electron spray-level Four bar-flight time mass spectrum, to bioactivity
Peptide GLNYYQQKPVA carries out chromatography and mass spectral analysis, and its mass chromatography extraction figure is as shown in figure 1, extract the two level at this peak
As shown in Figures 2 and 3, the polypeptide mass-to-charge ratio that can obtain this peak is 641.3308Da, and retention time is for mass spectrogram and az, by crack conditions
24.8min。
3) result
From the figure 3, it may be seen that situation about being broken according to az, by, calculates by Mascot software analysis, obtains mass-to-charge ratio
641.3308Da fragment sequence be Gly-Leu-Asn-Tyr-Tyr-Gln-Gln-Lys-Pro-Val-Ala
(GLNYYQQKPVA) SEQ ID NO, are designated as：1.The fragment is relative with κ-ss-casein variants A the 60th~70 residue sequence
Should, the GenBank numberings of κ-casamino acid sequence are AAA30433.1, and sequence is shown in SEQ ID NO：3.
The anti-inflammatory activity experiment of the biologically active peptide of embodiment 2
First, the experiment (ELISA method) of biologically active polypeptide GLNYYQQKPVA rush Factor of Macrophage
1. experiment reagent and instrument：
Reagent：Experimental animal balb/c mouse (male 6-8 week old), Shanghai Slac Experimental Animal Co., Ltd.；Mouse
Lymphocyte extract solution, Shanghai Suo Laibao bio tech ltd；RPMI1640 culture mediums, GIBCO companies；Bovine serum albumin
(bovine serum albumin, BSA) in vain, Genebase companies；The milk-derived biologically active polypeptide that embodiment 1 obtains
GLNYYQQKPVA；ELISA cell factors Quick kit (TNF-α, IL-1 β and IL-6), Wuhan doctor's moral bioengineering is limited
Company.
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.；Hera cell 150CO2 incubator Heraeus companies；Dragon Wellscan
MK3 ELIASA Labsystems companies.
2. experimental method：
It is 2 × 10 to add number of cells6/ ml μ l/ the holes of cell suspension 100, it is adherent to add after purification containing peptide
The μ l/ holes of RPMI1640 complete culture solutions (10%FBS) 200, inflammation group added LPS to the μ g/ml of final concentration 10 at 24 hours, even
Continuous culture 48 hours, inflammation group add LPS to final concentration 100ng/ml in 24 hours before culture terminates.After culture terminates, centrifugation
Collect cell culture supernatant liquid.100 μ l supernatants, 37 DEG C of reactions 90 are added in the ELISA Plate of coated cell factor antibody
After minute, biotin labelled antibodies are added, 37 DEG C are reacted 60 minutes, and after PBS washings, it is compound to add Avidin-peroxidase
Thing, react 30 minutes.Nitrite ion is added after PBS washings, is reacted 20 minutes.After adding colour developing terminate liquid, using ELIASA in ripple
Absorbance (OD450) is determined under long 450nm.
3. experimental result and analysis：
The measure that the biologically active peptide GLNYYQQKPVA of table 1 influences on Macrophage Cell factor level
Note：*, compared with negative control, there is significant difference (P ＜ 0.05)；*, compared with negative control group, have significantly
Sex differernce (P ＜ 0.01)
As can be known from Table 1, TNF-α, IL-1 β and IL-6 these three cell factors experimental result in, TNF-α, IL-1 β
In 0.2mg/ml and significant difference (P ＜ 0.01) is appeared above, IL-6 significant difference (P ＜ occurs in 0.5mg/ml
0.01), it was demonstrated that the GLNYYQQKPVA under finite concentration can promote Turnover of Mouse Peritoneal Macrophages to activate and discharge TNF-α, IL-1
β, IL-6, floors of these cell factors under normal macrophages quiescent condition is improved, so as to adjust the immunity of body.
2nd, the measure (Griess methods) of the biologically active polypeptide GLNYYQQKPVA rush macrophage nitric oxide amount of inducing
1. experiment reagent and instrument：
Reagent：Experimental animal balb/c mouse (male 6-8 week old) Shanghai Communications University is agriculture real with biological institute animal
Test center；The milk-derived biologically active polypeptide GLNYYQQKPVA that embodiment 1 obtains；LPS, purchased from Sigma companies；Dimethyl diaminophenazine chloride contaminates
Color liquid, green skies biotechnology research institute production.
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.；Hera cell 150CO2 incubator Heraeus companies；Dragon Wellscan
MK3 ELIASA Labsystems companies.
2. test method：
It is 2 × 10 to add number of cells6/ ml μ l/ the holes of cell suspension 100, it is adherent to add after purification containing peptide
The μ l/ holes of RPMI1640 complete culture solutions (10%FBS) 200, inflammation group add LPS to the μ g/ml of final concentration 10 in 24h, continuously
After cultivating 48h, the μ l/ holes of nutrient solution supernatant 50 are collected, add Griess reagents 1 and Griess reagents successively in nutrient solution supernatant
2 each 50 μ l/ holes, after reacting at room temperature 10 minutes, absorbance (OD540) is determined under 540nm wavelength.
3. experimental result and analysis：
The biologically active polypeptide GLNYYQQKPVA of table 2 promotees the measure of the macrophage nitric oxide amount of inducing
Note：*, compared with negative control, there is significant difference (P ＜ 0.05)；
*, compared with negative control group, there is significant difference (P ＜ 0.01)
Experimental result is shown in Table 2, as shown in Table 2, biologically active polypeptide GLNYYQQKPVA, concentration point is added in experimental group
Not Wei 1mg/mL and 0.5mg/mL, make with LPS the promotion macrophage grown under inflammatory conditions for growing under normal circumstances
The nitric oxide amount of inducing has facilitation.Compared with cell blank group, there is significant difference (P<0.05).Work as bioactivity
Polypeptide GLNYYQQKPVA addition concentration is 0.1mg/mL, is compared in the case where LPS makes inflammatory conditions, can also promote macrophage one
The increase of the nitrogen oxide amount of inducing, and there is significant difference (P<0.05).But the cell blank group with growing under normal circumstances
Compare, without significant difference.Illustrating that biologically active polypeptide GLNYYQQKPVA has under the conditions of finite concentration promotes macrophage thin
The increased ability of born of the same parents' nitric oxide amount of inducing.
The activity of fighting against senium experiment of the biologically active peptide of embodiment 3
First, biologically active polypeptide GLNYYQQKPVA improves the experiment of drosophila survival ability
1. experiment reagent and instrument：
Reagent：Oregon K wild type Drosophila melanogasters, agricultural college of Shanghai Communications University genetics experiments room；Agar powder, state
Chemical reagent Co., Ltd of medicine group；The milk-derived biologically active polypeptide GLNYYQQKPVA that embodiment 1 obtains.
Instrument and equipment：The ultra-clean water of CM-230 types mole, Shanghai Moller scientific instrument Co., Ltd；G136T type Zealway intelligence
Energy high-temperature sterilization pot, Xiamen Zhi Wei instruments Science and Technology Ltd.；BJ-CD SERIES bio-incubators, Shanghai is rich to prove to be true after interrogation industry public affairs
Department；GRX-9073 type hot air sterilizers, one permanent Science and Technology Ltd. of Shanghai.
2. experimental method：
Using drosophila as experimental model：The drosophila adult newly to sprout wings in 8 hours is collected, male and female random transferring is divided after anesthesia to respectively
In experimental group, every group of each sex 100, every group of setting 3 is parallel, and control group gives conventional corn powder culture medium, experimental group
GLNYYQQKPVA biologically active peptides-corn culture medium respectively containing 0.05mg/ml, 0.5mg/ml, 1mg/ml.Every 2 days more
Change fresh culture once, observe daily and record the death toll of different sexes drosophila, untill drosophila is all dead.Draw
Drosophila survival curve, and calculate the average life span of different sexes drosophila and maximum life span (takes 5 drosophilas of last death to carry out
Statistics).
3. experimental result and analysis：
This experiment is as follows to the result of study of the life span of drosophila melanogaster of feeding various concentrations biologically active peptide：Can be with from Fig. 4 (A)
It was found that for blank control group Male Drosophila, feeding concentration is that 0.05mg/ml GLNYYQQKPVA is not notable
Change the survival rate of Male Drosophila, and when peptide concentration reaches 0.5mg/ml and 1mg/ml, same time point, Male Drosophila is deposited
Motility rate is significantly improved.From Fig. 4 (B), relative to blank control group female Drosophila, feeding concentration is 0.5mg/ml and 1mg/
During ml, in same time point, the survival rate of female Drosophila increases, but result difference unobvious.
Influence situations of the table 3-1 GLNYYQQKPVA to the Male Drosophila life-span
Note：* sign has significant difference (P compared with blank control group<0.05)；Similarly hereinafter.
Influence situations of the table 3-2 GLNYYQQKPVA to the female Drosophila life-span
It was found from from table 3-1, relative to blank control group, low dose group Male Drosophila average life span does not have significant change,
But middle dose group and advanced amount group Male Drosophila average life span are improved, respectively 16.84% and 9.69%, but only middle dosage
Group generates significant difference (p<0.05), illustrate that the average life span conspicuousness of middle dose group Male Drosophila improves.Meanwhile middle dose
The half death time of amount group and high dose group drosophila is improved, but does not have notable difference in terms of MaLS.By table
3-2 understands that female Drosophila low dose group, middle dose group and high dose group increase in terms of average life span, but do not produce
Raw significant difference.But the MaLS of middle dose group and high dose group increases, extend 7 days respectively compared with blank control group
With 6 days, and generate significant difference (P<0.05).
This experimental result illustrates that biologically active polypeptide GLNYYQQKPVA can improve being averaged for drosophila under finite concentration
Life-span and MaLS, but it is relevant with concentration and sex.This phenomenon related to tested material concentration, strain be probably because
GLNYYQQKPVA participates in the part biological metabolism of drosophila, or the antioxidant system organized by improving drosophila is prolonged to reach
The effect of long life span of drosophila melanogaster.Because the metabolism of different lines drosophila can have any different, so as to cause the difference of result.And the difference of sex
It is different, it may be possible to because female Drosophila inherently has certain conservative and the resistance to external environment, so
GLNYYQQKPVA is to female Drosophila life and unobvious.
2nd, biologically active polypeptide GLNYYQQKPVA hydrogen peroxide Acute oxidative is tested
1. experiment reagent and instrument：
Reagent：Oregon K wild type Drosophila melanogasters, agricultural college of Shanghai Communications University genetics experiments room；Agar powder, state
Chemical reagent Co., Ltd of medicine group；Hydrogen peroxide, Shanghai Ling Feng chemical reagent Co., Ltd；The milk-derived that embodiment 1 obtains
Biologically active polypeptide GLNYYQQKPVA.
Instrument and equipment：The ultra-clean water of CM-230 types mole, Shanghai Moller scientific instrument Co., Ltd；Mi Libo Millipore
MILLEX GP0.22 μm filter membranes, Millipore Corp. of the U.S.；GL-22M high speed freezing centrifuges, Shanghai Lu Xiang instrument centrifuge instruments
Co., Ltd.
2. experimental method：
The drosophila adult newly to sprout wings in 8 hours is collected, male and female random transferring is divided after anesthesia into each experimental group, takes the life-span real
The preferable peptide concentration culture medium of middle result is tested, sets blank control group and experimental group, control group to give conventional corn powder culture medium.
Every group of male and female sex drosophila is 50, and drosophila is cultivated three weeks.Then 5 males and 5 female Drosophilas are taken to be transferred to every time
Contain a papery disk in one new container, in new container, disk contain 300 μ L concentration for 5% sucrose solution with
And concentration is 30% hydrogen peroxide 1ml, blank group and experimental group are exposed to toxicity peroxide caused by this hydrogen peroxide
In environment, 10 Duplicate Samples of every group of setting, its oxidation resistance is observed.Every 4 hour record drosophila The dead quantity and sex, until
Drosophila is all dead.
3. experimental result and analysis：
It is male in Each point in time after GLNYYQQKPVA feedings from Fig. 5 (A) as can be seen that for Male Drosophila
The survival rate of property drosophila is above the drosophila without GLNYYQQKPVA feedings, and the time-to-live increases compared with blank control group,
After illustrating feeding GLNYYQQKPVA, Male Drosophila oxidation resistance increases.In Fig. 5 (B), feeding GLNYYQQKPVA's is female
Property drosophila, survival rate is obvious high and control group in 15h in the hydrogen peroxide environment of high concentration, illustrates female Drosophila this period
Oxidation resistance increases.But later experiments group and control group survival curve essentially coincide, and illustrate feeding GLNYYQQKPVA's
The oxidation resistance of female Drosophila gradually weakens, and does not have difference with control group after certain time.This test result indicates that,
GLNYYQQKPVA can improve the oxidation resistance of drosophila.According to H2O2Acute toxicity testing result, it can speculate
GLNYYQQKPVA may improve drosophila to H by adjusting cat catalase activity2O2The resistivity of damage.
3rd, the experiment that biologically active polypeptide GLNYYQQKPVA influences on drosophila SOD and MAD content
1. experiment reagent and instrument：
Reagent：Oregon K wild type Drosophila melanogasters, agricultural college of Shanghai Communications University genetics experiments room；Agar powder, state
Chemical reagent Co., Ltd of medicine group；MDA MDA kits, Science and Technology Ltd. of Nanjing Keygen Biotech；SOD super oxygens
Compound is disproportionated enzyme reagent kit, and bio tech ltd is built up in Nanjing；The milk-derived biologically active polypeptide that embodiment 1 obtains
GLNYYQQKPVA。
Instrument and equipment：The ultra-clean water of CM-230 types mole, Shanghai Moller scientific instrument Co., Ltd；Organize homogenizer, Shanghai
Member is as bio tech ltd；G136T type Zealway intelligence high-temperature sterilization pots, Xiamen Zhi Wei instruments Science and Technology Ltd.；
BJ-CD SERIES bio-incubators, Shanghai Bo Xun industrial corporations；GRX-9073 type hot air sterilizers, one permanent science and technology of Shanghai have
Limit company；Infinite type ELIASAs, Austrian Di Ken Co., Ltds.
2. experimental method：
The drosophila adult newly to sprout wings in 8 hours is collected, male and female random transferring is divided after anesthesia into each experimental group, every group each
Sex 100, every group of setting 3 is parallel, and control group gives conventional corn powder culture medium, and experimental group is respectively to contain 0.05mg/
Ml, 0.5mg/ml, 1mg/ml GLNYYQQKPVA biologically active peptides-corn culture medium.Change fresh culture once within every 2 days,
After raising 30 days, every group weighs drosophila 40mg, adds 0.5ml physiological saline, and homogenate is ground in ice bath, the interval 10s seconds, is entered repeatedly
Row 3 times, is made homogenate, and every group of drosophila SOD activity and MDA levels are determined according to kit explanation.Utilize MDA detection reagents
The levels of lipid peroxidation product MDA in box detection drosophila body, the wavelength of spectrophotometer is 532nm.
3. experimental result and analysis：
Influences of the GLNYYQQKPVA of table 4 to drosophila SOD, MDA
As can be known from Table 4, relative to blank control group, the SOD contents in the female male drosophila body of polypeptide treatment group are improved,
And for Male Drosophila group, when peptide concentration reaches 1mg/ml, there is significant difference in the SOD contents in drosophila body, and
Then there is significant difference when peptide concentration is 0.5mg/ml and 1mg/ml in female Drosophila group.Illustrate by taking in certain polypeptide,
Internal SOD contents can be improved, and help body protective itself to prevent oxidative damage.MDA contents can see from table 4,
MDA contents in experimental group Male Drosophila and female Drosophila body have reduction.Relative to male blank control group MDA contents 1.37
± 0.21 μm of ol/L, there is the reduction of conspicuousness for the MDA contents of 0.5mg/ml and 1mg/ml drosophila groups in concentration, and female Drosophila
In group, when 1mg/ml peptides are handled, there is the reduction of conspicuousness in the MDA contents in drosophila body.Because MDA is body lipid peroxide
Change and generate, the reduction of its content illustrates that the Antioxidant Enzymes vigor of drosophila is improved indirectly, so as to protect body
Histoorgan will not produce a large amount of MDAs.
From experimental result as can be seen that SOD and MDA experimental result is mutually proved, it may be said that gelatine/biological activity polypeptide
GLNYYQQKPVA is favorably improved the vigor of the Antioxidant Enzymes in body body, so as to effectively improve the anti-oxidant energy of body
Power, reduce body is stimulated by the bad factor, so as to reduce organism aging process, aging and sick probability, all in all, for male
The effect of drosophila is better than female Drosophila.
By above example as can be seen that biologically active polypeptide GLNYYQQKPVA has anti-inflammatory properties and anti-aging work(
Energy.
The above-mentioned description to embodiment is understood that for ease of those skilled in the art and using invention.
Person skilled in the art obviously can easily make various modifications to these embodiments, and described herein general
Principle is applied in other embodiment without by performing creative labour.Therefore, the invention is not restricted to above-described embodiment, ability
Field technique personnel do not depart from improvement that scope made and modification all should be the present invention's according to the announcement of the present invention
Within protection domain.
Sequence table
<110>Shanghai Communications University；Zhejiang Hui Tai life and healths Science and Technology Ltd.
<120>A kind of biologically active polypeptide GLNYYQQKPVA and its preparation method and application
<160> 3
<170> SIPOSequenceListing 1.0
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<213>Artificial sequence (Artificial Sequence)
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Gly Leu Asn Tyr Tyr Gln Gln Lys Pro Val Ala
1 5 10
<210> 2
<211> 33
<212> DNA
<213>Artificial sequence (Artificial Sequence)
<400> 2
ggactcaatt actaccaaca gaaaccagtt gca 33
<210> 3
<211> 190
<212> PRT
<213>Artificial sequence (Artificial Sequence)
<400> 3
Met Met Lys Ser Phe Phe Leu Val Val Thr Ile Leu Ala Leu Thr Leu
1 5 10 15
Pro Phe Leu Gly Ala Gln Glu Gln Asn Gln Glu Gln Pro Ile Arg Cys
20 25 30
Glu Lys Asp Glu Arg Phe Phe Ser Asp Lys Ile Ala Lys Tyr Ile Pro
35 40 45
Ile Gln Tyr Val Leu Ser Arg Tyr Pro Ser Tyr Gly Leu Asn Tyr Tyr
50 55 60
Gln Gln Lys Pro Val Ala Leu Ile Asn Asn Gln Phe Leu Pro Tyr Pro
65 70 75 80
Tyr Tyr Ala Lys Pro Ala Ala Val Arg Ser Pro Ala Gln Ile Leu Gln
85 90 95
Trp Gln Val Leu Ser Asn Thr Val Pro Ala Lys Ser Cys Gln Ala Gln
100 105 110
Pro Thr Thr Met Ala Arg His Pro His Pro His Leu Ser Phe Met Ala
115 120 125
Ile Pro Pro Lys Lys Asn Gln Asp Lys Thr Glu Ile Pro Thr Ile Asn
130 135 140
Thr Ile Ala Ser Gly Glu Pro Thr Ser Thr Pro Thr Thr Glu Ala Val
145 150 155 160
Glu Ser Thr Val Ala Thr Leu Glu Asp Ser Pro Glu Val Ile Glu Ser
165 170 175
Pro Pro Glu Ile Asn Thr Val Gln Val Thr Ser Thr Ala Val
180 185 190
Claims (10)
1. a kind of biologically active polypeptide GLNYYQQKPVA, it is characterised in that its amino acid sequence is Gly-Leu-Asn-Tyr-
Tyr-Gln-Gln-Lys-Pro-Val-Ala。
A kind of 2. biologically active polypeptide GLNYYQQKPVA according to claim 1, it is characterised in that the bioactivity
Polypeptide is milk-derived.
3. encode the nucleotide fragments of biologically active polypeptide GLNYYQQKPVA described in claim 1, it is characterised in that the core
The sequence of acid fragments such as SEQ ID NO：Shown in 2.
4. biologically active polypeptide GLNYYQQKPVA as claimed in claim 1 preparation method, it is characterised in that pass through gene work
The method of journey is artificial synthesized, or is directly obtained from dairy products by the method isolated and purified, or directly by chemical synthesis system
It is standby.
5. biologically active polypeptide GLNYYQQKPVA as claimed in claim 1 application, it is characterised in that the bioactivity is more
Applications of the peptide GLNYYQQKPVA in the food with anti-inflammatory properties, health products, medicine or cosmetics are prepared.
6. biologically active polypeptide GLNYYQQKPVA as claimed in claim 1 application, it is characterised in that the bioactivity is more
Applications of the peptide GLNYYQQKPVA in the food with anti-senescence function, health products or medicine is prepared.
7. biologically active polypeptide GLNYYQQKPVA as claimed in claim 1 application, it is characterised in that the bioactivity is more
Applications of the peptide GLNYYQQKPVA in the food with anti-inflammatory properties and anti-senescence function, health products or medicine is prepared.
8. a kind of anti-inflammatory products, it is characterised in that including biologically active polypeptide GLNYYQQKPVA as claimed in claim 1 or institute
State biologically active polypeptide GLNYYQQKPVA derivative；Described anti-inflammatory products include anti-inflammatory food, anti-inflammatory health product, anti-inflammatory
Medicine or anti-inflammatory cosmetics；The derivative of the biologically active polypeptide GLNYYQQKPVA, refers in biologically active polypeptide
On GLNYYQQKPVA amino acid side groups, aminoterminal or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate,
Acetylation, phosphorylation, esterification or glycosylation modified, obtained polypeptide derivative.
A kind of 9. anti-aging product, it is characterised in that including biologically active polypeptide GLNYYQQKPVA as claimed in claim 1 or
The derivative of the biologically active polypeptide GLNYYQQKPVA；Described anti-aging product includes antisenility cistanche food, anti-ageing healthcare
Product or antiaging agent；The derivative of the biologically active polypeptide GLNYYQQKPVA, refers in biologically active polypeptide
On GLNYYQQKPVA amino acid side groups, aminoterminal or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate,
Acetylation, phosphorylation, esterification or glycosylation modified, obtained polypeptide derivative.
10. a kind of product with anti-inflammatory properties and anti-senescence function, it is characterised in that including biology as claimed in claim 1
Active peptides GLNYYQQKPVA or described biologically active polypeptides GLNYYQQKPVA derivative；With anti-inflammatory properties and anti-aging
The product of function includes food, health products or medicine；The derivative of the biologically active polypeptide GLNYYQQKPVA, refers in life
On thing active peptides GLNYYQQKPVA amino acid side groups, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonyl
Change, methylate, acetylation, phosphorylation, esterification or glycosylation modified, obtained polypeptide derivative.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201711125040.9A CN107840880A (en) | 2017-11-14 | 2017-11-14 | A kind of biologically active polypeptide GLNYYQQKPVA and its preparation method and application |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201711125040.9A CN107840880A (en) | 2017-11-14 | 2017-11-14 | A kind of biologically active polypeptide GLNYYQQKPVA and its preparation method and application |
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| Publication Number | Publication Date |
|---|---|
| CN107840880A true CN107840880A (en) | 2018-03-27 |
Family
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| CN201711125040.9A Withdrawn CN107840880A (en) | 2017-11-14 | 2017-11-14 | A kind of biologically active polypeptide GLNYYQQKPVA and its preparation method and application |
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| CN (1) | CN107840880A (en) |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN110938130A (en) * | 2019-11-08 | 2020-03-31 | 上海交通大学 | Bioactive polypeptide RVFQPLPHENKPLTL, and preparation method and application thereof |
| CN110938131A (en) * | 2019-11-08 | 2020-03-31 | 上海交通大学 | Bioactive polypeptide RDLDAPDDVDFF, and preparation method and application thereof |
| CN111100196A (en) * | 2019-11-08 | 2020-05-05 | 上海交通大学 | Bioactive polypeptide QILSVPGWTYSR, and preparation method and application thereof |
| CN112724238A (en) * | 2021-01-21 | 2021-04-30 | 浙江辉肽生命健康科技有限公司 | Bioactive peptide with amino acid structure FREGTTPKPK, and preparation method and application thereof |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107011429A (en) * | 2017-05-24 | 2017-08-04 | 浙江辉肽生命健康科技有限公司 | A kind of biologically active peptide Gly Leu Pro Asn and its preparation and application |
| CN107163129A (en) * | 2014-12-19 | 2017-09-15 | 浙江辉肽生命健康科技有限公司 | The preparation and application of κ casein derived biologically active peptides |
| CN107177000A (en) * | 2017-07-06 | 2017-09-19 | 浙江辉肽生命健康科技有限公司 | A kind of biologically active polypeptide DRAAHVKQVL and its preparation method and application |
-
2017
- 2017-11-14 CN CN201711125040.9A patent/CN107840880A/en not_active Withdrawn
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107163129A (en) * | 2014-12-19 | 2017-09-15 | 浙江辉肽生命健康科技有限公司 | The preparation and application of κ casein derived biologically active peptides |
| CN107163128A (en) * | 2014-12-19 | 2017-09-15 | 浙江辉肽生命健康科技有限公司 | The preparation and application of κ casein derived biologically active peptides |
| CN107011429A (en) * | 2017-05-24 | 2017-08-04 | 浙江辉肽生命健康科技有限公司 | A kind of biologically active peptide Gly Leu Pro Asn and its preparation and application |
| CN107177000A (en) * | 2017-07-06 | 2017-09-19 | 浙江辉肽生命健康科技有限公司 | A kind of biologically active polypeptide DRAAHVKQVL and its preparation method and application |
Non-Patent Citations (3)
| Title |
|---|
| YAN JIN等: "Peptide profiling and the bioactivity character of yogurt in the simulated gastrointestinal digestion", 《JOURNAL OF PROTEOMICS》 * |
| 高扬等: "乳源性小肽QEPV的抗衰老功能研究", 《中国乳品工业》 * |
| 龚娅莉: "保加利亚乳杆菌水解酪蛋白条件及产物研究", 《中国优秀硕士学位论文全文数据库工程科技I辑》 * |
Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN110938130A (en) * | 2019-11-08 | 2020-03-31 | 上海交通大学 | Bioactive polypeptide RVFQPLPHENKPLTL, and preparation method and application thereof |
| CN110938131A (en) * | 2019-11-08 | 2020-03-31 | 上海交通大学 | Bioactive polypeptide RDLDAPDDVDFF, and preparation method and application thereof |
| CN111100196A (en) * | 2019-11-08 | 2020-05-05 | 上海交通大学 | Bioactive polypeptide QILSVPGWTYSR, and preparation method and application thereof |
| CN110938130B (en) * | 2019-11-08 | 2021-07-09 | 上海交通大学 | Bioactive polypeptide RVFQPLPHENKPLTL, and preparation method and application thereof |
| CN110938131B (en) * | 2019-11-08 | 2021-07-09 | 上海交通大学 | Bioactive polypeptide RDLDAPDDVDFF, 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 |
| CN112724238A (en) * | 2021-01-21 | 2021-04-30 | 浙江辉肽生命健康科技有限公司 | Bioactive peptide with amino acid structure FREGTTPKPK, and preparation method and application thereof |
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