CN107840878A - A kind of biologically active polypeptide NNQFLPYPYYAKPA and its preparation method and application - Google Patents
A kind of biologically active polypeptide NNQFLPYPYYAKPA and its preparation method and application Download PDFInfo
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- CN107840878A CN107840878A CN201711122902.2A CN201711122902A CN107840878A CN 107840878 A CN107840878 A CN 107840878A CN 201711122902 A CN201711122902 A CN 201711122902A CN 107840878 A CN107840878 A CN 107840878A
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- nnqflpypyyakpa
- biologically active
- active polypeptide
- polypeptide
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—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
- 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
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Toxicology (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Biophysics (AREA)
- Mycology (AREA)
- Nutrition Science (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The present invention relates to albumen field, more particularly to a kind of biologically active polypeptide NNQFLPYPYYAKPA and its preparation method and application, its amino acid sequence of biologically active polypeptide NNQFLPYPYYAKPA is Asn Asn Gln Phe Leu Pro Tyr Pro Tyr Tyr Ala Lys Pro Ala.By the experiment of ion vitro immunization function point analysis, internal Antisenility Experiment, demonstrating polypeptide NNQFLPYPYYAKPA has preferable immunoloregulation function and activity of fighting against senium, on the one hand, the biologically active polypeptide NNQFLPYPYYAKPA of the present invention can strengthen the in-vitro multiplication ability of lymphocyte and macrophage, 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 immunoloregulation function, 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 NNQFLPYPYYAKPA and its preparation side
Method 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.Li Su duckweeds et al. find rat peritoneal macrophages with newborn source immunomodulatory peptides (PGPIPN) the feeding rat of synthesis
The phagocytosis immunoloregulation function 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, improve the ability that body resists extraneous pathogenic infection, reduce machine
The body incidence of disease, and the immunological rejection of body will not be caused.
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 NNQFLPYPYYAKPA 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 NNQFLPYPYYAKPA, its amino acid sequence are Asn-
Asn-Gln-Phe-Leu-Pro-Tyr-Pro-Tyr-Tyr-Ala-Lys-Pro-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 73rd~86.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 NNQFLPYPYYAKPA of the nucleotide fragments energy encoding mature of 73rd~86 amino acids residue.
Preferably, the biologically active polypeptide has immunoloregulation function and anti-senescence function.
Second aspect of the present invention, there is provided the nucleotide fragments of the biologically active polypeptide NNQFLPYPYYAKPA are encoded,
Its sequence is：5 '-aat aat caa ttt ctg cca tac cca tat tat gca aag cca gct-3 ', such as SEQ
ID NO：Shown in 2.
Third aspect present invention, there is provided the preparation method of the biologically active polypeptide NNQFLPYPYYAKPA, Ke Yitong
The method for crossing genetic engineering is artificial synthesized, can be directly obtained, can directly led to by the method isolated and purified from dairy products
Cross chemical synthesis preparation.
Fourth aspect present invention, there is provided the biologically active polypeptide NNQFLPYPYYAKPA has immunological regulation in preparation
Application in the food of function, health products, medicine or cosmetics.
Fifth aspect present invention, there is provided the biologically active polypeptide NNQFLPYPYYAKPA has anti-aging work(in preparation
Can food, the application in health products or medicine.
Sixth aspect present invention, there is provided the biologically active polypeptide NNQFLPYPYYAKPA is being prepared while had immune
Application in the food of regulatory function and anti-senescence function, health products or medicine.
Specifically, biologically active polypeptide NNQFLPYPYYAKPA of the invention, which can be used for preparing, reduces free radical to skin
The cosmetics of skin injury, prepare the medicine with immunological regulation and/or anti-aging；And due to the biologically active polypeptide of the present invention
Product after NNQFLPYPYYAKPA is degraded by intestines and stomach still has bioactivity, therefore can be also used for preparing Yoghourt etc.
Food, the health products for adjusting immunity, and the oral medicine being used to prepare with immunological regulation and/or anti-aging.
Seventh aspect present invention, there is provided a kind of immunological regulation product, including the biologically active polypeptide
NNQFLPYPYYAKPA or described biologically active polypeptides NNQFLPYPYYAKPA derivative；Described immunological regulation product includes
Immunological regulation food, immunological regulation health products, immunoregulation medicament or immunological regulation cosmetics；The biologically active polypeptide
NNQFLPYPYYAKPA derivative, refer on biologically active polypeptide NNQFLPYPYYAKPA amino acid side groups, ammonia
Cardinal extremity or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate, acetylation, phosphorylation, the modification such as esterification or glycosylation,
Obtained polypeptide derivative.
Eighth aspect present invention, there is provided a kind of anti-aging product, including the biologically active polypeptide
NNQFLPYPYYAKPA or described biologically active polypeptides NNQFLPYPYYAKPA derivative；Described anti-aging product includes anti-
Aging food, antisenescence health product or antiaging agent；The derivative of the biologically active polypeptide NNQFLPYPYYAKPA, refers to
On biologically active polypeptide NNQFLPYPYYAKPA amino acid side groups, aminoterminal or c-terminus progress hydroxylating, carboxyl
Change, be carbonylated, methylating, acetylation, phosphorylation, the modification such as esterification or glycosylation, obtained polypeptide derivative.
Ninth aspect present invention, there is provided product a kind of while that there is immunoloregulation function and anti-senescence function, including
The derivative of the biologically active polypeptide NNQFLPYPYYAKPA or described biologically active polypeptides NNQFLPYPYYAKPA；With exempting from
The product of epidemic disease regulatory function and anti-senescence function includes food, health products or medicine；The biologically active polypeptide
NNQFLPYPYYAKPA derivative, refer on biologically active polypeptide NNQFLPYPYYAKPA amino acid side groups, ammonia
Cardinal extremity 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 NNQFLPYPYYAKPA's of the present invention has the beneficial effect that：The milk-derived bioactivity of the present invention is more
Peptide NNQFLPYPYYAKPA has preferably regulation immunity of organisms activity and activity of fighting against senium；On the one hand, biology of the invention
Active peptides NNQFLPYPYYAKPA can strengthen the in-vitro multiplication ability of lymphocyte and macrophage, and raising body is resisted outer
The ability of boundary's pathogenic infection, reduce the body incidence of disease；On the other hand, it is possible to increase the vigor of internal anti-peroxidation enzyme system, increase
The function of strong body resistance external source sexual stimulus, so as to reduce organism aging process, aging and sick probability, there is immune adjust to exploitation
The dairy products and health products of section function and anti-senescence function tool are of great significance.
Brief description of the drawings
Fig. 1：Mass chromatography extraction figure (m/z=843.4302)；
Fig. 2：Mass-to-charge ratio is the second order mses figure of 843.4302 fragment；
Fig. 3：Mass-to-charge ratio is 843.4302 polypeptide az, by crack conditions；
Fig. 4：Influences of the various concentrations NNQFLPYPYYAKPA to C. Elegans Automatic Screening fecundity；
Fig. 5：Nematode growth conditions in the L4 phases under different condition of culture；
Fig. 6：The influence that biologically active polypeptide NNQFLPYPYYAKPA grows to C. Elegans Automatic Screening body；
Fig. 7：Influences of the biologically active polypeptide NNQFLPYPYYAKPA to C. Elegans Automatic Screening under oxidative stress.
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：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, 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 NNQFLPYPYYAKPA'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 Asn 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 Asn, Gln, Phe, Leu, Pro, Tyr, Pro, Tyr, Tyr, Ala,
Lys, Pro 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 NNQFLPYPYYAKPA.
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 NNQFLPYPYYAKPA carries out chromatography and mass spectral analysis, and its mass chromatography extraction figure is as shown in figure 1, extract the two of this peak
As shown in Figures 2 and 3, the polypeptide mass-to-charge ratio that can obtain this peak is 843.4302Da, retention time for level mass spectrogram and az, by crack conditions
It is 65.6min.
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
843.4302Da fragment sequence be Asn-Asn-Gln-Phe-Leu-Pro-Tyr-Pro-Tyr-Tyr-Ala-Lys-Pro-Ala
(NNQFLPYPYYAKPA) SEQ ID NO, are designated as：1.The fragment and κ-ss-casein variants A the 73rd~86 residue sequence phase
Corresponding, the GenBank numberings of κ-casamino acid sequence are AAA30433.1, and sequence is shown in SEQ ID NO：3.
The regulation immunity of organisms activity experiment of the biologically active peptide of embodiment 2
First, mtt assay measure biologically active polypeptide NNQFLPYPYYAKPA vitro lymphocyte proliferation capacity experimental
1. experiment material and instrument：
Reagent and material：(male 6-8 week old, Shanghai Communications University are agriculture with biological institute for experimental animal balb/c mouse
Animal experimental center)；The milk-derived biologically active polypeptide NNQFLPYPYYAKPA that embodiment 1 obtains；Mouse lymphocyte extracts
Liquid (is purchased from Suo Laibao companies)；RPMI1640 culture mediums (are purchased from GIBCO companies)；3- (4,5- dimethylthiazole -2) -2,5- bis-
Phenyl tetrazole bromide (MTT, purchased from Amresco companies)；ConA (ConA, purchased from Sigma companies)；Bovine serum albumin
(BSA, purchased from Genebase companies) in vain；Pepsin (is purchased from Sigma companies)；Pancreatin (Corolase PP, it is public purchased from AB
Department).
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.；Hera cell 150CO2 incubators, Heraeus companies；Dragon
Wellscan MK3 ELIASAs, 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 extract solution, carries out Yuan Dynasty's culture.With
Cell density is adjusted to 2.5 × 10 by complete RPMI1640 nutrient solutions6Individual/mL.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 (pH7.2~7.4,3mol/L PBS) and negative control group (500 μ g/mL BSA) are set, and research shows that its is right
Do not influenceed 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, careful abandoning supernatant, 100 μ L dimethyl sulfoxide (DMSO)s is added per hole,
37 DEG C of biochemical cultivation cases hatch 10min, shake up, light absorption value is determined at 570nm with ELIASA.
Vitro lymphocyte proliferation ability represents 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 biologically active polypeptide NNQFLPYPYYAKPA of table 1 to vitro lymphocyte proliferation
| Experiment packet | Stimulus index SI |
| Negative control group | 1 |
| NNQFLPYPYYAKPA | 1.194±0.138* |
Note：* labelled notation is compared with negative control, there is significant difference (P ＜ 0.05).
Experimental result is shown in Table 1.As shown in Table 1, it is 100 μ g/ in biologically active peptide NNQFLPYPYYAKPA mass concentration
Under conditions of mL, milk-derived biologically active peptide NNQFLPYPYYAKPA stimulus index is more than BSA, illustrates NNQFLPYPYYAKPA
The propagation of external mouse lymphocyte can be stimulated to a certain extent.And NNQFLPYPYYAKPA stimulus index reaches
1.194, and negative control group has significant difference (P<0.05).Therefore, it can be assumed that active peptides NNQFLPYPYYAKPA
With the ability for remarkably promoting mouse lymphocyte propagation, a kind of health products or additive can be used as to eat, it is possible to increase
Animal and the immunity of human body.
2nd, biologically active polypeptide NNQFLPYPYYAKPA rush macrophage phagocytosis dimethyl diaminophenazine chloride capacity experimental
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 NNQFLPYPYYAKPA that embodiment 1 obtains；LPS, purchased from Sigma companies；Dimethyl diaminophenazine chloride
Dyeing liquor, 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. experimental method：
It is 2 × 10 to add number of cells6/ ml μ l/ the holes of cell suspension 100, adherent add after purification contain active peptide
NNQFLPYPYYAKPA (1mg/ml) the μ l/ holes of RPMI1640 complete culture solutions (10%FBS) 200 are experimental group, and addition is free of
What the μ l/ holes of RPMI1640 complete culture solutions (10%FBS) 200 of active peptide were cultivated is set to blank group；And experimental group and
Blank group adds LPS to the μ g/ml of final concentration 10 when 24h is arrived in culture；Continue to cultivate to 48h, cell culture fluid is abandoned in suction.PBS
37 DEG C of μ l/ holes of dimethyl diaminophenazine chloride dye liquor 80 are added behind clean-out opening bottom, is inhaled after 10 minutes and abandons dye liquor, with PBS twice after, add per hole
Enter 150 μ l cell pyrolysis liquid (glacial acetic acid：Absolute ethyl alcohol=1:1, v/v).After 4 DEG C of dissolvings overnight, determine and inhale under wavelength 540nm
Shading value (OD540).
3. experimental result and analysis：
The biologically active polypeptide NNQFLPYPYYAKPA of table 2 promotees the measure of macrophage phagocytosis dimethyl diaminophenazine chloride ability
| Experiment packet | Inflammation group absorbance (OD540) |
| Blank group | 0.1031±0.0846 |
| Experimental group | 0.151±0.0274** |
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, compared with cell blank, addition 1mg/ml biologically active polypeptides NNQFLPYPYYAKPA's
Inflammation group macrophage phagocytosis dimethyl diaminophenazine chloride ability substantially increases, and compared with cell blank group, has significant difference (P ＜
0.01).Illustrate biologically active polypeptide NNQFLPYPYYAKPA in being swallowed in the case of having inflammation generation to macrophages in vitro
The red ability of property has significant facilitation.
The activity of fighting against senium experiment of the biologically active peptide of embodiment 3
First, the experiment that biologically active polypeptide NNQFLPYPYYAKPA influences on C. Elegans Automatic Screening fecundity
1. experiment reagent and instrument：
Reagent：C. Elegans Automatic Screening (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, Chemical Reagent Co., Ltd., Sinopharm Group；Ferment
Female powder, Chemical Reagent Co., Ltd., Sinopharm Group；The milk-derived biologically active polypeptide NNQFLPYPYYAKPA 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 flat boards
Taking strain Escherichia coli, picking single bacterium is fallen within 10ml LB fluid nutrient mediums, 37 DEG C in LB plate streakings,
200rpm, shaken cultivation 24h, it is used to be inoculated with NGM flat boards nursing nematode to OD600=0.4.100 μ L bacterium solutions are taken to be applied to 60mm
NGM flat boards, notice that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM flat boards having been coated with are in room temperature (21-25 DEG C) mistake
It can be used after night.
(2) culture of nematodes
Nematode used is hermaphroditic in this experiment, 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 (more than 80% insect is in reproduction period i.e. in plate) 2-3 plates, take 5ml M9 wash buffers 2
It is secondary, buffer solution is sucked in 15ml centrifuge tubes, 1000r/min centrifugation 3min, supernatant discarding.5ml is added newly to bleach with synchronization
Liquid, 2.5min is acutely vibrated at room temperature, adult polypide is corroded.Centrifugation, supernatant discarding.Ensure total processing time no more than
5min, prevent from damaging worm's ovum.Resuspension will be precipitated by adding M9 buffer solutions, be centrifuged after mixing, supernatant discarding, be repeated this process 3 times.
2) prescribe a time limit spawning method
Some nematodes in the egg-laying season of picking are in same flat board, 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 flat board,
Choose nematode in flat board, then the ovum in flat board is in same growth period.
(4) index determining
Using C. Elegans Automatic Screening as animal model, the L4 phase nematodes after the processing of picking synchronization arrive respective concentration for this experiment
In NGM plates.Each concentration at least 8 nematodes, each NGM plates are transferred to one, are designated as 0 day, move to daily later in new plate until
Nematode reproduction is no longer laid eggs substantially, and the total laying of nematode is counted before it enters the egg-laying season.
3. experimental result and analysis：
Experimental result is as shown in figure 4, compared with not feeding polypeptide NNQFLPYPYYAKPA blank group, feeding not homogeneity
In the experimental group for measuring concentration, its eggs on average number has different degrees of increase.The polypeptide NNQFLPYPYYAKPA concentration of feeding
For 300mg/L when, nematode eggs on average number has highly significant difference (P compared with blank group<0.01), it is in its concentration
When 400mg/L, 500mg/L, significant difference (P is but only presented compared with blank group<0.05), this is also further demonstrated that
300mg/L acts on optium concentration for mixing galanin peptide NNQFLPYPYYAKPA, can't suppress nematode with the raising of peptide concentration
Reproduction, but its action effect weakens.In summary, polypeptide NNQFLPYPYYAKPA can be obviously improved nematode under finite concentration
Fecundity.Meanwhile this test result indicates that, polypeptide NNQFLPYPYYAKPA 300mg/L are optimum concentration.But with dense
The increase of degree, the fecundity of nematode but no longer significantly improve.
2nd, biologically active polypeptide NNQFLPYPYYAKPA grows the experiment influenceed to C. Elegans Automatic Screening body
1. experiment reagent and instrument：
Reagent：C. Elegans Automatic Screening (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, Chemical Reagent Co., Ltd., Sinopharm Group；Ferment
Female powder, Chemical Reagent Co., Ltd., Sinopharm Group；The milk-derived biologically active polypeptide NNQFLPYPYYAKPA 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 flat boards
Taking strain Escherichia coli, picking single bacterium is fallen within 10ml LB fluid nutrient mediums, 37 DEG C in LB plate streakings,
200rpm, shaken cultivation 24h, it is used to be inoculated with NGM flat boards nursing nematode to OD600=0.4.100 μ L bacterium solutions are taken to be applied to 60mm
NGM flat boards, notice that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM flat boards having been coated with are in room temperature (21-25 DEG C) mistake
It can be used after night.
(2) culture of nematodes
Nematode used is hermaphroditic in this experiment, 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 (more than 80% insect is in reproduction period i.e. in plate) 2-3 plates, take 5ml M9 wash buffers 2
It is secondary, buffer solution is sucked in 15ml centrifuge tubes, 1000r/min centrifugation 3min, supernatant discarding.5ml is added newly to bleach with synchronization
Liquid, 2.5min is acutely vibrated at room temperature, adult polypide is corroded.Centrifugation, supernatant discarding.Ensure total processing time no more than
5min, prevent from damaging worm's ovum.Resuspension will be precipitated by adding M9 buffer solutions, be centrifuged after mixing, supernatant discarding, be repeated this process 3 times.
2) prescribe a time limit spawning method
Some nematodes in the egg-laying season of picking are in same flat board, 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 flat board,
Choose nematode in flat board, then the ovum in flat board 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 is developed for nematode growth to a certain extent.The nematode of each group synchronization culture is growing to
During L2 phases (culture 2 days or so), 40 nematodes of picking to respective NGM flat boards respectively, continuous 2 days, 3 days, 4 days, 5 days, 6 days, 8
My god, observe its growth conditions with inverted microscope within 10 days, determine and record its body length, 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
(the 4th day), the adult stage (the 6th day), Continuous Observation 8 days, until the 10th day of nematode growth, determine nematode under each time point
Body is grown.Can be seen that each group nematode its body length in the L4 phases with reference to Fig. 5 and Fig. 6 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
Coincide, at nematode L3 phases (the 3rd day), although slightly different for the average body length of nematode, do not present statistically aobvious
Write sex differernce.Experiment shows that polypeptide NNQFLPYPYYAKPA concentration can't influence the growth of nematode.Meanwhile it is also seen that
Nematode is that it grows stage the most quick in the L3 phases (the 3rd day) to L4 phases (the 4th day).
3rd, biologically active polypeptide NNQFLPYPYYAKPA Acute oxidative stress survival experiment
1. experiment reagent and instrument：
Reagent：C. Elegans Automatic Screening (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, Chemical Reagent Co., Ltd., Sinopharm Group；Ferment
Female powder, Chemical Reagent Co., Ltd., Sinopharm Group；30% hydrogenperoxide steam generator, Chemical Reagent Co., Ltd., Sinopharm Group；Implement
The milk-derived biologically active polypeptide NNQFLPYPYYAKPA 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 flat boards
Taking strain Escherichia coli, picking single bacterium is fallen within 10ml LB fluid nutrient mediums, 37 DEG C in LB plate streakings,
200rpm, shaken cultivation 24h, it is used to be inoculated with NGM flat boards nursing nematode to OD600=0.4.100 μ L bacterium solutions are taken to be applied to 60mm
NGM flat boards, notice that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM flat boards having been coated with are in room temperature (21-25 DEG C) mistake
It can be used after night.
(2) culture of nematodes
Nematode used is hermaphroditic in this experiment, 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 (more than 80% insect is in reproduction period i.e. in plate) 2-3 plates, take 5ml M9 wash buffers 2
It is secondary, buffer solution is sucked in 15ml centrifuge tubes, 1000r/min centrifugation 3min, supernatant discarding.5ml is added newly to bleach with synchronization
Liquid, 2.5min is acutely vibrated at room temperature, adult polypide is corroded.Centrifugation, supernatant discarding.Ensure total processing time no more than
5min, prevent from damaging worm's ovum.Resuspension will be precipitated by adding M9 buffer solutions, be centrifuged after mixing, supernatant discarding, be repeated this process 3 times.
2) prescribe a time limit spawning method
Some nematodes in the egg-laying season of picking are in same flat board, 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 flat board,
Choose nematode in flat board, then the ovum in flat board is in same growth period.
(4) index determining
Experiment packet：Blank group and polypeptide group.L4 phase nematodes after synchronization is handled are placed in corresponding NGM plates, experiment
In H containing 20mM2O2NGM flat boards in carry out, 10 are no less than per plate quantity, counts 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. flee to flat board wall
Or cover and thirst；2. worm's ovum is hatched into bag sample worm in vivo：3. pierce in agar.
3. experimental result and analysis：
Influences of the biologically active polypeptide NNQFLPYPYYAKPA of table 3 to nematode under oxidative stress
As can be seen from Table 3, there is the average life span under oxidative stress of experimental group nematode conspicuousness to improve (P ＜ 0.05),
Extremely significant difference (P is presented in polypeptide NNQFLPYPYYAKPA groups<0.05).The each group half death time is also accordingly in certain journey
Extend on degree, hybrid peptide group is presented conspicuousness and improves (P compared with other experimental groups<0.05).As shown in fig. 7, aoxidizing
Under stressed condition, experimental group survival rate is obviously higher than blank group survival rate.This explanation under the conditions of oxidative stress, deposit by nematode
Motility rate is significantly improved, it may be possible to because polypeptide NNQFLPYPYYAKPA can effectively help nematode to resist oxidative damage, clearly
Except the accumulation of internal caused free radical and reduction peroxide, rather than realized by strengthening its heat hardiness.Organism life-span
Extension be due to improve resistance of the cell to stress conditions to a certain extent, thus anti-aging and pressure stress bars
Much relations be present in the survival rate under part.This results show polypeptide NNQFLPYPYYAKPA can significantly increase the pressure of nematode
Power with oxidative stress ability, stress improve the survival rate of nematode, illustrate certain density polypeptide NNQFLPYPYYAKPA for line
Worm has the effect of anti-aging.
It can be drawn by above example, biologically active polypeptide NNQFLPYPYYAKPA of the present invention has immunological regulation work(
Energy and anti-senescence function.
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 NNQFLPYPYYAKPA and its preparation method and application
<160> 3
<170> SIPOSequenceListing 1.0
<210> 1
<211> 14
<212> PRT
<213>Artificial sequence (Artificial Sequence)
<400> 1
Asn Asn Gln Phe Leu Pro Tyr Pro Tyr Tyr Ala Lys Pro Ala
1 5 10
<210> 2
<211> 42
<212> DNA
<213>Artificial sequence (Artificial Sequence)
<400> 2
aataatcaat ttctgccata cccatattat gcaaagccag ct 42
<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 NNQFLPYPYYAKPA, it is characterised in that its amino acid sequence is Asn-Asn-Gln-
Phe-Leu-Pro-Tyr-Pro-Tyr-Tyr-Ala-Lys-Pro-Ala。
2. a kind of biologically active polypeptide NNQFLPYPYYAKPA according to claim 1, it is characterised in that the biology is living
Property polypeptide is milk-derived.
3. encode the nucleotide fragments of biologically active polypeptide NNQFLPYPYYAKPA described in claim 1, it is characterised in that described
The sequence of nucleotide fragments such as SEQ ID NO：Shown in 2.
4. biologically active polypeptide NNQFLPYPYYAKPA as claimed in claim 1 preparation method, it is characterised in that pass through gene
The method of engineering is artificial synthesized, or is directly obtained from dairy products by the method isolated and purified, or directly passes through chemical synthesis
Prepare.
5. biologically active polypeptide NNQFLPYPYYAKPA as claimed in claim 1 application, it is characterised in that the bioactivity
Applications of the polypeptide NNQFLPYPYYAKPA in the food with immunoloregulation function, health products, medicine or cosmetics are prepared.
6. biologically active polypeptide NNQFLPYPYYAKPA as claimed in claim 1 application, it is characterised in that the bioactivity
Applications of the polypeptide NNQFLPYPYYAKPA in the food with anti-senescence function, health products or medicine is prepared.
7. biologically active polypeptide NNQFLPYPYYAKPA as claimed in claim 1 application, it is characterised in that the bioactivity
Polypeptide NNQFLPYPYYAKPA answering in the food with immunoloregulation function and anti-senescence function, health products or medicine is prepared
With.
8. a kind of immunological regulation product, it is characterised in that including biologically active polypeptide as claimed in claim 1
NNQFLPYPYYAKPA or described biologically active polypeptides NNQFLPYPYYAKPA derivative；Described immunological regulation product includes
Immunological regulation food, immunological regulation health products, immunoregulation medicament or immunological regulation cosmetics；The biologically active polypeptide
NNQFLPYPYYAKPA derivative, refer on biologically active polypeptide NNQFLPYPYYAKPA amino acid side groups, ammonia
Cardinal extremity or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate, acetylation, phosphorylation, esterification or glycosylation modified, obtain
The polypeptide derivative arrived.
9. a kind of anti-aging product, it is characterised in that including biologically active polypeptide NNQFLPYPYYAKPA as claimed in claim 1
Or the derivative of the biologically active polypeptide NNQFLPYPYYAKPA；Described anti-aging product includes antisenility cistanche food, anti-ageing
Old health products or antiaging agent；The derivative of the biologically active polypeptide NNQFLPYPYYAKPA, refers to more in bioactivity
On peptide NNQFLPYPYYAKPA amino acid side groups, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonylation, first
Base, acetylation, phosphorylation, esterification or glycosylation modified, obtained polypeptide derivative.
10. a kind of product with immunoloregulation function and anti-senescence function, it is characterised in that including as claimed in claim 1
Biologically active polypeptide NNQFLPYPYYAKPA or described biologically active polypeptides NNQFLPYPYYAKPA derivative；With immune tune
The product of section function and anti-senescence function includes food, health products or medicine；The biologically active polypeptide NNQFLPYPYYAKPA
Derivative, refer on biologically active polypeptide NNQFLPYPYYAKPA amino acid side groups, aminoterminal or c-terminus enter
Row hydroxylating, carboxylated, be carbonylated, methylate, acetylation, phosphorylation, esterification or glycosylation modified, obtained polypeptide derives
Thing.
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| CN108623669A (en) * | 2018-05-02 | 2018-10-09 | 扬州大学 | Immune-active peptides and its enrichment method and application in a kind of acidified milk |
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Cited By (2)
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| CN108623669A (en) * | 2018-05-02 | 2018-10-09 | 扬州大学 | Immune-active peptides and its enrichment method and application in a kind of acidified milk |
| CN108623669B (en) * | 2018-05-02 | 2021-07-09 | 扬州大学 | Immune active peptide in fermented milk and enrichment method and application thereof |
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