CN110903376B - Bioactive polypeptide RISLPLPTFSSL, and preparation method and application thereof - Google Patents
Bioactive polypeptide RISLPLPTFSSL, and preparation method and application thereof Download PDFInfo
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- CN110903376B CN110903376B CN201911087306.4A CN201911087306A CN110903376B CN 110903376 B CN110903376 B CN 110903376B CN 201911087306 A CN201911087306 A CN 201911087306A CN 110903376 B CN110903376 B CN 110903376B
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- rislplptfssl
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- aging
- polypeptide
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Images
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
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- 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
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P39/00—General protective or antinoxious agents
- A61P39/06—Free radical scavengers or antioxidants
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- 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
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Abstract
The invention relates to the field of protein, and in particular relates to a bioactive polypeptide RISLPLPTFSSL, a preparation method and application thereof, wherein the amino acid sequence of the bioactive polypeptide RISLPLPTFSSL is Arg-Ile-Ser-Leu-Pro-Leu-Pro-Thr-Phe-Ser-Ser-Leu. In vitro anti-inflammatory activity experiments and in vivo anti-aging experiments prove that the polypeptide RISLPLPTFSSL has good anti-inflammatory function and anti-aging activity, and on one hand, the bioactive polypeptide RISLPLPTFSSL disclosed by the invention can promote the capacity of increasing the induced amount of macrophage nitric oxide, improve the capacity of resisting the infection of external pathogens by an organism and reduce the morbidity of the organism; on the other hand, the compound has good anti-aging activity, can remove free radicals in the organism and improve the quality of life, and has very important significance for developing foods, health-care products and medicines with anti-inflammatory and anti-aging functions.
Description
Technical Field
The invention relates to the field of proteins, in particular to a bioactive polypeptide RISLPLPTFSSL, and a preparation method and application thereof.
Background
With the improvement of living standard, the requirement of people on diet changes from 'pursuit amount' to 'quality'. Therefore, research on bioactive peptides having specific functions has been hot. In recent years, some food-derived polypeptides, such as short peptides of corn, soybean peptides, milk polypeptides, etc., have been found to have good biological activity. And experiments prove that the health-care tea has the functions of resisting aging, bacteria and cancers, resisting inflammation, reducing blood pressure and the like.
The polypeptides can be obtained through various ways such as microbial fermentation, digestion and enzymolysis and the like, and most of the polypeptides with biological activity consist of 2-20 amino acid residues, have the molecular weight of less than 6000Da and contain a certain amount of hydrophobic amino acids and aromatic amino acids.
Macrophages are the second defense line of the body against the invasion of external harmful substances, are widely present in various tissues of the body, are main immune response cells, participate in biological functions such as immune response, anti-inflammation and the like through phagocytosis and secretion of cytokines, and play an important role in an immune system. The function of the polypeptide present in macrophages was investigated.
Currently, there are some researches on anti-aging bioactive peptides in the prior art, but new bioactive polypeptides having anti-oxidation or anti-aging functions different from the existing polypeptides are still the current direction of further research needed to further expand the diversity of bioactive polypeptides.
Disclosure of Invention
The invention aims to provide a bioactive polypeptide RISLPLPTFSSL, and a preparation method and application thereof.
The purpose of the invention can be realized by the following technical scheme:
in a first aspect of the present invention, a biologically active polypeptide RISLPLPTFSSL is provided, wherein the amino acid sequence is Arg-Ile-Ser-Leu-Pro-Leu-Pro-Thr-Phe-Ser-Ser-Leu, as shown in SEQ ID NO: 1 is shown.
Preferably, the bioactive polypeptide is mouse bone marrow-derived macrophage peptide. The protein is particularly derived from Vimentin protein and is the amino acid residue from the 410 th to 421 th positions of the Vimentin protein. The amino acid sequence of the Vimentin protein is shown as SEQ ID NO: 2, respectively.
The amino acid sequence and the corresponding nucleotide sequence of the Vimentin protein are the prior art, and the nucleotide fragment for coding the 410 th to 421 th amino acid residues of the Vimentin protein can code mature bioactive polypeptide RISLPLPTFSSL.
Preferably, the bioactive polypeptide has anti-inflammatory and anti-aging functions.
In the second aspect of the present invention, a method for preparing the bioactive polypeptide RISLPLPTFSSL is provided, which can be artificially synthesized by genetic engineering methods, can be directly obtained from cells by a separation and purification method, and can be directly prepared by chemical synthesis.
In a third aspect of the invention, an application of the bioactive polypeptide RISLPLPTFSSL in preparing foods, health products, medicines or cosmetics with anti-inflammatory functions is provided.
In the fourth aspect of the invention, the application of the bioactive polypeptide RISLPLPTFSSL in preparing food, health-care products or medicines with the anti-aging function is provided.
In the fifth aspect of the invention, the application of the bioactive polypeptide RISLPLPTFSSL in preparing food, health-care products or medicines with anti-inflammatory and anti-aging functions is provided.
In particular, the biologically active polypeptide RISLPLPTFSSL of the present invention can be used for preparing cosmetics for reducing free radical damage to skin, and medicines for anti-inflammation and/or anti-aging.
In a sixth aspect of the invention, there is provided an anti-inflammatory product comprising said biologically active polypeptide RISLPLPTFSSL or a derivative of said biologically active polypeptide RISLPLPTFSSL; the anti-inflammatory product comprises anti-inflammatory food, anti-inflammatory health product, anti-inflammatory drug or anti-inflammatory cosmetic; the derivative of the biologically active polypeptide RISLPLPTFSSL refers to a polypeptide derivative obtained by performing modifications such as hydroxylation, carboxylation, carbonylation, methylation, acetylation, phosphorylation, esterification or glycosylation on an amino acid side chain group, an amino terminal or a carboxyl terminal of the biologically active polypeptide RISLPLPTFSSL.
In a seventh aspect of the invention, there is provided an anti-aging product comprising the biologically active polypeptide RISLPLPTFSSL or a derivative of the biologically active polypeptide RISLPLPTFSSL; the anti-aging product comprises anti-aging food, anti-aging health care product or anti-aging drug; the derivative of the biologically active polypeptide RISLPLPTFSSL refers to a polypeptide derivative obtained by performing modifications such as hydroxylation, carboxylation, carbonylation, methylation, acetylation, phosphorylation, esterification or glycosylation on an amino acid side chain group, an amino terminal or a carboxyl terminal of the biologically active polypeptide RISLPLPTFSSL.
In the eighth aspect of the present invention, there is provided a product having both anti-inflammatory and anti-aging functions, comprising the biologically active polypeptide RISLPLPTFSSL or a derivative of the biologically active polypeptide RISLPLPTFSSL; products with anti-inflammatory and anti-aging effects include foods, health products or drugs; the derivative of the biologically active polypeptide RISLPLPTFSSL refers to a polypeptide derivative obtained by performing modifications such as hydroxylation, carboxylation, carbonylation, methylation, acetylation, phosphorylation, esterification or glycosylation on an amino acid side chain group, an amino terminal or a carboxyl terminal of the biologically active polypeptide RISLPLPTFSSL.
The bioactive polypeptide RISLPLPTFSSL has the following beneficial effects: the mouse bone marrow-derived macrophage bioactive polypeptide RISLPLPTFSSL has good anti-inflammatory activity and anti-aging activity; on one hand, the bioactive polypeptide RISLPLPTFSSL can promote the capacity of increasing the induction quantity of macrophage nitric oxide, improve the capacity of resisting the infection of external pathogens of an organism and reduce the morbidity of the organism; on the other hand, the compound has good anti-aging activity, can remove free radicals in the organism and improve the quality of life, and has very important significance for developing foods, health-care products and medicines with anti-inflammatory and anti-aging functions.
Drawings
FIG. 1: mass chromatogram extraction (m/z 665.8907);
FIG. 2: a secondary mass spectrum of a fragment with a mass to charge ratio of 665.8907;
FIG. 3: and (3) the cleavage condition of the polypeptide az and by with the mass-to-charge ratio of 665.8907.
Detailed Description
Before the present embodiments are further described, it is to be understood that the scope of the invention is not limited to the particular embodiments described below; it is also to be understood that the terminology used in the examples is for the purpose of describing particular embodiments only, and is not intended to limit the scope of the present invention.
When numerical ranges are given in the examples, it is understood that both endpoints of each of the numerical ranges and any value therebetween can be selected unless the invention otherwise indicated. Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. In addition to the specific methods, devices, and materials used in the examples, any methods, devices, and materials similar or equivalent to those described in the examples may be used in the practice of the invention in addition to the specific methods, devices, and materials used in the examples, in keeping with the knowledge of one skilled in the art and with the description of the invention.
Unless otherwise indicated, the experimental methods, detection methods, and preparation methods disclosed herein all employ techniques conventional in the art of molecular biology, biochemistry, chromatin structure and analysis, analytical chemistry, cell culture, recombinant DNA technology, and related arts. These techniques are well described in the literature, and may be found in particular in the study of the MOLECULAR CLONING, Sambrook et al: a LABORATORY MANUAL, Second edition, Cold Spring Harbor LABORATORY Press, 1989and Third edition, 2001; ausubel et al, Current PROTOCOLS IN MOLECULAR BIOLOGY, John Wiley & Sons, New York, 1987 and periodic updates; the series METHODS IN ENZYMOLOGY, Academic Press, San Diego; wolffe, CHROMATIN STRUCTURE AND FUNCTION, Third edition, Academic Press, San Diego, 1998; (iii) METHODS IN ENZYMOLOGY, Vol.304, Chromatin (P.M.Wassarman and A.P.Wolffe, eds.), Academic Press, San Diego, 1999; and METHODS IN MOLECULAR BIOLOGY, Vol.119, chromatography Protocols (P.B.Becker, ed.) Humana Press, Totowa, 1999, etc.
The invention is described in detail below with reference to the figures and specific embodiments.
Example 1 Artificial Synthesis of active peptide RISLPLPTFSSL
Synthesis of bioactive peptide
1. 3g of RINK resin (degree of substitution 0.3mmol/g) was weighed into a 150ml reactor and soaked with 50ml of Dichloromethane (DCM).
After 2.2 hours, the resin was washed with 3 resin volumes of N-Dimethylformamide (DMF) and then drained, and this was repeated four times and the resin was drained until use.
3. The Fmoc protecting group on the resin was removed by adding a quantity of 20% piperidine (piperidine/DMF: 1:4, v: v) to the reactor and shaking on a decolourising shaker for 20 min. After deprotection, the resin was washed four times with 3 resin volumes of DMF and then drained.
4. And (3) detecting a small amount of resin by a ninhydrin (ninhydrin) method (detecting A and B, respectively, and reacting at 100 ℃ for 1min), wherein the resin is colored, which indicates that the deprotection is successful.
5. Weighing a proper amount of amino acid Arg and a proper amount of 1-hydroxy-benzotriazole (HOBT) into a 50ml centrifuge tube, adding 20ml of DMF to dissolve the amino acid Arg and the 1-hydroxy-benzotriazole (HOBT), then adding 3ml of N, N Diisopropylcarbodiimide (DIC) to shake and shake for 1min, adding the solution into a reactor after the solution is clarified, and then placing the reactor into a 30 ℃ shaking table to react.
After 6.2 hours, the column was capped with a suitable amount of acetic anhydride (acetic anhydride: DIEA: DCM ═ 1:1:2, v: v: v) for half an hour, then washed four times with 3 resin volumes of DMF and drained until needed.
7. The Fmoc protecting group on the resin was removed by adding a quantity of 20% piperidine (piperidine/DMF: 1:4, v: v) to the reactor and shaking on a decolourising shaker for 20 min. After deprotection was washed four times with DMF and then drained.
8. And (3) detecting a small amount of resin by a ninhydrin (ninhydrin) method (detecting A and B, respectively, and reacting at 100 ℃ for 1min), wherein the resin is colored, which indicates that the deprotection is successful.
9. Weighing an appropriate amount of the second amino acid Ile and an appropriate amount of HOBT in a 50ml centrifuge tube, adding 25ml DMF to dissolve the second amino acid Ile and the HOBT, adding 2.5ml DIC to shake for 1min, adding the solution into a reactor after the solution is clarified, and then placing the reactor in a shaker at 30 ℃ to react.
After 10.1 hours, a small amount of resin is taken for detection, and the detection is carried out by an indanthrone method (two drops are respectively detected A and B, and the reaction is carried out for 1min at 100 ℃), if the resin is colorless, the reaction is complete; if the resin is colored, the condensation is not complete and the reaction is continued.
11. After the reaction was completed, the resin was washed four times with DMF and then drained, and a certain amount of 20% piperidine (piperidine/DMF ═ 1:4, v: v) was added to the reactor, and the mixture was shaken on a decolorizing shaker for 20min to remove the Fmoc-protecting group from the resin. After the protection is removed, washing with DMF for four times, and then draining to detect whether the protection is removed.
12. And sequentially grafting amino acids Ile, Ser, Leu, Pro, Thr, Phe, Ser and Leu according to the steps 9-11.
13. After the last amino acid had been grafted, the protection was removed, washed four times with DMF and the resin was drained with methanol. The polypeptide was then cleaved from the resin with 95 cleavage medium (trifluoroacetic acid: 1,2 ethanedithiol: 3, isopropylsilane: water: 95:2:2:1, v: v: v) (10 ml of cleavage medium per gram of resin) and centrifuged four times with glacial ethyl ether (cleavage medium: ethyl ether: 1:9, v: v).
To this end, bioactive peptide RISLPLPTFSSL was synthesized.
Confirmation of biologically active peptides
1) UPLC analysis
UPLC conditions were as follows:
the instrument comprises the following steps: waters ACQUITY UPLC ultra-high performance liquid-electrospray-quadrupole-time-of-flight mass spectrometer
Specification of chromatographic column: BEH C18 chromatographic column
Flow rate: 0.4mL/min
Temperature: 50 deg.C
Ultraviolet detection wavelength: 210nm
Sample introduction amount: 2 μ L
Gradient conditions: solution A: water containing 0.1% formic acid (v/v), liquid B: acetonitrile containing 0.1% formic acid (v/v)
2) Mass spectrometric analysis
The mass spectrometry conditions were as follows:
ion mode: ES +
Mass range (m/z): 100-1000
Capillary voltage (Capillary) (kV): 3.0
Sampling cone (V): 35.0
Ion source temperature (. degree. C.): 115
Desolvation temperature (. degree. C.): 350
Desolventizing gas stream (L/hr): 700.0
Collision energy (eV): 4.0
Scan time (sec): 0.25
Inner scan time (sec): 0.02
According to the analysis method, the ultra-high performance liquid chromatography-electrospray-quadrupole-time-of-flight mass spectrometry is used for carrying out chromatographic analysis and mass spectrometric analysis on the bioactive peptide RISLPLPTFSSL, the mass chromatogram extraction diagram is shown in figure 1, the secondary mass spectrogram of the peak and the az and by fracture conditions are shown in figures 2 and 3, the polypeptide mass-to-charge ratio of the peak is 665.8907Da, and the retention time is 114.9 min.
3) Results
As can be seen from FIG. 3, according to the cases of az and by fragmentation, the fragment sequence with mass-to-charge ratio of 665.8907Da obtained by analysis and calculation of Mascot software is Arg-Ile-Ser-Leu-Pro-Leu-Pro-Thr-Phe-Ser-Ser-Leu (RISLPTFSSL), and is marked as SEQ ID NO: 1. the fragment corresponds to the residue sequence of Vimentin protein 410-421, the GenBank number of the Vimentin protein amino acid sequence is AAA40556.1, and the sequence is shown in SEQ ID NO: 2.
example 2 anti-inflammatory Activity assay of bioactive peptides
Determination of macrophage-promoting nitric oxide-inducing amount of bioactive polypeptide RISLPLPTFSSL (Griess method)
1. Experimental reagents and instruments:
reagent: experimental animals balb/c mice (male 6-8 weeks old) were collected at the animal Experimental center of the college of agriculture and biology of Shanghai university of transportation; the mouse bone marrow macrophage-derived bioactive peptide RISLPLPTFSSL obtained in example 1; LPS, purchased from Sigma; neutral red staining solution, produced by Biyuntian biotechnological research institute.
The instrument equipment comprises: LRH-250F Biochemical incubator Shanghai Hengshi Co., Ltd; GL-22M high speed refrigerated centrifuge Shanghai Luxiang apparatus centrifuge Instrument Co., Ltd; hera cell 150CO2 incubator Heraeus; dragon Wellscan MK3 microplate reader Labsystems.
2. The test method comprises the following steps:
the number of the added cells was 2X 106100 μ l/well of a cell suspension per ml, 200 μ l/well of a complete peptide-containing RPMI1640 culture medium (10% FBS) was added after adherent purification, LPS was added to a final concentration of 10 μ g/ml at 24 hours in an inflammation group, 50 μ l/well of a culture supernatant was collected after continuous culture for 48 hours, 50 μ l/well of Griess reagent 1 and Griess reagent 2 were sequentially added to the culture supernatant, and after reaction at room temperature for 10 minutes, an absorbance value (OD540) was measured at a wavelength of 540 nm.
3. Experimental results and analysis:
TABLE 1 determination of macrophage nitric oxide-inducing amount of biologically active polypeptide RISLPLPTFSSL
| Experiment grouping | Normal group | Inflammation group |
| Cell blank | 0.0594±0.0051 | 0.3244±0.0382 |
| RISLPLPTFSSL 1mg/ml | 0.1270±0.0262** | 0.4881±0.0255** |
| RISLPLPTFSSL 0.5mg/ml | 0.1285±0.0103** | 0.3350±0.0311** |
| RISLPLPTFSSL 0.1mg/ml | 0.0630±0.0002 | 0.3485±0.0195** |
Note: significant difference compared to negative control (P < 0.05);
significant difference compared with negative control group (P <0.01)
The results are shown in Table 1, and it is understood from Table 1 that the addition of the biologically active polypeptide RISLPLPTFSSL at concentrations of 1mg/mL and 0.5mg/mL to the test group promotes the NO induction of macrophages, both in normal growth and in LPS-induced inflammation. There was a significant difference (P <0.01) compared to the cell blank. When the added concentration of the bioactive polypeptide RISLPLPTFSSL is 0.1mg/mL, the increase of the nitric oxide induction amount of macrophages can be promoted compared with that in the situation of inflammation caused by LPS, and the difference is significant (P < 0.01). But there were no significant differences compared to the cell blank grown under normal conditions. The biologically active polypeptide RISLPLPTFSSL is shown to have the ability to promote an increase in nitric oxide-induced levels in macrophages at certain concentrations.
Example 3 anti-aging Activity assay of bioactive peptides
Experiment of bioactive polypeptide RISLPLPTFSSL on antioxidant level of in vivo organ
1. Experimental reagents and instruments:
reagent: experimental animal ICR mouse (male 5 weeks old), shanghai city experimental animal center; d-gal, national pharmaceutical group chemical reagents, Inc.; paraformaldehyde, chemical reagents of the national drug group, ltd; sodium chloride, national pharmaceutical group chemical reagents ltd; the mouse bone marrow macrophage-derived bioactive peptide RISLPLPTFSSL obtained in example 1; BCA protein kit, Nanjing Kaikyi Biotech Co., Ltd; MDA lipid peroxide kit, south kyo kaiky biotechnology limited; SOD superoxide dismutase kit, Nanjing, biological technology Limited; T-AOC total antioxidant activity kit, Nanjing, established Biotechnology Limited.
The instrument equipment comprises: model CM-230 Mohr super Water, Shanghai Mole scientific instruments, Inc.; millipore Milllex GP0.22 μm membrane filter, Millipore USA; GL-22M high-speed refrigerated centrifuge, Shanghai Luxiang apparatus centrifuge instruments Inc.
2. The experimental method comprises the following steps:
(1) model for animal aging
After one week of adaptive ICR mouse feeding, 4 groups of 6 mice were divided. Group 1 was a low dose intragastric group, mice were injected subcutaneously in the neck and back with D-gal at a dose of 500mg/kg daily and intragastric bioactive polypeptide RISLPLPTFSSL at a dose of 1 mg/day; group 2 was a high dose intragastric group, mice were injected subcutaneously in the neck and back with D-gal at a dose of 500mg/kg daily, and 3 mg/mouse a day dose of intragastric bioactive polypeptide RISLPLPTFSSL; group 3 was blank, mice grew normally; group 4 was an animal model group, and mice were injected subcutaneously into the neck and back with D-gal at a dose of 500mg/kg daily, and gavage with 0.9% normal saline; the injection period of D-gal and the gavage period of polypeptide were 42 days. The bedding is replaced every 3 days and the feed and distilled water supply is ensured. The weight of the mice was weighed once every five days, D-gal injection was prepared according to the weight of the mice, and the D-gal injection was filtered through a 0.22 μm syringe filter to ensure sterility.
(2) Obtaining animal viscera
After the experiment period is finished, blood of a mouse is obtained by an eyeball-picking blood-taking method, the mouse is killed by breaking the neck after the blood is obtained, then a body of the mouse is placed on a low-temperature ice box, the brain, the spleen, the liver and the kidney of the mouse are quickly picked, the obtained viscera are placed in a pre-sterilized 1.5mL centrifuge tube, and all organ samples are stored in a refrigerator at the temperature of-80 ℃ for inspection. All procedures in the procedure of treating the experimental animals followed the guidance comments on the animals being treated in good care published by the department of scientific technology in 2006. The spleen of the mouse is directly soaked in a prepared 4% paraformaldehyde solution to fix the shape. The paraformaldehyde powder is relatively insoluble, and a trace amount of sodium bicarbonate can be added to adjust the pH value to be alkaline so as to aid dissolution. The preparation of the paraformaldehyde solution needs to be completed in a fume hood.
(3) Sample detection
Grinding all organs to be detected in a low-temperature environment, diluting the ground organs into 10% tissue homogenate by using a4 ℃ sterile PBS solution, centrifuging 4000g at 4 ℃, sucking and taking supernate, removing precipitates, and operating according to a kit instruction or placing the mixture in a refrigerator at minus 80 ℃ for detection.
3. Experimental results and analysis:
as can be seen from Table 2-1, the SOD content in the liver and kidney of the mice in the polypeptide gavage group showed significant increase (P <0.01) compared to the mice in the animal model group. The fact that the mice in the polypeptide gavage group are stimulated by large dose of D-gal for a long time and the SOD enzyme system in the mice is not completely destroyed even if the D-gal is excessively injected indicates that the experimental animals are continuously stimulated by the aging-causing factors in the injection period to reduce the SOD content in different organs, but simultaneously ingest a certain amount of polypeptide RISLPLPTFSSL to have certain protection effect on oxidative damage in the mice.
TABLE 2-1 variation of SOD content in different organs of each group of experimental animal mice
Note: significant differences (P <0.05) in plots compared to model group controls; the plot showed significant differences (P <0.01) compared to the model group control, as follows.
As can be seen from Table 2-2, the liver MDA content of the mice in the animal model group is 26.77 + -7.25 nmol/L, and compared with the animal model group, the MDA content of the liver of the two groups of mice with the polypeptide gavage is significantly different (P < 0.01). As MDA can be used for estimating the accumulation condition of lipid peroxides in animals, it can be known that in the process of forming an aging model, sugar metabolism pathways of mice in an animal model group are disordered due to long-term injection of excessive D-gal, a large amount of free radicals are generated to cause oxidative damage, a large amount of lipid peroxides are generated in liver tissues of the mice, and MDA is used as the lipid peroxides, so that the increase of the content of the lipid peroxides in the animals can be laterally reflected to reduce the activity of antioxidant enzyme systems in the mice. The obvious reduction of the MDA content in the liver of the mice in the polypeptide gavage group shows that the ingestion of the polypeptide RISLPLPTFSSL can effectively protect important tissues and organs from being stimulated by adverse factors to generate a large amount of lipid peroxides.
TABLE 2-2 changes in MDA content in different organs of various groups of experimental animal mice
As can be seen from tables 2-3, the liver T-AOC value of the mice in the animal model group is 0.68 +/-0.20U/mgprot, and compared with the mouse in the model group, the mice in the high-dose and low-dose gavage groups of the polypeptide show significant difference (P < 0.05); the content of the kidney T-AOC in the mice of the animal model group is 0.63 +/-0.22U/mgprot, and compared with the mice of the animal model group, the mice of the low-dose gavage group have significant difference (P <0.05) and the mice of the high-dose gavage group also have significant difference (P < 0.01). The results show that in the whole experimental period, because the experimental animals are continuously stimulated by the senescence-causing factors, the liver and kidney tissues of the mice in the animal model group are damaged, so that the total antioxidant capacity of the mice is reduced. Compared with animal model group and blank group, the total antioxidant capacity of main organs of mice in polypeptide gavage group is always maintained at a higher level in the process of being stimulated by aging-causing factors, which indicates that the animal body and the main organs thereof have higher self-protection function by taking the bioactive polypeptide RISLPLPTFSSL.
TABLE 2-3 Change in T-AOC in groups of Experimental animals mice
The embodiments described above are described to facilitate an understanding and use of the invention by those skilled in the art. It will be readily apparent to those skilled in the art that various modifications to these embodiments may be made, and the generic principles described herein may be applied to other embodiments without the use of the inventive faculty. Therefore, the present invention is not limited to the above embodiments, and those skilled in the art should make improvements and modifications within the scope of the present invention based on the disclosure of the present invention.
Sequence listing
<110> Shanghai university of transportation; zhejiang ghui peptide Life health science and technology Limited
<120> a bioactive polypeptide RISLPLPTFSSL, and its preparation method and application
<160> 2
<170> SIPOSequenceListing 1.0
<210> 1
<211> 12
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 1
Arg Ile Ser Leu Pro Leu Pro Thr Phe Ser Ser Leu
1 5 10
<210> 2
<211> 466
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 2
Met Ser Thr Arg Ser Val Ser Ser Ser Ser Tyr Arg Arg Met Phe Gly
1 5 10 15
Gly Ser Gly Thr Ser Ser Arg Pro Ser Ser Asn Arg Ser Tyr Val Thr
20 25 30
Thr Ser Thr Arg Thr Tyr Ser Leu Gly Ser Ala Leu Arg Pro Ser Thr
35 40 45
Ser Arg Ser Leu Tyr Ser Ser Ser Pro Gly Gly Ala Tyr Val Thr Arg
50 55 60
Ser Ser Ala Val Arg Leu Arg Ser Ser Val Pro Gly Val Arg Leu Leu
65 70 75 80
Gln Asp Ser Val Asp Phe Ser Leu Ala Asp Ala Ile Asn Thr Glu Phe
85 90 95
Lys Asn Thr Arg Thr Asn Glu Lys Val Glu Leu Gln Glu Leu Asn Asp
100 105 110
Arg Phe Ala Asn Tyr Ile Asp Lys Val Arg Phe Leu Glu Gln Gln Asn
115 120 125
Lys Ile Leu Leu Ala Glu Leu Glu Gln Leu Lys Gly Gln Gly Lys Ser
130 135 140
Arg Leu Gly Asp Leu Tyr Glu Glu Glu Met Arg Glu Leu Arg Arg Gln
145 150 155 160
Val Asp Gln Leu Thr Asn Asp Lys Ala Arg Val Glu Val Glu Arg Asp
165 170 175
Asn Leu Ala Glu Asp Ile Met Arg Leu Arg Glu Lys Leu Gln Glu Glu
180 185 190
Met Leu Gln Arg Glu Glu Ala Glu Ser Thr Leu Gln Ser Phe Arg Gln
195 200 205
Asp Val Asp Asn Ala Ser Leu Ala Arg Leu Asp Leu Glu Arg Lys Val
210 215 220
Glu Ser Leu Gln Glu Glu Ile Ala Phe Leu Lys Lys Leu His Asp Glu
225 230 235 240
Glu Ile Gln Glu Leu Gln Ala Gln Ile Gln Glu Gln His Val Gln Ile
245 250 255
Asp Val Asp Val Ser Lys Pro Asp Leu Thr Ala Ala Leu Arg Asp Val
260 265 270
Arg Gln Gln Tyr Glu Ser Val Ala Ala Lys Asn Leu Gln Glu Ala Glu
275 280 285
Glu Trp Tyr Lys Ser Lys Phe Ala Asp Leu Ser Glu Ala Ala Asn Arg
290 295 300
Asn Asn Asp Ala Leu Arg Gln Ala Lys Gln Glu Ser Asn Glu Tyr Arg
305 310 315 320
Arg Gln Val Gln Ser Leu Thr Cys Glu Val Asp Ala Leu Lys Gly Thr
325 330 335
Asn Glu Ser Leu Glu Arg Gln Met Arg Glu Met Glu Glu Asn Phe Ala
340 345 350
Leu Glu Ala Ala Asn Tyr Gln Asp Thr Ile Gly Arg Leu Gln Asp Glu
355 360 365
Ile Gln Asn Met Lys Glu Glu Met Ala Arg His Leu Arg Glu Tyr Gln
370 375 380
Asp Leu Leu Asn Val Lys Met Ala Leu Asp Ile Glu Ile Ala Thr Tyr
385 390 395 400
Arg Lys Leu Leu Glu Gly Glu Glu Ser Arg Ile Ser Leu Pro Leu Pro
405 410 415
Thr Phe Ser Ser Leu Asn Leu Arg Glu Thr Asn Leu Glu Ser Leu Pro
420 425 430
Leu Val Asp Thr His Ser Lys Arg Thr Leu Leu Ile Lys Thr Val Glu
435 440 445
Thr Arg Asp Gly Gln Val Ile Asn Glu Thr Ser Gln His His Asp Asp
450 455 460
Leu Glu
465
Claims (2)
1. The application of the bioactive polypeptide RISLPLPTFSSL is characterized in that the bioactive polypeptide RISLPLPTFSSL is applied to the preparation of foods, health-care products or medicines with the anti-aging function; the amino acid sequence of the bioactive polypeptide RISLPLPTFSSL is Arg-Ile-Ser-Leu-Pro-Leu-Pro-Thr-Phe-Ser-Ser-Leu.
2. An anti-aging product comprising a biologically active polypeptide RISLPLPTFSSL; the anti-aging product comprises anti-aging food, anti-aging health care product, anti-aging drug or anti-aging cosmetic; the amino acid sequence of the bioactive polypeptide RISLPLPTFSSL is Arg-Ile-Ser-Leu-Pro-Leu-Pro-Thr-Phe-Ser-Ser-Leu.
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