CN116514912A - Straw mushroom polypeptide for resisting skin oxidative damage and application thereof - Google Patents
Straw mushroom polypeptide for resisting skin oxidative damage and application thereof Download PDFInfo
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- CN116514912A CN116514912A CN202310611164.7A CN202310611164A CN116514912A CN 116514912 A CN116514912 A CN 116514912A CN 202310611164 A CN202310611164 A CN 202310611164A CN 116514912 A CN116514912 A CN 116514912A
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- antioxidant
- straw mushroom
- polypeptide
- dwpgfk
- oxidative damage
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/18—Antioxidants, e.g. antiradicals
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
- A61Q19/08—Anti-ageing preparations
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Organic Chemistry (AREA)
- Dermatology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Mycology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- General Chemical & Material Sciences (AREA)
- Nutrition Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Birds (AREA)
- Epidemiology (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention discloses a straw mushroom polypeptide for resisting skin oxidative damage and application thereof. The amino acid sequence of the straw mushroom polypeptide is DWPGFK. The invention extracts and purifies polypeptide from straw mushroom fruiting body protein, determines the amino acid sequence of one antioxidant peptide through LC-MS/MS, and has DPPH free radical clearance of 73.58 percent+/-0.38 percent and Fe after antioxidant activity detection 2+ The chelation rate was 84.46% + -1.32% and the reducing power was 0.42+ -0.01. The straw mushroom polypeptide provided by the invention can play a role in protecting the oxidative damage of HSF cells by reducing the ROS level, protecting the integrity of cell membranes, enhancing endogenous antioxidant enzyme, increasing glutathione peroxidase activity and reducing malondialdehyde content, can be used as a natural antioxidant peptide or antioxidant stress reagent, and has potential application prospects in the fields of preparing medicines, antioxidant damage health-care products, skin care products and the like for scavenging free radicals.
Description
Technical Field
The invention belongs to the technical field of biological extracts, and relates to a straw mushroom polypeptide for resisting skin oxidative damage and application thereof.
Background
Excessive free radical attack on biomolecules in the human body causes oxidative damage, which to some extent causes potential damage to the body, leading to the development of various diseases such as cancer, aging, atherosclerosis and Alzheimer's disease. Several studies have shown that antioxidants, at relatively low concentrations, can inhibit or delay oxidative damage to cells, and have an important role in human health. The research of efficient and safe natural antioxidants has been the focus of attention of researchers at home and abroad. Antioxidant peptides extracted from natural products are reported to have free radical scavenging activity with less toxicity and side effects to humans than chemically synthesized drugs. The only disadvantage is the low oral bioavailability of polypeptide drugs. Ouyang Junfang et al point out that oral biomacromolecule drugs have very limited stability and absorption degree in the gastrointestinal tract, reviewed the entrapment mode of lipid nanocarriers on protein polypeptide drugs and their corresponding mechanism of overcoming physiological barriers, and introduced important characteristics and recent research progress for improving the oral bioavailability of protein polypeptide drugs (Ouyang Junfang, zhang Yongjie, chen Xijing. Research progress of lipid nanocarriers for oral delivery of protein polypeptide drugs [ J ]. J.China medicine industry J2022,53 (09): 1240-1250.).
Numerous studies have demonstrated that edible fungi are rich in a variety of antioxidants including polysaccharides, phenols, proteins, peptides, carotenoids, ergosterol, vitamins C and E, and the like. In addition, edible mushrooms grow faster than plants, which makes them a relatively abundant source of commercial natural bioactive compounds. Pei Yuncheng the preparation and preliminary analysis of stability of antioxidant peptide of pleurotus eryngii stem have been studied, wherein the DPPH free radical clearance of the antioxidant peptide of pleurotus eryngii is 55.52% + -0.89%, the clearance is lower, and the antioxidant capacity is not strong (Pei Yuncheng, zhu Dan, cui Cailian, et al. Preparation of antioxidant peptide of apricot Bao Gubing and preliminary analysis of stability thereof [ J ]. Food industry technology, 2020,41 (4): 8.). Straw mushrooms contain various active ingredients, especially abundant proteins, but no related report has been made so far on the preparation of antioxidant peptides from straw mushroom fruiting bodies as raw materials.
Human Skin Fibroblasts (HSF) are the major constituent cells of the dermis layer, which, in conjunction with the extracellular matrix, secrete synthetic elastin, collagen, cytokines, etc., are important for delaying skin aging. However, HSF cells exhibit reduced numbers, reduced proliferation capacity, reduced metabolic function, reduced levels of secreted collagen and elastin, disordered arrangement of elastic fibers and collagen fibers, and the like as skin ages. Therefore, the proliferation rate of HSF cells, and the content of collagen and elastin in HSF cells are very important indicators for evaluating anti-aging performance.
Disclosure of Invention
The invention aims to provide a straw mushroom polypeptide for resisting skin oxidative damage and application thereof.
The technical solution for realizing the purpose of the invention is as follows:
the amino acid sequence of the straw mushroom polypeptide for resisting skin oxidative damage is DWPGFK, namely Asp-Trp-Pro-Gly-Phe-Lys, and is shown as SEQ ID NO. 1.
The application of the straw mushroom polypeptide in preparing a medicament for removing free radicals is provided.
The free radical is DPPH.
The application of the straw mushroom antioxidant peptide in preparing skin care products or health care products for resisting skin oxidative damage is provided.
Compared with the prior art, the invention has the following advantages:
the invention firstly extracts and purifies polypeptide from the sporophore protein of straw mushroom, discovers a plurality of polypeptides with good DPPH free radical scavenging ability and oxidation injury human skin fibroblast protecting ability, determines the amino acid sequence of one polypeptide as DWPGFK through LC-MS/MS, and has the DPPH free radical scavenging rate of 73.58 percent+/-0.38 percent and Fe through the detection of antioxidant activity 2+ The chelating ability is 84.46 +/-1.32%, the reducing power is 0.42+/-0.01, and the preparation method has potential application prospects in the fields of preparing medicaments for removing free radicals, antioxidant injury health-care products, skin care products and the like by reducing ROS level, protecting cell membrane integrity, enhancing endogenous antioxidant enzymes (SOD and CAT), increasing glutathione peroxidase (GSH-PX) activity and reducing Malondialdehyde (MDA) content, playing the role of protecting the oxidative injury of HSF cells.
Drawings
FIG. 1 shows the separation of products Q1, Q2 by anion column.
FIG. 2 shows DPPH radical scavenging of isolated products Q1, Q2.
FIG. 3 shows the separation of the products G1, G2, G3, G4, G5 by means of gel columns.
FIG. 4 shows DPPH radical scavenging of isolated products G1, G2, G3, G4, G5.
FIG. 5 is a TIC profile of G3.
FIG. 6 is a secondary mass spectrum of an active polypeptide.
FIG. 7 is a prediction of the structure of an active polypeptide.
FIG. 8 shows the effect of different concentrations of DWPGFK on cell viability.
FIG. 9 is H 2 O 2 Induced HSF oxidative stress injury model.
FIG. 10 shows the concentration of DWPGFK versus H 2 O 2 Protection of damaged HSF cells.
FIG. 11 shows the concentration of DWPGFK versus H 2 O 2 Influence of SOD enzymatic activity in damaged HSF cells.
FIG. 12 shows the concentration of DWPGFK versus H 2 O 2 Influence of MDA content of injured HSF cells.
FIG. 13 shows the concentration of DWPGFK versus H 2 O 2 Influence of GSH-Px activity in injured HSF cells.
FIG. 14 shows the concentration of DWPGFK versus H 2 O 2 Effect of CAT content of damaged HSF cells.
Detailed Description
The invention will be described in further detail with reference to specific embodiments and drawings.
1. Measurement of antioxidant Activity:
DPPH Radical Scavenging Activity (DRSA): assays were performed with reference to the kit (purchased from suzhou grissin biotechnology limited).
2.Fe 2+ Chelation rate: reference (Ma Mengjiao. Preparation of antioxidant peptide of Carnis Trionycis and anti-aging function study [ D ]]Tin-free, university of Jiangnan 2020:1-68).
3. Measurement of reducing force: the reducing power of the samples was determined by the method of reference (Dong Y R, qi G H, yang Z P, et al preparation, separation and antioxidant properties of hydrolysates derived from Grifola frondosa protein [ J ]. Analytical and Bioanalytical Chemistry,2015,33 (6): 500-506).
Example 1
(1) Repeatedly washing straw mushroom fruiting bodies to remove impurities such as cultivation materials, draining water, freeze-drying, pulverizing into powder, and mixing with the double distilled water according to the mass ratio of 10:1, adding double distilled water to dissolve straw mushroom powder, standing for 4h, centrifuging at 8000r/min at 4 ℃ for 20min, taking supernatant, using 80% saturation according to an ammonium sulfate saturation table, adding ammonium sulfate into the supernatant, fully dissolving, standing for 12h, centrifuging to obtain precipitate, dissolving the precipitate in double distilled water, adding into a dialysis bag, placing into ultrapure water, dialyzing for 48h, and freeze-drying after the completion to obtain straw mushroom protein.
(2) Dissolving straw mushroom protein in double distilled water (substrate mass concentration is 3.11g/100 mL), adjusting pH and temperature to the optimal action condition of alkaline protease (purchased from Shanghai Meilin Biochemical technology Co., ltd., enzyme activity unit 250U/mg), balancing for 30min, addingAdding alkaline protease, performing enzymolysis for 3.7h, adding enzyme with an amount of 3.81% (the addition amount of alkaline protease accounts for the mass percent of straw mushroom protein), inactivating enzyme after enzymolysis, heating at 90deg.C for 15min to terminate reaction, centrifuging at 4deg.C for 15min at 8000r/min, collecting supernatant, and lyophilizing to obtain enzymolysis product. Separating and purifying the enzymolysis product sequentially with 10kDa and 3kDa ultrafiltration centrifuge tubes, and lyophilizing to obtain three polypeptide components with different molecular weights, wherein F1<3kDa，3kDa<F2<10kDa，F3>10kDa. The antioxidant activity (DPPH free radical scavenging Activity, fe) of three polypeptide components of different molecular weights were tested separately 2+ Chelating rate and reducing power), and the results are shown in table 1, and it can be seen from table 1 that the polypeptide component having the optimal antioxidant activity is F1.
TABLE 1 antioxidant Activity of three polypeptide Components of different molecular weights
Note that: the different letters represent significant differences (P < 0.05)
Note：Different lettcrs indicate significant difference(P＜0.05)
(3) The polypeptide fraction F1 was isolated and purified using a Q Sepharose FF (1 cm. Times.5 cm) anion exchange column coupled to the AKTA Pure system. Sample F1 was dissolved in Tris-HCl (20 mM pH 7.5) buffer, applied through a 0.22 μm microporous membrane, and the Q Sepharose FF anion column was equilibrated with Tris-HCl (20 mM pH 7.5) buffer. Elution was performed with a linear gradient of 1M NaCl (0-100%) in the same buffer at a flow rate of 1 mL/min. The elution process was monitored at 280nm and the results are shown in FIG. 1, showing two absorption peaks, with absorption peak 375 designated Q1 and absorption peak 50 designated Q2. DPPH radical scavenging activities of Q1 and Q2 were measured, respectively, and the results are shown in FIG. 2, which indicate that the antioxidant activity of component Q1 is highest.
Component Q1 was further purified using a Superdex 30 Increate10/300 GL gel column. Sample Q1 was dissolved in ultrapure water, passed through a microporous membrane of 0.22 μm, and applied to a column, the column was equilibrated with ultrapure water at a flow rate of 0.5mL/min, the column was eluted with the same mobile phase at room temperature at 0.5mL/min, the elution was monitored at 280nm, and 5 components were isolated, as shown in FIG. 3, the DPPH radical scavenging activities of G1, G2, G3, G4 and G5 were measured in the order named G1, G2, G3, G4 and G5 from the order named G3, G4 and G5 from the order named G3, G2, G3, G4 and G5, as shown in FIG. 4, were 32.77.+ -. 0.71%, 58.54.+ -. 1.45%, 68.98.+ -. 0.68%, 49.25.+ -. 0.65%, 42.77.+ -. 0.36% and the results showed that the antioxidant activity of G3 was the highest.
(4) G3 was separated using a Nano-HPLC liquid phase system UltiMate 3000RSL Cnano (ThermoFisher Scientific). Sample G3 was dissolved in ultrapure water, the sample was loaded by an autosampler and bound to a Trap column (100 μm. Times.20 mm, RP-C18, agilent), mobile phase A was a 0.1% formic acid-water solution, mobile phase B was a 0.1% formic acid-acetonitrile solution, and then separated by Analysis column (75 μm. Times.150 mm, RP-C18, new Objective) under the following conditions: mobile phase B:0-5min,5%;5-30min,5-38%;30-35min,38-95%, and flow rate of 300nL/min. Mass spectrometry was then performed by a Q-actual plus mass spectrometer (ThermoFisher Scientific), parent ion scan range: 350-2000m/z, and performing full scan acquisition spectrum under information dependent acquisition working mode (DDA, date Dependent Acquisition), wherein the TIC spectrum is shown in figure 5. The protein discover 2.1 software is used for analyzing the map, a plurality of antioxidant active peptides are identified and obtained, the amino acid composition and sequence of each antioxidant active peptide are determined, wherein the amino acid sequence of one antioxidant active peptide is DWPGFK, the mass spectrum of one antioxidant active peptide is shown as SEQ ID NO.1, the mass spectrum of one antioxidant active peptide is shown as fig. 6, and the molecular weight of one antioxidant active peptide is 748.9kDa.
(5) The performance of DWPGFK peptides was predicted by bioinformatics.
Bioactive peptide predictor PeptideRanker gives a score for DWPGFK peptides with an antioxidant activity score greater than 0.9. The physicochemical property of the obtained amino acid sequence DWPGFK was predicted in the peptderanker bioactive peptide prediction server: isoelectric point is between 5.55-5.84; amino acid residues with one positive charge and one negative charge; the stability is good; the predicted half-life of the reticulocyte in the mammal is 1.1h, the half-life in the yeast is 3min, and the half-life in the escherichia coli is more than 10h; is a hydrophilic polypeptide.
The safety of the obtained straw mushroom antioxidant peptide is evaluated in a PeptideRanker bioactive peptide prediction server, toxicity and sensitization of the straw mushroom antioxidant peptide are predicted, and the result shows that the straw mushroom antioxidant peptide is nontoxic and has no sensitization and higher safety.
(6) Obtaining DWPGFK peptide by adopting a solid phase synthesis method at a biological engineering limited company, and determining the antioxidant activity of the DWPGFK peptide, wherein the clearance rate of DPPH free radicals is 73.58% +/-0.38%; fe (Fe) 2+ The chelation rate is 84.46% + -1.32%; the reducing force is 0.42+/-0.01. The structure of the obtained straw mushroom antioxidant peptide is predicted by PepDraw, and the result is shown in figure 7.
Example 2
This example investigated the oxidative damage protection effect of straw mushroom antioxidant peptide DWPGFK on HSF cells.
1. Cell viability assay (MTT method)
(1) Main experimental reagent and equipment: MTT cell proliferation assay kit (BBI, E606334), fluorescence inverted microscope (olympus), and enzyme-labeled instrument (Thermo Fisher).
(2) The experimental steps are as follows:
1) Cell-free culture medium, PBS washing cells 3 times, 0.25% trypsin digestion of adherent cells.
2) Cell counting was performed with a cell counter, single cell suspensions were prepared and plated uniformly in 96-well plates at 2X 10 3 Cells/well, 100 μl/well.
3) The cells were cultured overnight, and different concentrations of drug were added and culture continued for 24h.
4) The 96-well plate was removed from the incubator, and fresh MTT solution (0.5 mg/mL), 10. Mu.L/well, was added to each well, and the culture was continued for 4 hours.
5) The 96-well plate was removed from the incubator, the supernatant was aspirated, and 100. Mu. L Formazan Solubilization Solution was added to each well.
6) The 96-well plate was gently shaken on a shaker for 10 minutes until complete dissolution of the formazan was observed under a common light microscope.
7) The absorbance was measured at 570nm in an enzyme-labeled immunoassay instrument.
To investigate the effect of polypeptides on HSF cell viability, the MTT assay was used. As shown in fig. 8, DWPGFK was 100%, 103.51%, 106.28%, 110.97%, 107.68%, 74.37%, 12.61% at mass concentrations of 0, 0.016, 0.8, 0.4, 2, 6, 10mg/mL, respectively, for 24h, with cells; the DWPGFK has the proliferation effect when the concentration is 0.016, 0.8, 0.4 and 2mg/mL for 24 hours, and the cell activity is higher than that of the control group by 100 percent. The volvariella volvacea antioxidant peptide has IC50=7.129 mg/mL for HSF cells.
2. Build H 2 O 2 Induced HSF oxidative stress injury model
(1) Cell culture media was discarded, cells were washed 3 times with PBS and adherent cells were digested with 0.25% trypsin.
(2) Cell counting was performed with a cell counter, single cell suspensions were prepared and plated uniformly in 96-well plates at 5X 10 3 Cells/well, 100 μl/well.
(3) The cells were cultured overnight at 1, 10, 50, 100, 250, 500, 1000mM H 2 O 2 Cells 1, 2, 3, 4h were treated separately.
(4) The 96-well plate was removed from the incubator, and fresh MTT solution (0.5 mg/mL), 10. Mu.L/well, was added to each well, and the culture was continued for 4 hours.
(5) The 96-well plate was removed from the incubator, the supernatant was aspirated, and 100. Mu. L Formazan Solubilization Solution was added to each well.
(6) The 96-well plate was gently shaken on a shaker for 10 minutes until complete dissolution of the formazan was observed under a common light microscope.
(7) The absorbance was measured at 570nm in an enzyme-labeled immunoassay instrument.
Cell proliferation inhibition (%) = (1-experimental absorbance/control absorbance) ×100%.
Test results are shown in FIG. 9, different H 2 O 2 The IC50 values for HSF cells cultured at different concentrations for different times were 1h (ic50= 531.1 μm), 2h (ic50=413.5 μm), 3h (ic50= 409.9 μm), 4h (ic50=242.8 μm), respectively.
3. Different concentrations of straw mushroom antioxidant peptide DWPGFK to H 2 O 2 Damaged (damaged)Protection of HSF cells.
Blank set (without sample and H 2 O 2 ) And control group (Add H only) 2 O 2 ) The experiment was performed according to the above experimental procedure.
The experimental results are shown in FIG. 10, in which DWPGFK was used as control, H 2 O 2 Treatment and H 2 O 2 After treatment, the cell viability was increased at 2mg/mL for DWPGFK at 0.5830, 0.2998, 0.2562, 0.3024, 0.3343, 0.4263, 0.2914, 0.1553U/mg, respectively, after addition of samples at concentrations of 0.016, 0.08, 0.4, 2, 6, 10mg/mL, respectively. This suggests that DWPGFK at a concentration of 2mg/mL can inhibit cell death due to oxidative stress.
4. Different concentrations of straw mushroom antioxidant peptide DWPGFK to H 2 O 2 Influence of SOD enzymatic activity in damaged HSF cells.
The measurement was carried out by the method of the kit for detecting total SOD activity (WST-8 method).
Percent inhibition= (a Blank control 1 －A Sample of )/(A Blank control 1 －A Blank control 2 )×100％。
As a result of the experiment, as shown in FIG. 11, the cells were treated with DWPGFK at different concentrations of 0.016, 0.08, 0.4, 2, 6, 10mg/mL, and the activities of intracellular SOD in the blank group, the control group and the sample group were 29.716 (blank), 8.3950 (control), 8.6547, 8.7983, 14.8333, 22.2610, 15.0703, 8.3497U/mg, respectively, according to the above experiment. DWPGFK can effectively inhibit the attack of ROS on SOD at the concentration of 2mg/mL, inhibit oxidative damage and protect cells.
5. Different concentrations of straw mushroom antioxidant peptide DWPGFK to H 2 O 2 Influence of MDA content of injured HSF cells.
Malondialdehyde (MDA) is a natural product of oxidation of lipids in living organisms. Lipid oxidation occurs when animal or plant cells develop oxidative stress (oxidative stress). Some fatty acids gradually decompose to a complex series of compounds, including MDA, after oxidation.
Measured as described in the lipid oxidation (MDA) assay kit.
As a result of the experiment, as shown in FIG. 12, the cells were treated with DWPGFK at different concentrations of 0.016, 0.08, 0.4, 2, 6, 10mg/mL, and the viability of intracellular MDA in the blank group, the control group and the sample group was 4.6817 (blank), 35.0277 (control), 36.8630, 33.6883, 34.3747, 17.7817, 32.9170, 36.5640U/mg, respectively, according to the above experiment. The DWPGFK can effectively inhibit oxidation reaction at the concentration of 2mg/mL, and has the least content of MDA compared with the control group, and the most obvious effect. This suggests that DWPGFK at a concentration of 2mg/mL can inhibit protection of cells from oxidative stress.
6. Different concentrations of straw mushroom antioxidant peptide DWPGFK to H 2 O 2 Influence of GSH-Px activity in injured HSF cells.
Glutathione peroxidase can scavenge peroxides in living cells, playing a key role in protecting cells from free radical damage. Intracellular lipids react readily with free radicals to produce lipid peroxides. Glutathione peroxidase can reduce lipid peroxides with reduced Glutathione (GSH), thereby eliminating the toxic effects of free radicals.
The detection was performed as described in the glutathione peroxidase (GSH-Px) detection kit (NADPH method).
As a result of the experiment, as shown in FIG. 13, the DWPGFK-treated cells were treated at different concentrations of 0.016, 0.08, 0.4, 2, 6, 10mg/mL, and the activity of GSH-Px in the cells of the blank group, the control group and the sample group was 143.4800 (blank), 64.9100 (control), 72.4557, 76.0607, 94.9537, 102.1840, 89.0887, 52.0400U/mg, respectively. The GSH-Px activity of DWPGFK was significantly increased at a concentration of 2mg/mL, indicating that DWPGFK could inhibit the protection of cells from oxidative stress at a concentration of 2 mg/mL.
7. Different concentrations of straw mushroom antioxidant peptide DWPGFK to H 2 O 2 Effect of CAT content of damaged HSF cells.
The detection is carried out according to the method in the catalase detection kit.
As a result of the experiment, as shown in FIG. 14, the cells were treated with DWPGFK at different concentrations of 0.016, 0.08, 0.4, 2, 6, 10mg/mL, and the activities of intracellular CAT in the blank group, the control group and the sample group were 5.1027 (blank), 3.2233 (control), 3.2857, 3.3997, 3.5010, 3.8850, 3.4517, 3.3093U/mg, respectively, according to the above experiment. CAT activity was improved at a concentration of 2mg/mL for DWPGFK compared with the other, which indicates that DWPGFK at a concentration of 2mg/mL can inhibit the protection of cells due to oxidative stress.
In summary, example 1 is a complete preparation process of straw mushroom antioxidant peptide DWPGFK. Example 2 the oxidative damage protection effect of straw mushroom antioxidant peptide DWPGFK on human skin fibroblast HSF was analyzed, and the change of the intracellular SOD, CAT, GSH-Px enzyme activity and MDA content was observed, and the oxidative damage protection effect on HSF cells was verified.
Claims (4)
1. The straw mushroom polypeptide for resisting skin oxidative damage is characterized in that the amino acid sequence is DWPGFK, namely Asp-Trp-Pro-Gly-Phe-Lys, and is shown as SEQ ID NO. 1.
2. Use of a straw mushroom polypeptide according to claim 1 for the preparation of a medicament for scavenging free radicals.
3. The use according to claim 1, wherein the free radical is DPPH.
4. The use of the straw mushroom antioxidant peptide according to claim 1 in the preparation of skin care products or health care products for resisting skin oxidative damage.
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