CN112898383A - Oligopeptide, active peptide composition and application of oligopeptide and active peptide composition in preparation of product with anti-inflammatory effect - Google Patents
Oligopeptide, active peptide composition and application of oligopeptide and active peptide composition in preparation of product with anti-inflammatory effect Download PDFInfo
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- 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
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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
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/164—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
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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
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- 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
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
Abstract
The invention relates to the technical field of biomedicine, and particularly discloses an oligopeptide, an active peptide composition and application thereof in preparation of a product with an anti-inflammatory effect. The oligopeptide has a structure shown in a formula I. The active peptide composition comprises oligopeptide with a structure shown in a formula I and active cyclic peptide with a structure shown in a formula II; experiments show that the oligopeptide bifidobacterium oligopeptide-alpha and the active peptide saccharomyces cerevisiae cyclic peptide-beta can inhibit HaCaT cell inflammatory injury and apoptosis caused by LPS exposure. Therefore, the bifidobacterium oligopeptide-alpha, the saccharomyces cerevisiae cyclic peptide-beta and the composition thereof can be used as active substances in cosmetics, skin care products, foods, health care products or medicines to play a role in resisting inflammation.
Description
Technical Field
The invention relates to the technical field of biomedicine, in particular to an oligopeptide, an active peptide composition and application thereof in preparation of products with anti-inflammatory effects.
Background
Inflammation is an adaptive response induced by various external stimuli, is one of the most basic protective responses of normal organisms and cells to foreign bodies such as pathogens, viruses and the like, is the basis of various physiological and pathological processes, and can be generated in tissues with infection, trauma, toxicity or autoimmune injury. The inflammatory process is also the first step in the immune response to toxins, invading pathogens and allergens, as well as damaged tissues.
The skin is the largest protective organ of the human body, and as the interface between the human body and the environment, the skin forms a strong barrier against external stimuli. In inflammatory diseases where barrier functions such as atopic dermatitis, aging, and dry skin are impaired, the skin provides a first line of immune protection against infection, and thus, it is very important to enhance the barrier protection function of the skin. The immune response of the skin is crucial for the host to fight pathogenic microorganisms, but immune dysregulation can lead to chronic inflammation of the skin, resulting in sustained cell damage and various skin diseases.
Lipopolysaccharide (LPS) is a component of the outer wall of the cell wall of gram-negative bacteria, and is a substance composed of lipids and polysaccharides; after the lipopolysaccharide enters the body, the organism can be caused to generate inflammatory reaction; however, there are many causes for inducing cell inflammation, and most of the anti-inflammatory drugs do not have cell inflammatory damage caused by anti-Lipopolysaccharide (LPS).
Therefore, it is of great significance to develop a drug having an effect of resisting cell inflammatory injury caused by Lipopolysaccharide (LPS).
Disclosure of Invention
In view of the above, the present invention provides an oligopeptide and an active peptide composition with a completely new structure, and further studies show that the oligopeptide and the active peptide composition have the effect of resisting cell inflammatory injury caused by Lipopolysaccharide (LPS).
The detailed technical scheme of the invention is as follows:
in a first aspect, the present invention provides an oligopeptide having the structure shown in formula i:
the active cyclic peptide with the structure shown as the formula I is named as bifidobacterium oligopeptide-alpha (abbreviated as HT-1); the amino acid sequence is Phe-Ser-Thr-His-Gly-Gly (shown as SEQ ID No. 1).
The bifidobacterium oligopeptide-alpha can be separated from bifidobacterium; can also be prepared according to the methods in the examples.
In a second aspect, the invention provides an active peptide composition, which comprises an oligopeptide with a structure shown in formula I and an active cyclic peptide with a structure shown in formula II;
the active cyclic peptide with the structure shown in the formula II is named as saccharomyces cerevisiae cyclic peptide-beta (abbreviated as DF-1); the amino acid sequence is Cycle- [ Trp-Leu-His-Val ]. The acyclic linear amino acid sequence can be the amino acid sequence shown as SEQ ID No.2 in the sequence table.
The saccharomyces cerevisiae cyclopeptide-beta can be obtained by separating saccharomyces cerevisiae; can also be prepared according to the methods in the examples.
Preferably, the molar ratio of the oligopeptide with the structure shown in the formula I to the active cyclic peptide with the structure shown in the formula II is 1-8: 1-8.
Further preferably, the molar ratio of the oligopeptide with the structure shown in the formula I to the active cyclic peptide with the structure shown in the formula II is 1-3: 1-3.
In a third aspect, the invention provides the use of an oligopeptide or an active peptide composition in the preparation of a product having anti-inflammatory properties.
Preferably, the oligopeptide or active peptide composition is used for preparing a product with the effect of resisting cell inflammatory injury caused by Lipopolysaccharide (LPS).
Preferably, the product is a cosmetic, a skin care product, a food, a health product or a medicament.
Further preferably, the cosmetic or skin care product comprises an emulsion, a cream, a gel, a water, an oil, a powder or a mask.
Further preferably, the food, health product or pharmaceutical is in the form of a tablet, capsule, powder, granule, pill, syrup, solution, suspension or aerosol.
Has the advantages that: the invention provides a bifidobacterium oligopeptide-alpha with a brand-new structure; experiments show that the bifidobacterium oligopeptide-alpha and the saccharomyces cerevisiae cyclic peptide-beta can inhibit HaCaT cell inflammatory injury and apoptosis caused by LPS exposure; and the activity of the saccharomyces cerevisiae cyclopeptide-beta is superior to that of bifidobacterium oligopeptide-alpha. Because the activity of the saccharomyces cerevisiae cyclic peptide-beta is better than that of the bifidobacterium oligopeptide-alpha, the active peptide composition formed by the saccharomyces cerevisiae cyclic peptide-beta and the bifidobacterium oligopeptide-alpha is further provided, so that the activity of the bifidobacterium oligopeptide-alpha is improved. According to the above activities: the bifidobacterium oligopeptide-alpha, the saccharomyces cerevisiae cyclic peptide-beta and the composition thereof have the function of resisting cell inflammatory injury caused by Lipopolysaccharide (LPS); therefore, the bifidobacterium oligopeptide-alpha, the saccharomyces cerevisiae cyclic peptide-beta and the composition thereof can be used as active substances in cosmetics, skin care products, foods, health care products or medicines to play a role in resisting inflammation. In addition, the bifidobacterium oligopeptide-alpha and the saccharomyces cerevisiae cyclic peptide-beta can be separated from bifidobacterium and saccharomyces cerevisiae, and the sources are rich; the bifidobacterium oligopeptide-alpha and the saccharomyces cerevisiae cyclic peptide-beta are small molecular compounds, the preparation process is simple, the operation is convenient, and the prepared bifidobacterium oligopeptide-alpha and the prepared saccharomyces cerevisiae cyclic peptide-beta have high purity, so that the application of the bifidobacterium oligopeptide-alpha and the prepared saccharomyces cerevisiae cyclic peptide-beta in foods, medicines, health-care products and cosmetics is facilitated.
Drawings
In order to more clearly illustrate the embodiments of the present invention or the technical solutions in the prior art, the drawings used in the description of the embodiments or the prior art will be briefly described below, it is obvious that the drawings in the following description are only drawings of some embodiments of the present invention, and for those skilled in the art, other drawings can be obtained according to these drawings without creative efforts.
FIG. 1 is a mass spectrum of HT-1.
FIG. 2 is a graph showing the results of high performance liquid chromatography measurement of HT-1.
FIG. 3 is a mass spectrum of DF-1.
FIG. 4 is a graph showing the results of high performance liquid chromatography measurement of DF-1.
FIG. 5 is a graph showing the results of the inhibition of LPS-induced HaCaT cell inflammatory cytokine and adhesion molecule expression by HT-1 and DF-1. Wherein FIG. 5A is a graph showing the effect of concentrations of HT-1 and DF-1 on cell viability; FIG. 5B is a graph showing the results of experiments in which HT-1 and DF-1 inhibit secretion of IL-6, IL-8, TNF- α, IL-1 β induced by LPS stimulation; FIG. 5C is a graph showing the effect of HT-1 and DF-1 on LPS-induced expression of ICAM-1 and VCAM-1.
FIG. 6 is a graph showing the results of experiments on the inhibition of LPS-induced HaCaT apoptosis by HT-1 and DF-1. Wherein, FIG. 6A is a graph showing the experimental results of the effect of HT-1 and DF-1 on the secretion of NO and PGE2 by HaCaT cells; FIG. 6B is a graph showing the experimental results of the effect of HT-1 and DF-1 on the expression of iNOS and COX-2 by HaCaT cells; FIG. 6C is a graph showing the results of an apoptosis test of HT-1 and DF-1 on HaCaT cells.
FIG. 7 is a graph showing the results of experiments in which HT-1 and DF-1 inhibit LPS-induced NF-. kappa.B signaling in HaCaT cells and activation of NLRP3 inflammasome. Wherein FIG. 7A is a graph showing the experimental results of HT-1 and DF-1 on the NF-. kappa.B signaling pathway in HaCaT cells; wherein FIG. 7B is a graph showing the results of an experiment of activation of NLRP3 by HT-1 and DF-1 on inflammatory bodies.
Detailed Description
The technical solution of the present invention will be clearly and completely described with reference to the following examples. It is to be understood that the described embodiments are merely exemplary of the invention, and not restrictive of the full scope of the invention. All other embodiments, which can be derived by a person skilled in the art from the embodiments given herein without making any creative effort, shall fall within the protection scope of the present invention.
Example 1 isolation of Bifidobacterium oligopeptide-alpha and Saccharomyces cerevisiae cyclopeptide-beta
Uniformly mixing 50g of bifidobacterium with 500mL of ethyl acetate and 2000mL of water, carrying out ultrasonic treatment for 20min, standing, extracting to obtain an aqueous phase layer, repeating the extraction process for multiple times, carrying out vacuum low-temperature freeze drying on the aqueous phase layer, and carrying out preparative HPLC (high performance liquid chromatography) to prepare and separate the oligopeptide-alpha (HT-1) of the bifidobacterium.
Uniformly mixing 50g of the saccharomyces cerevisiae with 500mL of ethyl acetate and 2000mL of water, carrying out ultrasonic treatment for 20min, standing, extracting to obtain an aqueous phase layer, repeating the extraction process for multiple times, carrying out vacuum low-temperature freeze-drying on the aqueous phase layer, and carrying out preparative separation by using preparative HPLC to obtain the saccharomyces cerevisiae cyclic peptide-beta (DF-1).
The preparation conditions of the preparative HPLC were as follows: taking 0.1% trifluoroacetic acid water solution as a mobile phase A, taking 0.1% trifluoroacetic acid acetonitrile solution as the mobile phase A, wherein the ratio of the mobile phase A: the mobile phase B was 50:50, and the measurement wavelength was 310. mu.m. As can be seen from FIGS. 2 and 4, the peak-off times of Bifidobacterium oligopeptide-alpha (HT-1) and Saccharomyces cerevisiae cyclic peptide-beta (DF-1) are 11.203min and 12.458min, respectively.
Example 2 chemical Synthesis of Bifidobacterium oligopeptide-alpha (HT-1) and Saccharomyces cerevisiae cyclopeptide-beta (DF-1)
(1) Placing 100mg of Fmoc-Tyr Wang Resin in a solid phase synthesis tube, adding N, N-Dimethylformamide (DMF), standing for 30 minutes to fully swell the Resin, filtering out the solvent, adding piperidine DMF solution, oscillating, and filtering out the solvent. Dissolving Fmoc-Ser-OH, 1-hydroxybenzotriazole and O-benzotriazol-tetramethylurea hexafluorophosphate in DMF, adding N, N-diisopropylethylamine, uniformly mixing, protecting from light, activating, adding into resin, stirring for 2 hours at 25 ℃ under the action of nitrogen blowing, carrying out suction filtration, washing with DMF and dichloromethane in sequence, and drying the solvent. Repeating the steps, sequentially adding activated Fmoc-Leu-OH, Fmoc-His-OH, Fmoc-Leu-OH, Fmoc-His-OH and Fmoc-Gly-OH into resin, stirring under the action of nitrogen blowing at 25 ℃, washing the resin after complete reaction, carrying out rotary evaporation on the obtained filtrate to obtain a precipitate, and carrying out freeze drying to obtain the bifidobacterium oligopeptide-alpha (HT-1), wherein the amino acid sequence of the bifidobacterium oligopeptide-alpha is Tyr-Ser-Leu-His-Leu-His-Gly.
(2) 100mg of Fmoc-Trp Wang Resin is put in a solid phase synthesis tube, N-Dimethylformamide (DMF) is added, then the mixture is kept stand for 30 minutes to fully swell the Resin, the solvent is filtered out, piperidine DMF solution is added, and the solvent is filtered out after oscillation. Dissolving Fmoc-Leu-OH, 1-hydroxybenzotriazole and O-benzotriazol-tetramethylurea hexafluorophosphate in DMF, adding N, N-diisopropylethylamine, uniformly mixing, protecting from light, activating, adding into resin, stirring for 2 hours at 25 ℃ under the action of nitrogen blowing, carrying out suction filtration, washing with DMF and dichloromethane in sequence, and drying the solvent. Repeating the steps, sequentially adding activated Fmoc-His-OH and Fmoc-Val-OH into resin, stirring for 2 hours at 25 ℃, washing the resin after complete reaction to obtain crude peptide X-1, cutting the resin from the X-1 by using a TFA solution to obtain a free-OH end, steaming solids obtained by removing the TFA by reduced pressure at 40 ℃ in a water bath, adding the solids into ethyl acetate, mixing the solids with equimolar amount of p-nitrophenol, preparing p-nitrophenol active ester X-2 by using DCC as a condensing agent, removing the protecting group Fmoc of the X-2 by using a piperidine DMF solution, dissociating an N end, removing redundant solvent to obtain crude peptide solids, and adding Na alkali2CO310 is prepared from solvent dioxane-3-10-4Diluting the solution, reacting at 25 deg.C for 5 hr, removing solvent by rotary evaporation at 40 deg.C in organic phase water bath, and freeze drying to obtain Saccharomyces cerevisiae cyclic peptide-beta (DF-1) with amino acid sequence of Cycle- [ Trp-Leu-His-Val]。
Measuring the bifidobacterium oligopeptide-alpha (HT-1) and the saccharomyces cerevisiae cyclic peptide-beta (DF-1) by using a mass spectrum, wherein the mass spectrum measurement conditions comprise ESI positive ion mode capillary voltage of 3kV, taper hole voltage of 50V, extraction voltage of 5V, desolvation temperature of 350 ℃ and atomized gas flow of 350L/h; the high performance liquid chromatography measurement conditions were that a Boston Green ODS-AQ chromatographic column (250 × 4.6mm) was used, a 0.1% aqueous trifluoroacetic acid solution was used as a mobile phase a, a 0.1% acetonitrile solution of trifluoroacetic acid was used as a mobile phase a, and the mobile phase a: the mobile phase B was 50:50, the flow rate was 1mL/min, the detection wavelength was 310 μm, and the sample size was 10 μ L.
From the mass spectral data (see FIG. 1), 826.4213 is [ M + H]+Ion, 751.3910 is y6 ion, 614.3317 is y5 ion, 501.2470 is y4 ion, 463.2436 is b4 ion, 251.1508 is y2 ion, 213.0988 is b2 ion, 110.0712 is [ His-COOH + H]+Ion, and the amino acid sequence of bifidobacterium oligopeptide-alpha (HT-1) is Tyr-Ser-Leu-His-Leu-His-Gly which is the structure shown in the formula I and can be determined from the mass spectrogram shown in figure 1;
from the mass spectral data (see FIG. 3), 536.2996 is [ M + H]+Ion, 437.2296 is [ M-Val + H2O+H]+Ion, 419.2199 is [ M-Leu + H2O+H]+Ion, 300.1713 is [ Trp-Leu-2H2O+H]+Ion, 251.1502 is [ Leu-His-2H2O+H]+Ion, 159.0919 is [ Trp-COOH + H]+Ion, 110.0720 is [ His-COOH + H]+Ion, 86.0981 is [ Leu-COOH + H]+Ions. Finally, the amino acid sequence of the saccharomyces cerevisiae cyclopeptide-beta (DF-1) can be determined to be Cycle- [ Trp-Leu-His-Val]Namely the structure shown in formula II.
Examples of the experiments
To evaluate the biological activities of the bifidobacterium oligopeptide-alpha (HT-1) and the saccharomyces cerevisiae cyclopeptide-beta (DF-1) and combinations thereof of the present invention, the following effect examples were performed.
Culturing HaCaT cells of immortalized keratinocyte cell line in a cell culture box at 37 ℃ and 5% CO2(DMEM medium). LPS concentration is 1 μ M for 12h, after the completion, PBS is used for washing cells, PBS is removed, DMEM culture medium or culture medium containing HT-1 or DF-1(20 μ M) is added again for further 24 h. The CCK8 method is used for detecting cell viability and collecting cells and culture solution.
In the test of the effect of HT-1 or DF-1 on HaCaT cell viability, the experiments were divided into 4 groups: normal Control group (Control); a LPS group; HT-120. mu.M group (LPS + HT-120. mu.M); DF-120. mu.M group (LPS + DF-120. mu.M). Each treatment condition was replicated 3 times in 3 wells and the experiment was repeated 3 times. The normal control group received no LPS stimulation, and the LPS group, HT-120. mu.M group and DF-120. mu.M group received LPS stimulation, respectively. CCK8 measures cell viability.
The experiments were divided into 4 groups: normal Control group (Control); a LPS group; HT-120. mu.M group (LPS + HT-120. mu.M); DF-120. mu.M group (LPS + DF-120. mu.M). Each treatment condition was replicated 3 times in 3 wells and the experiment was repeated 3 times. The normal control group received no LPS stimulation, and the LPS group, HT-120. mu.M group and DF-120. mu.M group received LPS stimulation, respectively. After HaCaT cells are treated according to experimental design, collecting the cells and cell supernatant; detecting the level of IL-6, IL-8, TNF-alpha, IL-1 beta with reference to the ELISA kit instructions; and (5) detecting the content change condition of the MMPs by referring to the operation instruction of the ELISA kit.
After the HaCaT cells were processed as designed, the cells were collected and centrifuged at 2000g for 3min at room temperature. Cells were suspended in pre-cooled 1 × PBS, centrifuged at 2000g for 3min, and the cells washed. Annexin V-FITC/PI double staining experiments were performed according to the manufacturer's instructions. Apoptosis was detected by flow cytometry and all experiments were repeated at least 3 times.
After the HaCaT cells were treated according to the experimental design, the cells were collected, washed 2 times with precooled PBS, added with 50 μ L of cell lysate, and left to stand at 4 ℃ for 30 min. Centrifuging at 10000r/min for 15min, taking supernatant to extract total protein, and performing protein quantification by using a BCA method. Total proteins were separated by SDS-PAGE and transferred to PVDF membrane. Blocking with 5% skimmed milk powder at room temperature for 2 h. The primary antibody was then added, shaken gently overnight at 4 ℃, washed 3 times with TBST, the corresponding secondary antibody was added, incubated 1h at room temperature, and rinsed 3 times.
The experimental results are as follows:
as can be seen from the data of the experimental results in FIG. 5A, the concentration of HT-1 and DF-1 below 1250. mu.M has a significant effect on the cell viability. As shown in FIG. 5B, compared with the Control group, secretion of IL-6, IL-8, TNF- α, IL-1 β by HaCaT was significantly increased by LPS stimulation, while secretion of IL-6, IL-8, TNF- α, IL-1 β induced by LPS stimulation was greatly inhibited by HT-1 and DF-1; as shown in FIG. 5C, expression of ICAM-1 and VCAM-1 was induced by LPS stimulation. To investigate the effect of HT-1 and DF-1 on the expression of ICAM-1 and VCAM-1 induced by LPS, we examined the effect of HT-1 and DF-1 on the expression of ICAM-1 and VCAM-1 induced by LPS. The results show that the stimulation of LPS leads ICAM-1 and VCAM-1 expression of HaCaT cells to be obviously increased, and HT-1 and DF-1 can inhibit the expression of ICAM-1 and VCAM-1 induced by LPS.
As shown in FIG. 6A, LPS stimulation resulted in a significant increase in cellular NO and PGE2 secretion, while HT-1 and DF-1 treatment resulted in significant inhibition of HaCaT cell NO and PGE2 secretion. Further, as shown in FIG. 6B, the expression of iNOS and COX-2 in HaCaT cells was significantly increased by LPS stimulation, while the expression of iNOS and COX-2 in HaCaT cells was significantly inhibited by LPS stimulation after HT-1 and DF-1 treatment. As shown in FIG. 6C, LPS stimulation resulted in increased apoptosis, while HaCaT apoptosis rate was significantly decreased after HT-1 and DF-1 treatment. Therefore, HT-1 and DF-1 can play an anti-inflammatory activity and a protective role by relieving HaCaT cell apoptosis induced by LPS stimulation.
As shown in FIG. 7A, LPS stimulation significantly up-regulated the expression of p-IKK-alpha, p-IKK-beta and p-IkB, while HT-1 and DF-1 treatment significantly inhibited the expression of p-IKK-alpha, p-IKK-beta and p-IkB by LPS stimulation, indicating that HT-1 and DF-1 inhibited HaCaT cell inflammatory injury by LPS stimulation by inhibiting NF-kB signaling pathway activation.
Further, as shown in fig. 7B, LPS stimulation significantly upregulated the expression of NLRP3, ASC, and Caspase-1, suggesting that LPS exposure significantly activated NLRP3 inflammasome, leading to inflammatory injury. While HT-1 and DF-1 treatment obviously inhibits the expression of NLRP3, ASC and Caspase-1 caused by LPS stimulation, which indicates that HT-1 and DF-1 inhibit HaCaT cell inflammatory injury caused by LPS stimulation by inhibiting the activation of NLRP3 inflammatory bodies.
The above-mentioned mechanism experimental results show that: bifidobacterium oligopeptide-alpha (HT-1) and Saccharomyces cerevisiae cyclic peptide-beta (DF-1) can inhibit HaCaT cell inflammatory injury and apoptosis caused by LPS exposure; and the action of the saccharomyces cerevisiae cyclic peptide-beta (DF-1) is superior to that of bifidobacterium oligopeptide-alpha (HT-1). Therefore, the bifidobacterium oligopeptide-alpha, the saccharomyces cerevisiae cyclic peptide-beta and the combination thereof have the function of resisting cell inflammatory injury caused by Lipopolysaccharide (LPS).
While the invention has been described with reference to a preferred embodiment, it will be understood by those skilled in the art that various changes in form and detail may be made therein without departing from the spirit and scope of the invention.
Sequence listing
<110> Shenzhen sea-invasive Biotech Limited
<120> oligopeptide, active peptide composition and application thereof in preparation of products with anti-inflammatory effect
<160> 2
<170> SIPOSequenceListing 1.0
<210> 1
<211> 6
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 1
Phe Ser Thr His Gly Gly
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<210> 2
<211> 4
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 2
Trp Leu His Val
1
Claims (8)
1. An oligopeptide, characterized by having the structure of formula i:
2. the method for producing an oligopeptide according to claim 1, wherein the oligopeptide is isolated from Bifidobacterium.
3. An active peptide composition is characterized by comprising an oligopeptide with a structure shown in a formula I and an active cyclic peptide with a structure shown in a formula II;
4. the active peptide composition of claim 3, wherein the molar ratio of the oligopeptide with the structure shown in formula I to the active cyclic peptide with the structure shown in formula II is 1-8: 1-8.
5. The active peptide composition of claim 3, wherein the molar ratio of the oligopeptide with the structure shown in formula I to the active cyclic peptide with the structure shown in formula II is 1-3: 1-3.
6. Use of the oligopeptide or active peptide composition according to any one of claims 1 to 5 in the preparation of a product having anti-inflammatory effect.
7. Use of the oligopeptide or active peptide composition according to any one of claims 1 to 3 in the preparation of a product having an effect of resisting inflammatory injury of cells caused by Lipopolysaccharide (LPS).
8. Use according to claim 6 or 7, wherein the product is a cosmetic, skin care, food, health product or pharmaceutical.
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| CN112979749A (en) * | 2021-02-26 | 2021-06-18 | 深圳海创生物科技有限公司 | Active cyclic peptide, active cyclic peptide composition and application of active cyclic peptide composition in preparation of products with antioxidation or anti-aging effects |
| CN114409730A (en) * | 2021-12-24 | 2022-04-29 | 深圳科兴药业有限公司 | Active peptide, active peptide composition and application of active peptide composition in preparation of product with anti-aging effect |
| CN114456230A (en) * | 2021-12-24 | 2022-05-10 | 深圳科兴药业有限公司 | Probiotic active peptide, active peptide composition and application of probiotic active peptide and active peptide composition in preparation of products with anti-inflammatory effect |
| CN115581633A (en) * | 2022-10-14 | 2023-01-10 | 深圳市维琪医药研发有限公司 | Novel use of peptide compounds in preparation of composition for skin aging repair |
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| CN114409730A (en) * | 2021-12-24 | 2022-04-29 | 深圳科兴药业有限公司 | Active peptide, active peptide composition and application of active peptide composition in preparation of product with anti-aging effect |
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