CN116925178A - Active peptide, composition and application thereof in preparation of product with effect of reducing fine lines and/or wrinkles - Google Patents
Active peptide, composition and application thereof in preparation of product with effect of reducing fine lines and/or wrinkles Download PDFInfo
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- CN116925178A CN116925178A CN202310743008.6A CN202310743008A CN116925178A CN 116925178 A CN116925178 A CN 116925178A CN 202310743008 A CN202310743008 A CN 202310743008A CN 116925178 A CN116925178 A CN 116925178A
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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
- 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
- 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)
- Dermatology (AREA)
- Organic Chemistry (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Epidemiology (AREA)
- Engineering & Computer Science (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Biophysics (AREA)
- Birds (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention relates to the technical field of biological medicines, and particularly discloses an active peptide, a composition and application thereof in preparation of a product with fine line and/or wrinkle fading effect. The active peptide has an amino acid sequence shown as SEQ ID NO. 1, SEQ ID NO. 2 or SEQ ID NO. 3; wherein, the amino acid sequence of SEQ ID NO. 1 is: ala-Glu-Phe-Gly-His; the amino acid sequence of SEQ ID NO. 2 is: glu-Phe-Ala-Glu-His; the amino acid sequence of SEQ ID NO. 3 is: his-Glu-Ala-Phe-Gly. Research shows that the active peptide and the composition composed of the active peptide and gamma-aminobutyric acid can effectively promote the generation of skin collagen and laminin; while also being capable of inhibiting the activity of Matrix Metalloproteinases (MMP), such as MMP-1, MMP3 and/or MMP-9), or the expression of enzymes; and can further reduce or even eliminate skin fine lines or wrinkles.
Description
Technical Field
The invention relates to the technical field of biological medicines, in particular to an active peptide, a composition and application thereof in preparing a product with fine line and/or wrinkle reducing effect.
Background
Natural aging of the skin, photoaging, facial expression, etc. are three major factors that cause facial wrinkles to occur. With the aging, ultraviolet irradiation, collagen synthesis capacity is reduced, collagen fiber is degraded, elasticity is lost, and the like, so that the formation of fine wrinkles and cracks on the face is increased. Facial expressions can also cause repetitive muscle contraction and accumulation of various facial wrinkles such as fish tail lines, intereyebrow lines, dimpled chin, smile lifting lines, forehead lines, nose and lip lines, lip lines and the like.
In order to delay skin aging and reduce wrinkles, some natural active factors are added into skin care products to promote skin cell proliferation and promote synthesis of collagen, elastic fibers and the like. In addition, injectable neuromodulators, such as muscle relaxants/inhibitors of muscle contraction, are effective in reducing dynamic wrinkles. Although the injectable neuromodulation has remarkable effects, various other problems such as anaphylaxis, injection site reactions (congestion, bleeding, pain, redness, swelling or tenderness) or muscle stiffness are easily induced, and serious problems such as difficulty in speaking, muscle weakness, ptosis and the like are even caused by serious patients. The chemical composition also has the disadvantages of skin irritation, potential anaphylactic reaction and the like in the aspects of inhibiting skin wrinkles and the like.
Currently, there are numerous attempts to improve the visual appearance of skin, such as wrinkles, fine lines, etc.; but it has at least one of the following drawbacks: such as high cost, high medical risk, skin irritation, poor effect, etc. Therefore, the continued development of more active ingredients with fine line and/or wrinkle reducing effects has significant utility.
Disclosure of Invention
In order to overcome at least one technical problem existing in the prior art, the invention provides an active peptide and a composition.
The technical scheme of the invention is as follows:
the invention firstly provides an active peptide which has an amino acid sequence shown as SEQ ID NO. 1, SEQ ID NO. 2 or SEQ ID NO. 3;
wherein, the amino acid sequence of SEQ ID NO. 1 is: ala-Glu-Phe-Gly-His;
the amino acid sequence of SEQ ID NO. 2 is: glu-Phe-Ala-Glu-His;
the amino acid sequence of SEQ ID NO. 3 is: his-Glu-Ala-Phe-Gly.
The inventors have surprisingly found in the study that: the active peptide of the amino acid sequence shown in SEQ ID NO. 1, the active peptide of the amino acid sequence shown in SEQ ID NO. 2 and the active peptide of the amino acid sequence shown in SEQ ID NO. 3 can effectively promote the generation of skin collagen and laminin.
The active peptide of the amino acid sequence shown in SEQ ID NO. 1, the active peptide of the amino acid sequence shown in SEQ ID NO. 2 and the active peptide of the amino acid sequence shown in SEQ ID NO. 3 can also inhibit the activity of Matrix Metalloproteinases (MMP), such as MMP-1, MMP3 and/or MMP-9, or the expression of enzymes; and can further reduce or even eliminate skin fine lines or wrinkles.
The invention also provides a composition which is selected from two or more than two active peptides with the amino acid sequences shown in SEQ ID NO. 1, SEQ ID NO. 2 or SEQ ID NO. 3.
Preferably, the composition further comprises gamma-aminobutyric acid.
Further preferably, the composition comprises gamma-aminobutyric acid and active peptides of the amino acid sequences shown in SEQ ID NO. 1, SEQ ID NO. 2 and SEQ ID NO. 3.
The inventors have surprisingly found in further studies that a composition obtained by combining gamma-aminobutyric acid with an active peptide of the amino acid sequence shown in SEQ ID NO. 1, an active peptide of the amino acid sequence shown in SEQ ID NO. 2 and an active peptide of the amino acid sequence shown in SEQ ID NO. 3, has significantly improved skin collagen and laminin production compared with gamma-aminobutyric acid alone, an active peptide of the amino acid sequence shown in SEQ ID NO. 1, an active peptide of the amino acid sequence shown in SEQ ID NO. 2 or an active peptide of the amino acid sequence shown in SEQ ID NO. 3; has more excellent effect of promoting skin collagen and laminin generation.
Meanwhile, the inventor also discovers that the activity or the expression effect of the composition obtained by combining gamma-aminobutyric acid with the active peptide of the amino acid sequence shown in SEQ ID NO. 1, the active peptide of the amino acid sequence shown in SEQ ID NO. 2 and the active peptide of the amino acid sequence shown in SEQ ID NO. 3 is also obviously improved compared with that of the single gamma-aminobutyric acid, the active peptide of the amino acid sequence shown in SEQ ID NO. 1, the active peptide of the amino acid sequence shown in SEQ ID NO. 2 or the active peptide of the amino acid sequence shown in SEQ ID NO. 3; has more excellent effect of inhibiting the activity or expression of matrix metalloproteinase.
Still more preferably, the mass ratio of the active peptides of the amino acid sequences shown in SEQ ID NO:1, SEQ ID NO:2 and SEQ ID NO:3 is 1 (1-50): 1-50.
Still more preferably, the mass ratio of the active peptides of the amino acid sequences shown in SEQ ID NO:1, SEQ ID NO:2 and SEQ ID NO:3 is 1 (10-15): 20-30): 5-10.
Most preferably, the mass ratio of the active peptides of the amino acid sequences shown in SEQ ID NO:1, SEQ ID NO:2 and SEQ ID NO:3 is 1:11.6:23.7:9.8.
The invention also provides application of the active peptide or the composition in preparation of products with the effect of inhibiting the activity or the expression of extracellular matrix metalloproteinase.
Most preferably, the extracellular matrix metalloproteinase is matrix metalloproteinase 1, matrix metalloproteinase 3, and/or matrix metalloproteinase 9.
The invention also provides application of the active peptide or the composition in preparing products with fine line and/or wrinkle reducing effect.
The invention also provides application of the active peptide or the composition in preparing a product with the effect of promoting the generation of skin collagen and/or laminin.
Preferably, the product is a skin care product or a pharmaceutical product.
The beneficial effects are that: the invention provides a brand new active peptide; studies show that the active peptide with the amino acid sequence shown in SEQ ID NO. 1 (hereinafter referred to as active oligopeptide-1), the active peptide with the amino acid sequence shown in SEQ ID NO. 2 (hereinafter referred to as active oligopeptide-2) and the active peptide with the amino acid sequence shown in SEQ ID NO. 3 (hereinafter referred to as active oligopeptide-3), and the composition formed by the active peptide and gamma-aminobutyric acid can effectively promote the generation of skin collagen and laminin; while also being capable of inhibiting the activity of Matrix Metalloproteinases (MMP), such as MMP-1, MMP3 and/or MMP-9), or the expression of enzymes; and can further reduce or even eliminate skin fine lines or wrinkles. Furthermore, the active peptide or the composition provided by the invention is used as an active ingredient, and has important application value in preparing skin care products or medicines with corresponding functions.
Drawings
FIG. 1 shows the HPLC detection spectrum of active oligopeptide-1.
FIG. 2 is a mass spectrum of active oligopeptide-1.
FIG. 3 is a HPLC chromatogram of active oligopeptide-2.
FIG. 4 is a mass spectrum of active oligopeptide-2.
FIG. 5 is a HPLC chromatogram of active oligopeptide-3.
FIG. 6 is a mass spectrum of active oligopeptide-4.
FIG. 7 is a graph showing experimental results of the effect of the active peptides and compositions of the present invention on the activity and expression of matrix metalloproteinases in fibroblasts.
FIG. 8 is a graph showing the experimental results of the effect of the reactive peptides and compositions of the present invention on the ROS content of fibroblasts and the content of collagen, laminin, etc.
Detailed Description
The technical scheme of the present invention will be clearly and completely described in the following examples. It will be apparent that the described embodiments are only some, but not all, embodiments of the invention. All other embodiments, which can be made by those skilled in the art based on the embodiments of the invention without making any inventive effort, are intended to be within the scope of the invention.
EXAMPLE 1 preparation method of the active peptide of the present invention
The method comprises the following steps:
(1) normal culture of Human Dermal Fibroblasts (HDF);
(2) samples of facial flora collected from different healthy children are respectively added into culture medium (culture medium: peptone 6.0g/L, yeast powder 6.0g/L, glucose 8.0g/L, sodium acetate 3.0g/L, dipotassium hydrogen phosphate 1.0g/L, magnesium sulfate 0.2g/L, manganese sulfate 0.2 g/L), and stationary culture is carried out at 37 ℃ for 6h.
(3) Culturing the culture solution obtained in the step (2) in a solid culture medium, culturing by streaking, judging bacterial species, and performing expansion culture (the expansion culture method comprises transferring seed solution to a 5L fermentation tank, adding 5L liquid culture medium with pH value of 6.5, culturing at 37deg.C for 24 hr, and culturing under stirring until the bacterial cells reach OD 600 When=2.0, junctionBundle culturing, collecting culture solution, centrifuging, collecting thallus, and lyophilizing).
(4) Preparation of cell lysate: mixing the different thallus freeze-dried powders obtained in the step (3) with purified water according to a mass ratio of 1:50, performing ultrasonic crushing for 20min, sequentially dialyzing thallus lysates through dialysis membranes (the pore diameters are smaller than 1kDa, 1-3kDa, 3-5kDa, 5-10kDa, 10-15kDa and more than 15 kDa), collecting components with different molecular weights, degreasing, removing sugar and freeze-drying to obtain different molecular thallus lysates.
(5) Based on the Human Dermal Fibroblast (HDF) cultured in the step (1), the lysate of different molecular bacteria is evaluated to improve the activity of the Human Dermal Fibroblast (HDF) and promote the collagen production activity. Experimental results show that the thallus lysate (marked as LSQ-12 thallus lysate) with the molecular weight less than 1kDa, which is collected from the donor LSQ, has the strongest activity of improving Human Dermal Fibroblast (HDF) and promoting collagen production.
(6) Dissolving LSQ-12 thallus lysate with small amount of water, separating the lysate by sephadex G-15 column chromatography, 0.60mM (NH) 4 ) 2 SO 4 The buffer was eluted and the eluate was collected as one fraction per 1/4 column volume, yielding different fractions, labeled as LSQ-12- (1 kDa) -1, LSQ-12- (1 kDa) -2 … … LSQ-12- (1 kDa) -10 fractions.
(7) Based on the cultured Human Dermal Fibroblasts (HDF) obtained in the step (1), the LSQ-12 cell lysate-sephadex column chromatography isolate was evaluated to increase the activity of Human Dermal Fibroblasts (HDF) and promote collagen production. The experimental result shows that the LSQ-12- (1 kDa) -5 component has the strongest activity of improving Human Dermal Fibroblast (HDF) and promoting collagen production.
(8) Separating and preparing a fraction (LSQ-12- (1 kDa) -5) with optimal activity of improving Human Dermal Fibroblast (HDF) and collagen production promoting activity by HPLC (the liquid phase condition of the HPLC is that 0.1% trifluoroacetic acid-acetonitrile solution is taken as a mobile phase A, 0.1% trifluoroacetic acid aqueous solution is taken as a mobile phase B, the measured wavelength is 220 mu m, the flow rate is 10mL/min, and the chromatographic Column is XBIridge BEH C18 OBD Prep Column,5 mu m,19mm is 150mm;
collecting an eluent corresponding to a chromatographic peak of 10.064min, concentrating and drying to obtain the active oligopeptide-1;
collecting eluent corresponding to a chromatographic peak for 11.58min, concentrating and drying to obtain the active oligopeptide-2;
collecting an eluent corresponding to a chromatographic peak of 6.701min, concentrating and drying to obtain the active oligopeptide-3;
the HPLC elution procedure was set as shown in the following table:
furthermore, we used mass spectrometry in combination with Edman degradation to determine the amino acid sequence of active oligopeptide-1, active oligopeptide-2 and active oligopeptide-3; the results were as follows:
active oligopeptide-1: m/z 560.2468 is [ M+H ]] + Ions; m/z 542.2379 is [ M-H ] 2 O+H] + Ions; m/z 489.2107 is [ b4+H ]] + Ions; m/z 360.1677 is [ b3+2H ]] + Ions; m/z 342.1560 is [ b3-H ] 2 O+2H] + Ions; m/z 213.0986 is [ b2+2H ]] + Ions; m/z 195.0880 is [ b2-H ] 2 O+2H] + Ions; m/z 156.0769 is [ b1+2H ]] + Ions; m/z 110.0713 is [ His-COOH+H ]] + Ions. Combining with Edman degradation experiment results, finally identifying the amino acid sequence of the active oligopeptide-1 as Ala-Glu-Phe-Gly-His; namely the active peptide with the amino acid sequence shown in SEQ ID NO. 1.
Active oligopeptide-2: m/z 632.2655 is [ M+H ]] + Ions; m/z 614.2556 is [ M-H ] 2 O+H] + Ions; m/z 596.2463 is [ M-2H ] 2 O+H] + Ions; m/z 503.2250 is [ b4+2H] + Ions; m/z 356.1563 is [ b3+2H ]] + Ions; m/z 285.1193 is [ b2+2H ]] + Ions; m/z 267.1083 is [ b3-H ] 2 O+2H] + Ions; m/z 201.0870 is [ b3-b1+H ]] + Ions; m/z 156.0765 is [ b1+2H ]] + Ions; m/z110.0712 is [ His-COOH+H ]] + Ions. Combining with Edman degradation experimental results, finally identifying the amino acid of the active oligopeptide-1The sequence is Glu-Phe-Ala-Glu-His; namely the active peptide with the amino acid sequence shown in SEQ ID NO. 2.
Active oligopeptide-3: m/z 560.2460 is [ M+H ]] + Ions; m/z 542.2365 is [ M-H ] 2 O+H] + Ions; m/z 485.2151 is y4 ion; m/z 338.1461 is y3 ion; m/z 320.1354 is y3-H 2 O ions; m/z 302.1255 is [ y4-y1-COOH ]] + Ions; m/z 267.1089 is y2 ion; m/z 221.1033 is b2 ion; m/z 138.0666 is [ His-H ] 2 O+H] + Ions; m/z 120.0811 is [ His-2H ] 2 O+H] + Ions; m/z 110.0711 is [ His-COOH+H ]] + Ions. Combining with Edman degradation experiment results, finally identifying the amino acid sequence of the active oligopeptide-3 as His-Glu-Ala-Phe-Gly; namely the active peptide with the amino acid sequence shown in SEQ ID NO. 3.
Example 2 preparation of composition
And uniformly mixing gamma-aminobutyric acid with the active oligopeptide-1, the active oligopeptide-2 and the active oligopeptide-3 according to the mass ratio of 1:11.6:23.7:9.8, thus obtaining the composition.
Experimental example
The implementation method comprises the following steps: human Skin Fibroblasts (HSF) were grown to 90% confluency, digested with 0.25% trypsin and inoculated into 24-well and 6-well plates, and when 50% confluency was reached, the actives were added (final concentration 1.0 mg/mL). After the HSF cells are continuously cultured for 24 hours, the cells and the supernatant are collected, and the content of the cells and the supernatant are strictly operated according to the specifications of MMP-1, MMP-3, MMP-9, type I collagen, type III collagen, tropoelastin, laminin and ROS ELISA kit.
The total protein of the cells was extracted, the protein concentration was determined, and the protein levels of MMP-1, MMP-3 and MMP-9 were determined by Western blotting (Western blotting), using GAPDH as an internal reference. The experimental groupings are shown in the following table:
the skin is an important physiological barrier of the human body, can protect the body from pathogens, chemical and physical damages, and is also an organ directly exposed to the outside. The main histological features of skin aging are alterations in the composition of the skin matrix, such as reduction of collagen content and abnormal elastic fiber deposition. In the skin aging process of human body, the matrix metalloproteinase secreted and expressed by skin cells can specifically degrade almost all extracellular matrix components, and plays an important role in skin photoaging. The analytical results (FIG. 7A) showed that gamma-aminobutyric acid, acetyl hexapeptide-3, active oligopeptide-1, active oligopeptide-2, active oligopeptide-3 and gamma-aminobutyric acid, and MMP-1 content of the active peptide composition group were all reduced compared to the blank group, indicating that gamma-aminobutyric acid, acetyl hexapeptide-3, active oligopeptide-1, active oligopeptide-2, active oligopeptide-3 and gamma-aminobutyric acid, and active peptide composition were able to inhibit MMP-1 expression and secretion in HSF cells. Compared with gamma-aminobutyric acid and acetyl hexapeptide-3, the active oligopeptide-1, the active oligopeptide-2, the active oligopeptide-3 and gamma-aminobutyric acid have lower MMP-1 content in the active peptide composition group. The active oligopeptide-1, the active oligopeptide-2, the active oligopeptide-3 and the gamma-aminobutyric acid are shown, the active peptide composition inhibits the secretion of HSF cells, and the activity of expressing MMP-1 is stronger than that of gamma-aminobutyric acid and acetyl hexapeptide-3; furthermore, under the condition of the same concentration, the MMP-1 content of the composition group prepared in the example 2 is lower than that of the active oligopeptide-1, the active oligopeptide-2, the active oligopeptide-3 and the gamma-aminobutyric acid group. We speculate that active oligopeptide-1, active oligopeptide-2, active oligopeptide-3 and gamma-aminobutyric acid can better inhibit secretion and expression of HSF cell MMP-1 through synergistic effect.
Similarly, compared with the blank, the gamma-aminobutyric acid content, the acetyl hexapeptide-3 content, the active oligopeptide-1 content, the active oligopeptide-2 content, the active oligopeptide-3 content and the MMP-9 content of the composition prepared in the example 2 are all obviously reduced (figures 7B and 7C), which shows that the gamma-aminobutyric acid content, the acetyl hexapeptide-3 content, the active oligopeptide-1 content, the active oligopeptide-2 content, the active oligopeptide-3 content and the composition prepared in the example 2 content can inhibit the expression and secretion of the MMP-3 content and the MMP-9 content of HSF cells. Further, under the condition of the same concentration, the content of MMP-3 and MMP-9 in the composition group prepared in the example 2 is lower than that of the active oligopeptide-1, the active oligopeptide-2, the active oligopeptide-3 and the gamma-aminobutyric acid group. We speculate that active oligopeptide-1, active oligopeptide-2, active oligopeptide-3 and gamma-aminobutyric acid can inhibit secretion and expression of HSF cell MMP-3 and MMP-9 through synergistic effect.
Further analysis of the effect of the compositions prepared in example 2 on MMP-1, MMP-3 and MMP-9 protein expression the experimental results showed that compared to the blank control group, protein expression of gamma-aminobutyric acid, active oligopeptide-1, active oligopeptide-2, active oligopeptide-3, MMP-1, MMP-3 and MMP-9 of the composition group prepared in example 2 was inhibited (FIGS. 7D, 7E and 7F), indicating that gamma-aminobutyric acid, active oligopeptide-1, active oligopeptide-2, active oligopeptide-3 and the composition prepared in example 2 were able to inhibit protein expression of MMP-1, MMP-3 and MMP-9 in HSF cells. Further analysis and experiment results show that under the condition of the same concentration, the composition prepared in the example 2 has stronger inhibition activity on MMP-1, MMP-3 and MMP-9 protein expression than that of the active oligopeptide-1, the active oligopeptide-2, the active oligopeptide-3 and gamma-aminobutyric acid. In combination with ELISA detection test results, we speculate that the active oligopeptide-1, the active oligopeptide-2, the active oligopeptide-3 and the gamma-aminobutyric acid can better inhibit protein expression of the HSF cells MMP-1, MMP-3 and MMP-9 through synergistic effect.
Excessive ROS can induce oxidative stress reaction of cells of the organism to cause damage of biomacromolecule substances and even cause diseases, and the organism is required to timely remove excessive ROS free radicals through an antioxidant defense system in order to maintain the balance of reactive oxygen radicals, and meanwhile, a great deal of researches show that the removal of ROS plays an important role in relieving the skin aging process. Collagen is one of the proteins widely distributed in mammals, and has a high content, and also has a close relationship with the health degree, water retention and elasticity of skin. Collagen is a major protein in skin, and as the age increases, the ability of fibroblasts to synthesize collagen and elastin becomes lower and lower, once collagen is absent, the skin cannot maintain its normal morphology and structure, and problems such as roughness, sagging, collapse, wrinkles, and aging occur. In the skin aging process, the synthesis of collagen and elastin by fibroblasts is obviously reduced, and structural proteins in the cell matrix such as fibronectin, laminin and the like are also obviously reduced, so that the skin is finally caused to have elasticity deficiency and wrinkles are increased. Collagen, fibronectin, and laminin in the dermis are therefore important for skin care and for delaying skin aging.
First, the experimental results of the composition prepared in example 2 on the ROS content of HSF cells (FIG. 8A) were analyzed, and compared with the blank control group, the composition prepared in example 2 has reduced content of cellular ROS, which means that the composition prepared in example 2 can inhibit excessive production of ROS by HSF cells or promote scavenging of ROS by HSF cells. The results of in-depth analysis experiments show that under the condition of the same concentration, the composition prepared in the embodiment 2 can inhibit the excessive generation of ROS in HSF cells or promote the activity of the HSF cells to clear ROS, which is obviously stronger than that of reactive peptide and gamma-aminobutyric acid, and is stronger than that of acetyl hexapeptide-3 with the same concentration. We speculate that reactive oligopeptide-1, reactive oligopeptide-2, reactive oligopeptide-3 and gamma-aminobutyric acid can better inhibit the overproduction of ROS in HSF cells or improve the ROS scavenging activity of HSF cells through synergistic effect.
The experimental results of analyzing the influence of the composition prepared in example 2 on the expression and secretion of the HSF cell type I collagen, the III type collagen, the tropoelastin and the laminin show that compared with the blank control group, the gamma-aminobutyric acid, the acetyl hexapeptide-3, the active peptide and the composition prepared in example 2 have certain increase in the expression and secretion of the HSF cell type I collagen, the III type collagen, the tropoelastin and the laminin (figures 8B, 8C, 8D and 8E), which indicates that the gamma-aminobutyric acid, the acetyl hexapeptide-3, the active peptide and the composition prepared in example 2 can promote the expression and secretion of the HSF cell type I collagen, the III type collagen, the tropoelastin and the laminin. Further analysis and experiment results show that under the condition of the same concentration, the composition prepared in the embodiment 2 has stronger expression and secretion activities on the HSF cell type I collagen, type III collagen, tropoelastin and laminin than the active peptide and gamma-aminobutyric acid and stronger acetyl hexapeptide-3 with the same concentration. The active oligopeptide-1, the active oligopeptide-2, the active oligopeptide-3 and the gamma-aminobutyric acid can better promote the expression and secretion of the type I collagen, the type III collagen, the tropoelastin and the laminin of the HSF cells through synergistic effect, exert better and excellent oxidation resistance and skin aging resistance effects, and also can better delay the loss of the collagen and the elastin of the skin and alleviate the problems of rough skin, loose skin, collapse, wrinkles and the like.
Claims (10)
1. An active peptide is characterized by having an amino acid sequence shown as SEQ ID NO. 1, SEQ ID NO. 2 or SEQ ID NO. 3;
wherein, the amino acid sequence of SEQ ID NO. 1 is: ala-Glu-Phe-Gly-His;
the amino acid sequence of SEQ ID NO. 2 is: glu-Phe-Ala-Glu-His;
the amino acid sequence of SEQ ID NO. 3 is: his-Glu-Ala-Phe-Gly.
2. A composition comprising two or more active peptides selected from the group consisting of the active peptides having the amino acid sequences shown in SEQ ID NO. 1, SEQ ID NO. 2 or SEQ ID NO. 3.
3. The composition of claim 2, further comprising gamma-aminobutyric acid.
4. The composition of claim 2, wherein the composition comprises gamma-aminobutyric acid and an active peptide having the amino acid sequences shown in SEQ ID NO. 1, SEQ ID NO. 2 and SEQ ID NO. 3.
5. The composition according to claim 4, wherein the mass ratio of gamma-aminobutyric acid to active peptide of the amino acid sequences shown in SEQ ID NO. 1, SEQ ID NO. 2 and SEQ ID NO. 3 is 1 (1-50): 1-50.
6. The composition according to claim 5, wherein the mass ratio of gamma-aminobutyric acid to active peptide of the amino acid sequences shown in SEQ ID NO. 1, SEQ ID NO. 2 and SEQ ID NO. 3 is 1 (10-15): 20-30): 5-10.
7. The composition according to claim 5, wherein the mass ratio of gamma-aminobutyric acid to active peptides of the amino acid sequences shown in SEQ ID NO. 1, SEQ ID NO. 2 and SEQ ID NO. 3 is 1:11.6:23.7:9.8.
8. Use of an active peptide according to claim 1 or a composition according to any one of claims 2 to 7 for the preparation of a product having an inhibitory effect on the activity or expression of extracellular matrix metalloproteinases.
9. Use of an active peptide according to claim 1 or a composition according to any one of claims 2 to 7 for the preparation of a product having a fine line and/or wrinkle reducing effect.
10. Use of an active peptide according to claim 1 or a composition according to any one of claims 2 to 7 for the preparation of a product having a collagen and/or laminin production promoting effect on the skin.
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