CN114702549B - Active hexapeptide with antioxidation effect and application thereof - Google Patents

Active hexapeptide with antioxidation effect and application thereof Download PDF

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CN114702549B
CN114702549B CN202210356740.3A CN202210356740A CN114702549B CN 114702549 B CN114702549 B CN 114702549B CN 202210356740 A CN202210356740 A CN 202210356740A CN 114702549 B CN114702549 B CN 114702549B
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hexapeptide
use according
aging
product
human skin
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CN114702549A (en
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高理钱
贾艳
李孟础
张达
谢程亮
肖奇才
王璇
孙杰
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Sun Yat Sen University
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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
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
    • A61K38/08—Peptides 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
    • A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
    • 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
    • A61Q19/08—Anti-ageing preparations
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
    • Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
    • Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change

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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)
  • Medicinal Chemistry (AREA)
  • Organic Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Dermatology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Epidemiology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Biochemistry (AREA)
  • Genetics & Genomics (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Immunology (AREA)
  • Gerontology & Geriatric Medicine (AREA)
  • Biophysics (AREA)
  • Molecular Biology (AREA)
  • Birds (AREA)
  • Cosmetics (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
  • Peptides Or Proteins (AREA)

Abstract

The invention belongs to the technical field of cosmetic functional raw materials, and particularly relates to an active hexapeptide with an antioxidant effect and application thereof, which are bioactive peptides with antioxidant activity and capable of promoting proliferation and migration of human skin fibroblasts.

Description

Active hexapeptide with antioxidation effect and application thereof
Technical Field
The invention belongs to the technical field of cosmetic functional raw materials, and particularly relates to active hexapeptide with an antioxidant effect and application thereof.
Background
The cosmetics are compound mixtures prepared by reasonably blending and processing various raw materials, and the cosmetics have various raw materials and different performances. Among them, chemical synthesis and plant extraction have been the main sources of cosmetic functional raw materials. With the continuous update and development of traditional cosmetic raw materials, biological cosmetology and gene cosmetology become new targets for development, and especially peptide raw materials and skin care products containing peptide are more and more favored by people. The active peptide component is composed of a plurality of amino acids with a certain sequence, and most of biochemical reactions and evolutionary processes in organisms are regulated and controlled by a specific amino acid sequence (polypeptide or protein) to a certain extent, so that the bioactive peptide provides a brand new direction and thought for raw materials of cosmetics.
Human skin fibroblasts are the most predominant cells in the dermis layer of the skin and have an important role in maintaining the elasticity and tone of the skin. The human skin fibroblast has strong protein synthesis capability, can synthesize and secrete a large amount of matrix components such as elastin, collagen, glycosaminoglycan, glycoprotein and the like, further generates elastic fibers, collagen fibers and reticular fibers, and secretes various cell repair factors, so that the skin has strong renewal and self-repair capability. Therefore, the cell viability and proliferation properties of human skin fibroblasts are not only closely related to skin aging, but also play a critical role in skin barrier.
Free radicals have a clear relationship with aging and scientists believe that free radicals are one of the leading causes of aging. The free radicals can promote the generation of lipofuscin in vivo, and the lipofuscin is accumulated in skin cells to form senile plaque, and accumulation in brain cells can cause hypomnesis or dysnoesia, even senile dementia. The free radicals can also cause skin relaxation, increased wrinkles, reduced bone regeneration capacity, etc. in the elderly. Once the organism cannot be cleared in time due to excessive increase of free radicals caused by internal or external factors, cells and tissues can be damaged, and finally, the loss of organism functions and the occurrence of aging-related diseases are caused. Thus, scavenging excessive free radicals in and out of the body plays an important role in the prevention of aging and certain diseases.
From the above, it is seen that the development of bioactive peptides which have antioxidant activity and can promote proliferation and migration of human skin fibroblasts has important application prospects in preparing skin care products by using the peptides as cosmetic raw materials.
Disclosure of Invention
In order to overcome the defects in the prior art, the invention aims to provide a hexapeptide which has antioxidant activity, can promote proliferation and migration of human skin fibroblasts, promote synthesis of type I collagen, and can be used for resisting oxidation, aging, promoting wound healing and the like.
In order to achieve the above purpose, the present invention is realized by the following technical scheme:
the invention provides a hexapeptide, the amino acid sequence of which is shown in SEQ ID NO:1 (GHKGHK). The amino acid sequence of the hexapeptide is Gly-His-Lys-Gly-His-Lys.
The amino acid sequence of the invention adopts a standard Fmoc scheme, and reasonable synthesis is carried out by screening proper resin. The method comprises the following steps: the C-terminal carboxyl of the target polypeptide is connected with an insoluble polymer resin in a covalent bond form, then the amino group of the amino acid is taken as a starting point to react with the carboxyl of another molecular amino acid to form a peptide bond, and the process is repeated continuously, so that the target polypeptide product can be obtained. And after the synthesis reaction is finished, removing the protecting group, and separating the peptide chain from the resin to obtain a target product. The polypeptide synthesis is a solid phase synthesis process of repeatedly adding amino acid, and the solid phase synthesis sequence is synthesized from the C end to the N end. The high polymer resin is one of crosslinked polystyrene resin, polyamide resin, polyethylene-glycol resin and other resin.
The invention also provides application of the hexapeptide in preparation of antioxidant and/or anti-aging products.
The invention also provides application of the hexapeptide in preparing a product for promoting wound healing.
Preferably, the anti-aging is scavenging of free radicals that cause aging.
Preferably, the anti-aging is to promote the activity of human skin fibroblasts.
Preferably, the promotion of wound healing is to promote migration of human skin fibroblasts.
The invention evaluates polypeptide anti-aging, skin barrier improvement, skin repair, wound healing and the like by human skin fibroblasts; DPPH free radical scavenging experiments evaluate the antioxidant effect of polypeptides; the chick embryo chorioallantoic membrane assay evaluates the safety of the polypeptide. The research shows that the hexapeptide (GHGHK) can play a role in promoting the growth of human skin fibroblasts at a lower concentration, promote the synthesis of type I collagen, promote the elasticity and compactness of skin, effectively promote the migration of cells, and the in vitro chemical antioxidant detection also shows that the hexapeptide has antioxidant activity and very strong DPPH free radical scavenging capability, and can be applied to the aspects of antioxidant, anti-aging, wound healing and the like.
Preferably, the product is a pharmaceutical, cosmetic or health product.
Preferably, the product contains an effective dose of hexapeptide, the balance being adjuvants or other compatible components.
Further, in order to increase the applicable range of the product, the auxiliary materials comprise conventional diluents, fillers, binders, wetting agents, absorption promoters, surfactants, lubricants and stabilizers.
Further, the other compatible components include natural drugs, chemical drugs or biological drugs.
Preferably, in order to increase the application range of the medicine, the medicine for treating aging-related diseases further comprises pharmaceutically acceptable carriers and/or auxiliary materials, such as acidulants, toners, flavoring agents, sweeteners, or combinations thereof.
Preferably, the product can be made into various dosage forms, such as tablet, capsule, injection, liposome nanoparticle, controlled release agent, gel paste, ointment, topical liniment, patch, cream, detergent, emulsion, gel or toner, etc.
Compared with the prior art, the invention has the beneficial effects that:
the invention discloses a hexapeptide (GHGHK), which can promote proliferation and migration of human skin fibroblasts, promote synthesis of type I collagen, promote skin elasticity and compactness, has antioxidant activity and very strong DPPH free radical removal capability, has low irritation and high safety, can be applied to the fields of biological pharmacy, cosmetics and the like, such as preparation of anti-aging cosmetics, medicaments for aging-related diseases, wound healing promotion products, antioxidant products and the like, and has important application prospects.
Drawings
FIG. 1 is a high performance liquid chromatography identification map of a polypeptide;
FIG. 2 is a mass spectrometry diagram of a polypeptide;
FIG. 3 is a graph showing the results of a hexapeptide assay for affecting human skin fibroblast proliferation;
FIG. 4 is a graph showing the results of measurement of hexapeptide-based human skin fibroblast mobility (A is a 24h cell mobility increase curve; B is 24h cell mobility);
FIG. 5 shows the results of the measurement of the clearance of DPPH free radicals by hexapeptide;
FIG. 6 shows the results of measurement of hexapeptide effect on human type I collagen content;
FIG. 7 is a diagram of the chorioallantoic membrane assay of hexapeptide chick embryos.
Detailed Description
The following describes the invention in more detail. The description of these embodiments is provided to assist understanding of the present invention, but is not intended to limit the present invention. In addition, the technical features of the embodiments of the present invention described below may be combined with each other as long as they do not collide with each other.
The experimental methods in the following examples, unless otherwise specified, are conventional, and the experimental materials used in the following examples, unless otherwise specified, are commercially available.
EXAMPLE 1 hexapeptide solid phase Synthesis
The amino acid sequence of the invention adopts a standard Fmoc scheme, and reasonable synthesis is carried out by screening proper resin. The method comprises the following steps:
selecting a high molecular resin [ Wang resin (Wang resin) in crosslinked polystyrene, sequentially adding amino acids from right to left according to the characteristics of an amino acid sequence (GHGHK) Gly-His-Lys-Gly-His-Lys, connecting the carboxyl of Lys with one resin in a covalent bond form, then enabling the amino of Lys and the carboxyl of His to carry out a shrink reaction, then adding Gly to enable the amino of His to react with the carboxyl of Gly, removing the resin after connecting the last Gly amino acid, obtaining a target polypeptide, purifying by adopting High Performance Liquid Chromatography (HPLC) to obtain a final polypeptide product, and carrying out Mass Spectrum (MS) analysis on the polypeptide.
As shown in fig. 1 and 2, the theoretical molecular weight of the hexapeptide synthesized in this example is 662.75, the actual molecular weight is 662.71, and the sequence is: gly-His-Lys-Gly-His-Lys. Wherein Gly represents amino acid with English name of Glycine and Chinese name of Glycine and corresponding residue; his represents an amino acid with an English name of Histidine and a Chinese name of Histidine and a corresponding residue; lys represents an amino acid with an English name of Lysine and a Chinese name of Lysine and a corresponding residue.
EXAMPLE 2 Effect of hexapeptide on human skin fibroblast morphology and proliferation
Human skin fibroblasts were cultured in complete medium [ consisting of basal medium high glucose DMEM,10% fetal bovine serum (v/v), and 1% diabody (consisting of penicillin and streptomycin, v/v=1:1) ] and placed at 37 ℃, 5% co 2 Culturing in a constant temperature incubator until 80% -90% of fusion rate is reached in a cell culture dish, and then carrying out passage, transferring to two to three generations, and calculating the cell number by using a full-automatic cell counter.
The cells were packed in 3X 10 cells 3 The wells were inoculated in 96-well plates (PBS as a blank), medium was removed after cell attachment, 100. Mu.L of fresh medium containing 0.0032. Mu.M to 2. Mu.M (0.0032. Mu.M, 0.016. Mu.M, 0.08. Mu.M, 0.4. Mu.M, 2. Mu.M) polypeptide was added, the control group was added with an equal amount of DMEM medium, and after 24-72 h of incubation in the incubator, 10. Mu.L MTT was added per well, and after 4h incubation in the incubator was continued, 100. Mu.L DMSO was added, and finally incubation was continued for 4h in the incubator.
After the incubation, the optical density, i.e.OD, at 570nm was measured on an automatic microplate reader for each well, with 6 multiplex wells per group. Example the results of the experiment are shown in figure 3.
As a result, it was found that when hexapeptide of the present invention was applied to human fibroblasts for 72 hours, the cells of each polypeptide group became longer, the cell clostridia became longer, the cells became more compact, and the adherent cells increased. Meanwhile, the results of FIG. 3 show that there is a significant difference in proliferation of human skin fibroblasts when the concentration of the polypeptide is 0.0032. Mu.M to 2. Mu.M ** P＜0.01， *** P is less than 0.001), the hexapeptide of the invention can promote the activity of human skin fibroblasts, thereby improving skin elasticity and having certain anti-aging effect.
Example 3 cell scratch assay
After subculturing human skin fibroblasts as in example 2, about 5X 10 cells were added per well in a 24-well plate 4 After culturing the fibroblasts for 24 hours, vertical cross-scratches were made on each well with 200. Mu.L of a pipette tip, and the scraped cells were washed with PBS, then 500. Mu.L of serum-free medium containing 0.0032. Mu.M to 2. Mu.M (0.0032. Mu.M, 0.016. Mu.M, 0.08. Mu.M, 0.4. Mu.M, 2. Mu.M) polypeptide was sequentially added to each well [ consisting of basic medium high glucose DMEM,1% diabody (consisting of penicillin and streptomycin, v/v=1:1) ], and the culture was continued, and observed for 0h and 24h, respectively, and mobility was calculated using imageJ software, mobility= (initial scratch width-scratch width at the corresponding time point)/initial scratch width×100%.
The experimental results of FIG. 4 show that hexapeptide has a relatively obvious cell migration promoting effect at a relatively low concentration (0.0032 mu M), and the cell migration rate reaches 38.04%; and at the concentration of 2 mu M, the cell mobility reaches 83.38, which is 78.94% higher than that of a blank group without adding the drug (the cell mobility of the blank group without adding the drug is 4.44%). The hexapeptide disclosed by the invention has the effects of improving skin self-repair, improving skin barrier and promoting wound healing.
EXAMPLE 4 DPPH radical scavenging Activity of hexapeptide
180. Mu.L of DPPH reagent (1 mg of DPPH was fixed to 20mL with absolute ethanol) and 60. Mu.L of polypeptide (0.08 mM, 0.4mM, 2mM, 10mM, 50mM, respectively) were added to a 96-well plate as test groups. Simultaneously, a blank group and a model group are arranged, wherein the blank group is 180 mu L of absolute ethyl alcohol and 60 mu L of polypeptide, the model group is 180 mu L of DPPH reagent and 60 mu L of ultrapure water, 3 compound holes are arranged in each hole, and the reaction is carried out for 15-30 minutes at room temperature and in a dark place. Absorbance at 517nm was measured by a microplate reader after the reaction, and DPPH radical scavenging rate = {1- (test group-blank group)/(model group) } ×100%.
The results of the experiment in FIG. 5 show that the hexapeptide of the present invention has a certain free radical scavenging effect, and DPPH scavenging rate reaches 78.1% at 50mM concentration, which indicates that the hexapeptide of the present invention has a certain anti-free radical and anti-oxidation effect.
EXAMPLE 5 Effect of hexapeptide on human type I collagen
After subculturing human skin fibroblasts as in example 2, about 5X 10 cells were added per well in a 24-well plate 4 The fibroblast cells were cultured for 24 hours, then the medium was aspirated, and fresh serum-free DMEM medium was added to a final concentration of 0.1. Mu.M polypeptide, and the mixture was placed at 37℃with 5% CO 2 The culture was continued for 24 hours in a constant temperature incubator. In the experimental process, a negative control group and a positive control group are arranged, wherein the negative control group is an equal amount of serum-free DMEM medium, and the positive control group is an equal amount of serum-containing DMEM medium. After the culture, the cell culture supernatant was collected and centrifuged in a 1.5mL sterile centrifuge tube, and the human type I collagen (COL I) content was detected by ELISA method using a human type I collagen ELISA kit according to the instructions for use.
The experimental results in fig. 6 show that hexapeptide has a remarkable promoting effect on the synthesis of COL I in cells at a lower concentration (0.1 μm) compared with the negative control, which indicates that the hexapeptide of the present invention has an effect of promoting collagen secretion synthesis and has a good effect on improving skin elasticity and firmness.
Example 6 chick embryo chorioallantoic Membrane experiment
Placing 0-day-old hatching eggs at room temperature for half a day, then placing the air chamber upwards into an automatic incubator, and adjusting the temperature to 37.6+/-0.1 ℃ and the relative humidity to 46+/-1%; removing white egg and dead embryo from day 5; incubating until 10-12 days for later use. Removing eggshells at the air chamber end of the hatching eggs, slightly peeling off the eggshells after wetting the eggshells with normal saline to expose chorioallantoic membranes (CAM), and then placing a non-irritating rubber ring with the diameter of 1.5cm on the CAM; placing 1 mu M-50 mM polypeptide aqueous dispersion (50 mM) in an incubator for half an hour, then taking 0.3mL of polypeptide aqueous dispersion and directly dripping the polypeptide aqueous dispersion into the rubber ring, observing vascular effects such as CAM bleeding, vascular dissolution, coagulation bleeding and the like in the ring after 30 minutes, and performing evaluation according to the evaluation criteria of table 1; physiological saline is used as a negative control group, and 1% sodium dodecyl sulfate is used as a positive control group.
TABLE 1 vascular Effect evaluation criteria
Note that: bleeding refers to the outflow of blood from blood vessels and/or capillaries of a CAM; coagulation refers to the denaturation of intravascular and extravascular proteins, usually found only in large and moderately large blood vessels; vascular thawing refers to the disappearance of blood vessels on the CAM membrane.
The test results of fig. 7 show that the saline negative control group scored 0, the hexapeptide test group scored 0, and the 1% sodium dodecyl sulfate positive control group scored 3. The hexapeptide has extremely low irritation and high safety to human bodies and skin.
In summary, the invention synthesizes a hexapeptide (GHGHK) for the first time, the polypeptide can play a role in promoting the growth of human skin fibroblasts at a lower concentration, and can effectively promote the migration of the cells, and in-vitro chemical antioxidant detection also shows that the hexapeptide has antioxidant activity and strong DPPH free radical scavenging capability, can promote the proliferation and migration of the human skin fibroblasts, has low irritation and high safety, and can be applied to the fields of biopharmaceuticals, cosmetics and the like.
The embodiments of the present invention have been described in detail above, but the present invention is not limited to the described embodiments. It will be apparent to those skilled in the art that various changes, modifications, substitutions and alterations can be made to these embodiments without departing from the principles and spirit of the invention, and yet fall within the scope of the invention.
Sequence listing
<110> university of Zhongshan Shenzhen
<120> hexapeptide having antioxidant activity and use thereof
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 6
<212> PRT
<213> hexapeptide (Artificial Sequence)
<400> 1
Gly His Lys Gly His Lys
1 5

Claims (10)

1. A hexapeptide, characterized in that the amino acid sequence of the hexapeptide is as set forth in SEQ ID NO: 1.
2. Use of the hexapeptide of claim 1 for the preparation of an antioxidant and/or anti-aging product.
3. Use of the hexapeptide of claim 1 for the preparation of a wound healing product.
4. The use according to claim 2, wherein the anti-aging is scavenging of free radicals that cause aging.
5. The use according to claim 2, wherein said anti-aging is to promote the viability of human skin fibroblasts.
6. The use according to claim 3, wherein the promotion of wound healing is to promote migration of human skin fibroblasts.
7. Use according to claim 2 or 3, characterized in that the product is a pharmaceutical or cosmetic product.
8. Use according to claim 2 or 3, wherein the product contains an effective amount of hexapeptide, the balance being adjuvants or other compatible components.
9. The use according to claim 8, wherein the auxiliary materials comprise conventional diluents, fillers, binders, wetting agents, absorption promoters, surfactants, lubricants and stabilizers.
10. The use according to claim 8, wherein the other compatible components comprise natural drugs, chemical drugs or biological drugs.
CN202210356740.3A 2022-04-06 2022-04-06 Active hexapeptide with antioxidation effect and application thereof Active CN114702549B (en)

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Publication number Priority date Publication date Assignee Title
JP2006199671A (en) * 2005-01-19 2006-08-03 Suetsuna Yoko New hexapeptide and activated oxygen inhibitor
US20110052676A1 (en) * 2009-09-01 2011-03-03 James Vincent Gruber Composition For Delaying Cellular Senescence
KR101667383B1 (en) * 2012-03-28 2016-10-18 주식회사 인코스팜 Biotin-conjugated hexapeptide-2 analogue and use thereof
CN105131086B (en) * 2015-09-28 2018-10-09 华南理工大学 A kind of hexapeptide and its application
KR101809209B1 (en) * 2016-05-31 2017-12-15 주식회사 올리패스코스메슈티컬즈 Cosmetic composition for improving the health of scalp and manufacturing method thereof
CN109293737B (en) * 2018-09-27 2020-10-27 华南理工大学 Tetrapeptide for resisting skin aging and application thereof
CN109593127B (en) * 2018-12-10 2020-08-07 暨南大学 Gene recombinant collagen peptide MJ L GG-34 and preparation method and application thereof

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