CN107383163A - One kind promotees the ultrashort peptide of collagen secretion and its application - Google Patents
One kind promotees the ultrashort peptide of collagen secretion and its application Download PDFInfo
- Publication number
- CN107383163A CN107383163A CN201710533713.8A CN201710533713A CN107383163A CN 107383163 A CN107383163 A CN 107383163A CN 201710533713 A CN201710533713 A CN 201710533713A CN 107383163 A CN107383163 A CN 107383163A
- Authority
- CN
- China
- Prior art keywords
- collagen
- peptide
- ultrashort
- skin
- ultrashort peptide
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
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
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Dermatology (AREA)
- Organic Chemistry (AREA)
- Biophysics (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Biochemistry (AREA)
- Epidemiology (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Birds (AREA)
- Peptides Or Proteins (AREA)
- Cosmetics (AREA)
Abstract
The invention provides one kind to promote the ultrashort peptide of collagen secretion and its application, belongs to field of biomedicine technology.Described two kinds promote ultrashort peptide Magin FL and the Purin WH3 of collagen secretion, with promotion collagen synthesis ability, and there is extremely strong anti-oxidant, activity of fighting against senium, no cytotoxicity, simple without hemolytic activity, preparation method, therefore it is treating the reparation and regeneration of impaired epidermis for preparing, such as treat burn, scald, skin ulcer medicine, and replace EGF to be used for the fields such as skin repair, the anti-aging for stimulating skin collagen hyperplasia, anti-oxidant cosmetics and skincare product new raw material, and its effect may also be not limited to this.Ultrashort peptide Magin FL, Purin WH3 molecular weight are small, simple in construction, extremely low using the cost of chemical synthesis process, and the EGF of compared to every gram nearly 2,000,000 dollars of price has the characteristics of prominent beneficial.
Description
Technical field
The present invention relates to one kind to promote the ultrashort peptide of collagen secretion and its application, belongs to field of biomedicine technology.
Background technology
Aging is the inexorable law of any biological life process, with world wide the problem of an aging population it is increasingly prominent
Go out, anti-aging field has turned into the focus of global concern.Skin is one of organ the most obvious during body aging, with
Degeneration change can occur for the growth at age, skin, such as elastic regression, water content reduction, atrophy, wrinkle etc. occurs.
Skin senescence is the biological process of skin histology a series of complex, is all endogenous physiological factors and exogenous
The coefficient result of environmental factor.Aging can not only influence normal skin tissue's structure and physiological function, moreover, also can be direct
Influence the outward appearance and appearance of skin outer layer.Skin is made up of epidermis, skin corium and subcutaneous fat.Wherein, in skin corium
Fibroblasts to secrete produces collagen, directly related with the problem of aging of skin to maintain the intensity of skin and elasticity.Glue
Former albumen is the protein for forming human connective tissue, accounts for 1/3rd of human body total protein content more, and the glue in skin
Former albumen is then up to more than 75%, wherein mainly containing NTx albumen (Collagen I).The molecular weight of collagen is 30
Ten thousand dalton, it is made up of three peptide chains, and wherein NTx albumen is three spiral shells being combined into by 2 α 1 and 1 subunit of α 2
Structure is revolved, and interwinds into helical structure.The presence of collagen and skin health degree, water conservation and elasticity etc. have closely
Relation.The Histological change of skin senescence is mainly the reduction and loss of collagen.Collagen is lost in ageing skin
Master has two aspect reasons, is on the one hand that the collagen amount of Skin Cell synthesis is reduced, is on the other hand by matrix metalloprotease
MMP-1 in enzyme family (MMPs) constantly degrades.Because inherent cause etc. can not resist the environmental stimulis such as internal cause ultraviolet, radiation,
Skin can gradual aging, and then have influence on synthesis and the degradation process of collagen.When the speed of collagen degradation is more than it
During the speed of generation, skin relaxation will occurs, produce the obvious aging feature such as wrinkle
Possess anti-aging functional preparation in recent years and be constantly subjected to related discipline field, particularly health care, beauty
The great attention and common concern in the fields such as cosmetic science.Have now been developed that species is various, formulation is various, a feast for the eyes at present
Beautifying skin anti-aging cosmetics.But existing collagen Related product on the market, all using direct replenishing collagen as
Major function, however, collagen molecules amount is big, smearing mode can not almost make it penetrate keratoderma to act on skin corium
Fibroblast;If the direct replenishing collagen of injection system, because it can be degraded in vivo, multiple injection, mistake are needed
Cheng Fanfu, cost are high, while it is a Risks again that injectable collagen albumen, which causes immunological rejection,;If with edible, collagen
Liquid can be digested in enteron aisle and resolve into micromolecule polypeptide or single amino acids, therefore the effect of actual replenishing collagen has
Limit.Since it is found that since biologically active peptide, particularly the related growth factor polypeptide of skin tissue cell, collagen polypeptide,
The natural activity such as glutathione, carnosine peptide, genetically modified polypeptide molecule and chemically synthesized polypeptide etc. are developed and are successfully applied to
After beautifying skin anti-aging cosmetics, it has been found that amount of activated peptide can directly activate Skin Cell itself synthesis collagen egg
In vain, promote replenishing collagen content so as to reach maximally efficient, fundamentally lift the vigor of skin itself, activate skin
Smooth muscle cells collagen synthesis albumen, promote skin repair, resistance skin senescence.
Biologically active peptide just refers to that a kind of vital movement to living organism is beneficial or has the peptides of physiological action
Compound, it is that a kind of relative molecular mass is less than 6000Da, the polypeptide with various biological function.The biology of biologically active peptide
Meaning is mainly reflected in its mechanism of absorption better than amino acid and with incomparable two aspects of physiological function of amino acid.Especially
It is the ultrashort peptide of some small molecules, because it has ultrashort sequence, small-molecular-weight, therefore is even more to possess high security, be easy to
Synthesis, advantageous characteristic is absorbed etc. beneficial to skin, and have concurrently active peptide high bioactivity in itself, regulation cell physiological function and
Metabolic activity and then inherently change skin problem, at the same be also masses think anti-aging raw material the most safe and efficient it
One, therefore ultrashort peptide has highly important answer in beautifying skin reparation, health care and food, drug additive etc.
With value and DEVELOPMENT PROSPECT.
The content of the invention
Promote the ultrashort peptide of collagen secretion the present invention relates to one kind, including two kinds promote the ultrashort peptide Magin-FL of collagen secretions,
Purin-WH3 is preparing anti-aging anti-wrinkle cosmetic, medical improvement, conditioning and/or repair of skin agent, anti-oxidation medicine, food
The application in the fields such as additive.
Technical scheme:
One kind promotees the ultrashort peptide of collagen secretion, including two kinds promote collagen secretion ultrashort peptide Magin-FL, Purin-WH3;It is described
Ultrashort peptide Magin-FL:A kind of straight chain small peptide, molecular weight 1205.42Da, isoelectric point are 9.02, residual containing 10 amino acid
Base, the primary structure of complete sequence are:Phe-Phe-Arg-Thr-Ser-Cys-Arg-Ser-Val-Cys;Described ultrashort peptide
Purin-WH3:A kind of straight chain small peptide, molecular weight 672.88Da, isoelectric point are 9.31, contain 6 amino acid residues, complete sequence
Primary structure:Val-Val-Lys-Cys-Pro-Lys.
The beneficial effects of the present invention are:Two kinds provided by the invention promote collagen secretion ultrashort peptide Magin-FL, Purin-
WH3, have and promote that collagen secretion is active, anti-oxidant and activity of fighting against senium, to DPPH free radicals and ABTS·+Cation is free
Base clearance rate is fairly obvious;And by the ultrashort peptide Magin-FL of double luciferase reporter system detectios for I-type collagen
There is extremely strong transcriptional activity, its transcriptional activity 1.62 times can be improved when concentration is 5 μ g/ml;Meanwhile pass through Western
Blotting detects the expression that ultrashort peptide Purin-WH3 improves I-type collagen.In addition, two kinds of ultrashort peptides have molecule
Measure small, cytotoxicity is low, without hemolytic activity, it is simple in construction, easily prepared the features such as, therefore applied promote collagen secretion,
In the exploitation in the field such as anti-oxidant, anti-aging cosmetics or medical treatment, health products.
Brief description of the drawings
Fig. 1 is toxicity figure of two kinds of ultrashort peptides to HFF-1 cells.
Fig. 2 (a) is pGL3-COLI α 2 plasmid figure spectrogram.
Fig. 2 (b) is phRL-TK plasmid figure spectrogram.
Fig. 3 be in HEK293 cells ultrashort peptide Magin-FL to the influence figure of the transcriptional activities of pGL3-COLI α 2.
Fig. 4 is the influence figure that ultrashort peptide Purin-WH3 irradiates Col1 protein expressions after fibroblast to UVA.
In figure:
Embodiment
Below in conjunction with accompanying drawing and technical scheme, embodiment of the invention is further illustrated.
Embodiment 1
Two kinds of chemical syntheses for promoting collagen secretion ultrashort peptide Magin-FL, Purin-WH3:
Two kinds of chemical synthesis process for promoting collagen secretion ultrashort peptide Magin-FL, Purin-WH3 of (μ g1/) ml:According to ultrashort
Peptide amino acid sequence, its complete sequence is synthesized with automatic Peptide synthesizer (433A, Applied Biosystems), it is anti-by HPLC
Phase column chromatography desalination.
(2) molecular weight determination uses MALDI-TOF-MS (MALDI-TOF).
(3) two kinds of rush ultrashort peptide Magin-FL, Purin-WH3 high-efficient liquid phase chromatogram HPLC methods of collagen secretion of purifying
Its purity is identified, molecular weight determination uses MALDI-TOF-MS (MALDI-TOF), isoelectric focusing
Electrophoretic determination isoelectric point, amino acid sequence structure is determined with automatic Protein Sequencer.
Ultrashort peptide Magin-FL:A kind of straight chain small peptide, molecular weight 1205.42Da, isoelectric point are 9.02, contain 10 ammonia
Base acid residue, the primary structure of complete sequence are:Phe-Phe-Arg-Thr-Ser-Cys-Arg-Ser-Val-Cys;
Ultrashort peptide Purin-WH3:A kind of straight chain small peptide, molecular weight 672.88Da, isoelectric point are 9.31, contain 6 ammonia
Base acid residue, the primary structure of complete sequence:Val-Val-Lys-Cys-Pro-Lys.
Embodiment 2
Hemolytic activity determines:
The Healthy People blood of collection is mixed into anti-freezing with Alsever's Solution, brine 2 times is simultaneously resuspended into 107-108cell/ml
Suspension.The good red cell suspension of above-mentioned dilution mixes with being dissolved in the ultrashort peptide sample of physiological saline respectively, 37 DEG C of insulations
30min, 5min is centrifuged then at 1000rpm, supernatant surveys absorption value in 540nm.Negative control uses physiological saline, positive control
Using Triton X-100, percent hemolysis calculates as follows:Percent hemolysis H%=(A sample-A negative controls)/A
Positive control × 100%.
The ultrashort peptide hemolytic activity of 1. two kinds of table
As a result two kinds of haemolysis promoted when ultrashort peptide Magin-FL, Purin-WH3 concentration of collagen secretion is 160 μ g/ml are shown
Percentage is 0.41%, 1.62%.Illustrate the hemolytic activity that Magin-FL, Purin-WH3 do not have, be not easy to cause human body red
Cell rupture dissolve and to human body produce injury, therefore be very beneficial to its anti-oxidant and resisting age of skin medicine, food or
The further development and application in person's cosmetic additive agent field.
Embodiment 3
CTA:
The ultrashort peptide of the group is detected to human skin fibroblasts HFF-1 toxicity with mtt assay.
Human skin fibroblasts HFF-1 is purchased from Shanghai cell bank.First by fibroblast in containing 15% hyclone
And cultivated in the DMEM of dual anti-(penicillin and each 100U/ml of streptomysin), after cell covers with, with 0.25% trypsase
Digestion is got off, and is washed twice with above-mentioned culture medium, again suspension cell, and the μ l of cell suspending liquid 100 are added into 96 after cell count
In porocyte culture plates, every hole cell number is set to reach 105It is individual.Sample is added, control group adds the sterilizing ultra-pure water of same volume,
37 DEG C are put, 5%CO2Culture 24h in incubator.After culture terminates, 96 porocyte culture plates add 20 μ l 5mg/ml MTT per hole
Solution (is prepared) with cell culture PBS, continues to cultivate 5h, suctions out liquid in hole with syringe, 100 μ l are added per hole
DMSO, it is completely dissolved purple crystal several times with liquid-transfering gun piping and druming.ELIASA detects light absorbs, determines wavelength 490nm, reference wave
Long 630nm.
As a result as shown in figure 1, showing that two kinds of rush ultrashort peptide Magin-FL, Purin-WH3 concentration of collagen secretion are 160 μ g/
Cell survival rate during ml is 78.96%, 93.55%.Illustrate that two kinds of ultrashort peptide Magin-FL, Purin-WH3 do not have cell
Toxicity, normal cell survival rate is influenceed without conspicuousness, therefore be very beneficial to it and enter one in antisenility cosmetics additive field
The development and application of step.
Embodiment 4
Antioxidative Activity Determination:
(1) DPPH free radical scavenging activities (DPPH radical scavenging assay)
A certain amount of DPPH (2,2-diphenyl-1-picrylhydrazyl hydrate, Sigma, the U.S.) is weighed, is used
Methanol dissolves, and is made into 6 × 10-5M solution, it is now with the current.48 μ l DPPH solution and 2 μ l samples (2mg/ml) are mixed (final
Sample and DPPH mass ratio are 3:1), lucifuge stands 30min at room temperature, and light absorption value is determined at 517nm.Blank control group with
Sample dissolving medium replaces testing sample.Experiment do three it is parallel, ultraviolet specrophotometer return to zero when use methanol.
DPPH clearance rates (%)=(AB-AA)/AB × 100 (AB:Blank control group light absorption value;AA:Sample sets extinction
Value).
(2)ABTS·+Radical cation scavenging capacity
ABTS (3-ethylbezothiazoline-6-sulfonic acid) (3- ethyl benzo thiazole phenanthroline -6- sulfonic acid)
2mM ABTS storing liquids are made into PBS (pH7.4).By ABTS storing liquids and 70mM potassium peroxydisulfates (K2S2O8) aqueous solution
By volume 250:1 mixing, in room temperature avoid light place 15-16h.Before on-test, by ABTS·+Release to the suction at 734nm wavelength
Light value is 0.80 ± 0.03.By 4 μ l not sample and the above-mentioned corrected ABTS of 96 μ l·+Solution mixes, after room temperature places 10min,
The light absorption value of reaction solution is detected at 734nm wavelength.Blank control group is sterile deionized water used in sample dissolution.Experiment does three
It is individual parallel.
ABTS·+Clearance rate I (%)=(AB-AA)/AB × 100 (AB:Blank control group light absorption value;AA:Sample sets extinction
Value).
The ultrashort peptide antioxidation activity in vitro of 2. two kinds of table
As a result as shown in table 2, two kinds of ultrashort peptide Magin-FL, Purin-WH3 are respectively provided with antioxidation activity.Wherein, sample
When Magin-FL concentration is 2mg/ml, its DPPH free radical scavenging activity I% can reach 89.94%, ABTS·+Radical cation
Clearance rate I% can reach 68.29%;When sample P urin-WH3 concentration is 2mg/ml, its DPPH free radical scavenging activity I% can
Reach 85.37%, ABTS·+Radical cation clearance rate I% can reach 79.94%;Possess high antioxidation activity,
Free radical is significantly removed, can directly prevent the large biological molecules such as collagen from its damage.
Embodiment 5
Influence of the ultrashort peptide to collagen transcriptional activity is detected using Dual-luciferase reportor systerm:
HEK 293T cells in good condition are chosen, it is whole with the DMEM containing 10%FBS after being digested with 0.25% pancreatin
Only digest.By eugonic 293T cells with 5 × 104~1 × 105Individual/ml density is inoculated with 24 orifice plates.Used per the μ L of hole 500
10%FBS DMEM medium cultures, treat it is adherent after handled.Then, two sterile 2ml EP pipes are taken.One addition
1.2mL serum-frees are without dual anti-DMEM culture mediums and add 20 μ L liposomes Lipofectamine 2000, and slowly piping and druming is uniformly quiet
Put 5min.Another adds 1.2mL serum-frees without dual anti-DMEM culture mediums, while adds the pGL3-COLI α 2 built (as schemed
2 (a)), phRL-TK (such as Fig. 2 (b)), pEGFP-N3 plasmids (mass ratio 10:2:1) and the gross mass of addition is made to be no more than 1 μ
g.Uniformly piping and druming, stand 5 minutes.The fluid mixing chamber temperature of above-mentioned two EP pipes is stood into 20min, allows liposome fully to wrap up matter
Grain.The culture medium in 24 well culture plates is then sucked, 400 μ L serum-frees are added per hole and cultivates liquid without dual anti-DMEM and slowly adds
Enter 100 μ L liposome plasmid mixing liquids.Blank group adds 100 μ L serum-frees without dual anti-DMEM culture mediums.Finally, by 24 orifice plates
It is placed in 37 DEG C and cultivates 6-8h.Green fluorescence can be observed under fluorescence microscope.This is due to host cell expression green
Caused by gene in fluorescence photoprotein plasmid.We can calculate ratio of the luminescent cell in full cell and learn transfection efficiency.
The just change of energy effective detection luciferase more than 30% of general transfection efficiency.
All medicine serum-free DMEM nutrient solutions dilutions are configured to 5 μ g/mL and 50 μ g/mL, two kinds of concentration dilutions of height
Liquid.Because all systems add the internal reference plasmid of equivalent, if under the too low deducibility above two concentration of internal reference luciferase expression
Drug toxicity is excessive, because dilution lower concentration further screens.Adding transfection has the 293T cells of plasmid, per the μ l of hole 500, each
3 repetitions of concentration gradient, control group then add isometric serum-free without dual anti-DMEM nutrient solutions.24 orifice plates for adding medicine are put
In 37 DEG C of incubator cultures, supernatant is sucked after 12 hours, cell is carefully cleaned 2 times with PBS cushioning liquid.It is dilute with PBS afterwards
5 released × passive lysis buffer (Passive Lysis Buffer, PLB, Promega kit).It is dilute that 100 μ L are added per hole
1 × the PLB released.Room temperature concussion cracking 15min, -20 DEG C of freezing 15min, repeats freeze thawing step 2~3 time, so that cell is complete
Fully rupture discharges intracellular luciferase.
Fluorescein plum Activity determination:40 μ L lysates are suctioned out, luciferase is added to and detects 96 special hole round bottom detection plates
(Greiner U-plate).Lucifuge adds 20ul firefly luciferase reaction substrate Luciferase Assay per hole afterwards
Buffer (LAB), upper instrument readings.This step is used to detect firefly luciferase vigor.It is glimmering that 20 μ l sea pansies are added afterwards
Light element enzyme reaction substrate Stop&Glo (STOP), upper instrument readings.Reporter plasmid and internal reference have been respectively obtained by so handling
The enzyme content (quantity of enzyme is directly proportional to fluorescence radiation intensity) of plasmid, there is respective LAB/ in each hole during data processing
STOP values, i.e. firefly luciferase and the ratio (fLuc/rLuc) of sea cucumber luciferase.
As a result as shown in figure 3, relative luciferase activity when ultrashort peptide Magin-FL concentration is 5 μ g/ml, 50 μ g/ml
Respectively 1.62,1.80, it is as a result extremely notable.Illustrate the ability of ultrashort peptide Magin-FL tool efficient activations I-type collagen transcription,
Therefore it is very beneficial to further to open in rush collagen secretion, anti-aging, anti-oxidation medicine, food and cosmetic additive agent field
Hair application.
Embodiment 6
Western blotting electrophoresis detects COL1 protein expressions:
Human skin fibroblasts (HFF-1) are with the DMEM medium cultures containing 15% hyclone to growing logarithm
Phase, after being digested with 0.25% pancreatin, with 105Individual/ml is inoculated in 6 orifice plates, per hole 2ml.In 37 DEG C of CO2In incubator overnight
Culture makes cell attachment, treats that cell density length to 80% or so, culture medium is sucked, with phosphate buffer (PBS:0.8g
NaCl;0.2g KCl;2.9g Na2HPO4.12H2O;0.27g KH2PO4800ml deionized waters are dissolved in, stirring and dissolving, are settled to
1L, PH to 7.4, autoclaving are adjusted with dense HCl) wash cell 2-3 times.10ug/ml samples are added, blank adds 2% serum
Be irradiated processing using long wave ultraviolet UVA (320nm -400nm) is ultraviolet after DMEM processing 24h, cell be disposed after again
Plasma-free DMEM medium is changed to continue to cultivate 24h.Then cell culture supernatants are discarded, 1000g centrifugations 5min collects cell,
Cell is washed with the PBS of precooling twice.250ulRIPA cell pyrolysis liquids [50Mm Tris-HCl are added into the cell per hole
(PH7.4), 1%Nonidet P-40,0.25% NaTDC, 150mM NaCl, 1mM EDTA, 1Mm PMSF, 1Mm
NaF,1mM Na3VO4, each 1ug/ml aprotinin, leupeptin and pepstatin], 30min is cracked on ice.4 DEG C,
12000g centrifuges 20min, carefully draws supernatant, and supernatant is dispensed to new eppendorf pipes, draws 2ul Bradford
Method determines protein concentration.40ug pyrolysis products are transferred on pvdf membrane after 8% SDS-PAGE electrophoresis, 5% bovine serum albumin
White closing 2h;Add special primary antibody, primary antibody Col1 (1:2000) Cell Signaling Technology companies, β-actin are purchased from
(1:3000) ComWin Biotech companies, by specification operation, 4 DEG C of overnight incubations are purchased from;TBST(39g Tris,
89gNaCl, 0.29g KCl, 0.5%Tween, are settled to 1000ml, adjust PH to 7.4) washing 3 times with dense HCl, every time
5min;Then plus HRPO (HRP) mark goat-anti rabbit/mouse antibody normal temperature is incubated 1h, and secondary antibody is purchased from Cell
Signaling Technology companies, TBST are washed 3 times, each 5min;Nitrite ion colour developing is added in darkroom.
As a result as shown in figure 4, in the case of extraneous environment-stress (UVA=10.8J/cm2Irradiation), I-type collagen contains
Amount is substantially less than normal cell, and the collagen that the ultrashort peptide Purin-WH3 of dosing group, i.e. 10ug/ml can improve damage group contains
Measure to normal group.Thus illustrate that ultrashort peptide Purin-WH3 can effectively facilitate collagen expression, so ultrashort peptide Purin-
WH3 in skin repair and regeneration, stimulate Skin Cell collagen secretion, prevent skin aging, coarse anti-aging from curing U.S. etc.
Field possesses splendid DEVELOPMENT PROSPECT.
Claims (3)
1. one kind promotees the ultrashort peptide of collagen secretion, including two kinds of rush ultrashort peptides of collagen secretion:Magin-FL and Purin-WH3, it is special
Sign is:
The ultrashort peptide Magin-FL of described rush collagen secretion:A kind of straight chain small peptide, molecular weight 1205.42Da, isoelectric point are
9.02, containing 10 amino acid residues, the primary structure of complete sequence is Phe-Phe-Arg-Thr-Ser-Cys-Arg-Ser-
Val-Cys;
The ultrashort peptide Purin-WH3 of described rush collagen secretion:A kind of straight chain small peptide, molecular weight 672.88Da, isoelectric point are
9.31, containing 6 amino acid residues, the primary structure of complete sequence is Val-Val-Lys-Cys-Pro-Lys.
2. a kind of medicine for promoting the ultrashort peptide of collagen secretion and being used to prepare the reparation and regeneration of the impaired epidermis for the treatment of described in claim 1
Thing.
3. a kind of ultrashort peptide of collagen secretion that promotees described in claim 1 is as anti-aging, the main work of anti-oxidant cosmetics and skincare product
Property composition.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN201710533713.8A CN107383163B (en) | 2017-07-03 | 2017-07-03 | One kind promotees the ultrashort peptide of collagen secretion and its application |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN201710533713.8A CN107383163B (en) | 2017-07-03 | 2017-07-03 | One kind promotees the ultrashort peptide of collagen secretion and its application |
Publications (2)
Publication Number | Publication Date |
---|---|
CN107383163A true CN107383163A (en) | 2017-11-24 |
CN107383163B CN107383163B (en) | 2019-10-11 |
Family
ID=60334177
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CN201710533713.8A Active CN107383163B (en) | 2017-07-03 | 2017-07-03 | One kind promotees the ultrashort peptide of collagen secretion and its application |
Country Status (1)
Country | Link |
---|---|
CN (1) | CN107383163B (en) |
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN111888279A (en) * | 2020-09-02 | 2020-11-06 | 北京瀚梅生物科技有限公司 | Method for promoting collagen production and corresponding medicine or cosmetic |
CN114456234A (en) * | 2022-03-17 | 2022-05-10 | 中国石油大学(华东) | Antioxidant lipopeptide and preparation method and application thereof |
Citations (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101111222A (en) * | 2005-02-01 | 2008-01-23 | 伊玛吉恩有限公司 | Method for stimulation collagen synthesis and/or kgf expression |
EP2832742A1 (en) * | 2013-08-02 | 2015-02-04 | Infinitec Activos, S.L. | Peptides for the stimulation of collagen formation |
CN104402975A (en) * | 2014-12-11 | 2015-03-11 | 太原锦波生物医药科技有限公司 | Anti-aging short peptide and preparation method thereof |
CN105106028A (en) * | 2015-08-28 | 2015-12-02 | 深圳市维琪医药研发有限公司 | Polypeptide composition for hair growth |
CN105120836A (en) * | 2013-01-08 | 2015-12-02 | 诺娃细胞科技公司 | Novel peptide having collagen synthesizing abiliity and use thereof |
CN105131086A (en) * | 2015-09-28 | 2015-12-09 | 华南理工大学 | Hexapeptide and application thereof |
CN109206480A (en) * | 2017-07-03 | 2019-01-15 | 大连理工大学 | One kind promotees the ultrashort peptide of collagen secretion and its application |
-
2017
- 2017-07-03 CN CN201710533713.8A patent/CN107383163B/en active Active
Patent Citations (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101111222A (en) * | 2005-02-01 | 2008-01-23 | 伊玛吉恩有限公司 | Method for stimulation collagen synthesis and/or kgf expression |
CN105120836A (en) * | 2013-01-08 | 2015-12-02 | 诺娃细胞科技公司 | Novel peptide having collagen synthesizing abiliity and use thereof |
EP2832742A1 (en) * | 2013-08-02 | 2015-02-04 | Infinitec Activos, S.L. | Peptides for the stimulation of collagen formation |
CN104402975A (en) * | 2014-12-11 | 2015-03-11 | 太原锦波生物医药科技有限公司 | Anti-aging short peptide and preparation method thereof |
CN105106028A (en) * | 2015-08-28 | 2015-12-02 | 深圳市维琪医药研发有限公司 | Polypeptide composition for hair growth |
CN105131086A (en) * | 2015-09-28 | 2015-12-09 | 华南理工大学 | Hexapeptide and application thereof |
CN109206480A (en) * | 2017-07-03 | 2019-01-15 | 大连理工大学 | One kind promotees the ultrashort peptide of collagen secretion and its application |
Non-Patent Citations (3)
Title |
---|
HAINING YU ET AL.: ""Host defense peptides in skin secretions of Odorrana tiannanensis: Proof for other survival strategy of the frog than merely anti-microbial"", 《BIOCHIMIE》 * |
HAINING YU, ET AL.: ""Identification, eukaryotic expression and structure & function: characterizations of b-defensin like homologues from Pelodiscus sinensis"", 《DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY》 * |
XUEQING XU, ET AL.: ""The Chemistry and Biological Activities of Peptides from Amphibian Skin Secretions"", 《CHEM. REV.》 * |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN111888279A (en) * | 2020-09-02 | 2020-11-06 | 北京瀚梅生物科技有限公司 | Method for promoting collagen production and corresponding medicine or cosmetic |
CN114456234A (en) * | 2022-03-17 | 2022-05-10 | 中国石油大学(华东) | Antioxidant lipopeptide and preparation method and application thereof |
CN114456234B (en) * | 2022-03-17 | 2023-06-30 | 中国石油大学(华东) | Antioxidant lipopeptides, preparation method and application thereof |
Also Published As
Publication number | Publication date |
---|---|
CN107383163B (en) | 2019-10-11 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
CN109206480A (en) | One kind promotees the ultrashort peptide of collagen secretion and its application | |
JP5814177B2 (en) | Plant-derived elastin-binding protein ligand and method of use thereof | |
CN107344959A (en) | One kind promotees skin repair ultrashort peptide Purin WH, its preparation method and application | |
CN113248573B (en) | Application of active peptide and mesenchymal stem cell exosome for improving skin physiological characteristics in medicines or cosmetics | |
CN104968360A (en) | Compounds useful in the treatent and/or care of the skin, hair and/or mucous membranes and their cosmetic or pharmaceutical compositions | |
CN107106617A (en) | Include the cosmetics and/or medical composition and its use of product outside the bacterial cell from South Pole Pseudoalteromonas | |
CN102015764A (en) | Cosmetic or pharmaceutical compositions comprising metalloproteinase inhibitors | |
CN104922171B (en) | Use of extract of Chenopodium quinoa for preparing composition for promoting collagen production and resisting skin aging | |
Chakraborty et al. | Aqueous extract of human placenta as a therapeutic agent | |
KR20150120426A (en) | Cosmetic composition containing a brown alga extract, a yeast extract and ascorbic acid | |
Li et al. | In vitro antioxidant and anti-aging properties of swim bladder peptides from Atlantic cod (Gadus morhua) | |
CN109232714A (en) | One kind is for promoting ultrashort peptide and its application of collagen secretion | |
CN107383163B (en) | One kind promotees the ultrashort peptide of collagen secretion and its application | |
CN105662905B (en) | Purposes of the dihydromyricetin in preparing prevention dermal photodamage skin care item or drug | |
CN102188362A (en) | Autologous whole blood homogenate compound for reconstruction of autologous skin epidermis protective screen | |
Park et al. | Effects of egg shell membrane hydrolysates on skin whitening, wound healing, and UV-protection | |
CN110590912A (en) | Novel antioxidant active polypeptide OA-VI12 as well as preparation method and application thereof | |
CN101679495B (en) | Short bio-active peptides for cellular and immunological modulation | |
CN107383164B (en) | One kind is for promoting ultrashort peptide and its application of collagen secretion | |
CN109320591A (en) | A kind of polypeptide OA-GL12 and its application | |
Porto da Rocha et al. | Effects of a vitamin pool (vitamins A, E, and C) on the tissue necrosis process: experimental study on rats | |
CN111732634A (en) | Application of earthworm active peptide for inhibiting melanocyte proliferation in preparation of medicines or cosmetics | |
CN115894625A (en) | Polypeptide with anti-aging effect and application thereof | |
CN111067893B (en) | Composition and application thereof in preparation of skin repair product | |
CN107892718A (en) | A kind of polypeptide and preparation method and application |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
PB01 | Publication | ||
PB01 | Publication | ||
SE01 | Entry into force of request for substantive examination | ||
SE01 | Entry into force of request for substantive examination | ||
GR01 | Patent grant | ||
GR01 | Patent grant |