CN105153282A - Decapeptide and application thereof - Google Patents
Decapeptide and application thereof Download PDFInfo
- Publication number
- CN105153282A CN105153282A CN201510634074.5A CN201510634074A CN105153282A CN 105153282 A CN105153282 A CN 105153282A CN 201510634074 A CN201510634074 A CN 201510634074A CN 105153282 A CN105153282 A CN 105153282A
- Authority
- CN
- China
- Prior art keywords
- decapeptide
- ala
- application
- synthesis
- cell
- 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
Landscapes
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Cosmetics (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention discloses decapeptide and an application thereof. The amino acid sequence of synthetic polypeptide is as follows: al-Thr-Ala-Pro-Ala-Ala-Ser-Val-Ala-Leu, VTAPAASVAL for short, the molecular weight is 899.4, and the purity is 93.8%. The polypeptide uses a polypeptide synthesizer and is synthesized with a solid-phase synthesis method. The invention aims to provide a synthesis method which can protect red blood cell hemolysis as well as promote human skin fibroblast to proliferate and collagen to produce polypeptide, and a foundation is laid for application of the decapeptide in the fields of bio-pharmaceuticals, cosmetics and the like.
Description
Technical field
The present invention relates to the field such as bio-pharmaceuticals and makeup, be specifically related to a kind of improvement on synthesis and application thereof.
Background technology
Biologically active peptides has multiple body metabolism and physiological regulation function, absorption easy to digest, have Promote immunity to regulate, the dipeptides of the effect such as antibacterial, hypotensive, anticancer, anti-oxidant to the general name of the different peptide classes of complicated linear, ring structure, to be made up of with difference by peptide bond 25 natural amino acids and to be formed with arrangement mode.Bioactive peptide security is high, is the research topic that current international food circle is the most popular and the functional factor having development prospect.Modern nutriology shows, protein is after digestive enzyme effect and not exclusively absorb with the form of total free aminoacids, and the form greatly mainly with low peptide absorbs, and low peptide specific ionization amino acid has higher nutritive value and biological value.
Building cell oxidative damage model is the common method whether assess sample has resistance of oxidation, and red corpuscle is due to abundance, convenience of drawing materials, and is the common used material in external biological experiment.Free radical casts the first stone lipid on erythrocyte membrane and protein, makes cytolemma damaged, discharges the oxyphorase in red corpuscle, be called erythrocyte hemolysis.AAPH, H
2o
2with the material that Hemin is conventional induction erythrocyte hemolysis.
Atomic force microscope (AFM) is a kind of high-resolution novel imaging tool, cell morphology and Ultrastructural sign thereof has been widely used on biomedical boundary, its principle is that the interatomic interaction force by producing during detection probes scanning samples obtains sample topography structural information, machine software processes imaging as calculated
.free radical attack cells film makes it structure and function and loses, and cell haemolysis occurs.This conclusion is verified further by observing control group, damage group and protection group red corpuscle pattern by atomic force microscope (AFM).
Skin aging mainly the genetic predisposition (aging also referred to as the age) of people and people to the result of the physiological response (also referred to as photoaging) of environmental stress.Photoaging is the effect of external environment to the biological answer-reply of skin.Skin is usually relevant with wrinkled appearance with the shortage of normal hydration, skin sagging and lines to the response of photoaging.UVB irradiates can make active oxygen (reactiveoxygenspecies in inoblast, ROS) pile up, exceed its Scavenging activity, break oxidative and anti-oxidative balance, there is response to oxidative stress, regulate the cell response of a series of sequencing, even the old and feeble relevant signal path of regulation and control, promotes the generation of cell aging.Large quantity research shows that ROS is the important step in skin photoage generation evolution in intracellular accumulation.Human skin fibroblast is that human skin produces the main place of collagen protein, its quantity number and the productive rate of cell collagen albumen and skin aging state closely bound up.Therefore, the survival rate of human skin fibroblast and the productive rate of collagen protein are by a kind of model of evaluating skin aging state extensively approved.
Summary of the invention
The object of this invention is to provide a kind of improvement on synthesis with propagation and the collagen protein generation protected erythrocyte hemolysis and promote human skin fibroblast, can be applicable to the field such as bio-pharmaceuticals and makeup.
The present invention tests with the erythrocyte hemolysis that APPH induces and ultraviolet damage human skin fibroblast evaluates the anti-oxidant of polypeptide and anti aging effect is active.
Improvement on synthesis of the present invention is abbreviated as VTAPAASVAL, molecular weight 899.4, and sequence is: Val-Thr-Ala-Pro-Ala-Ala-Ser-Val-Ala-Leu.Wherein,
Val represents that English name is Valine, and Chinese is the amino acid whose corresponding residue of α-amino-isovaleric acid;
Thr represents that English name is Threonine, and Chinese is the amino acid whose corresponding residue of Threonine;
Ala represents that English name is Alanine, and Chinese is the amino acid whose corresponding residue of L-Ala;
Pro represents that English name is proline, and Chinese is the amino acid whose corresponding residue of proline(Pro);
Ser represents that English name is Serine, and Chinese is the amino acid whose corresponding residue of Serine;
Leu represents that English name is Leucine, and Chinese is leucic amino acid whose corresponding residue.
Aminoacid sequence of the present invention adopts standard Fmoc scheme, by the screening of resin, and rational polypeptide synthesis method.The C-end carboxyl of target polypeptides is connected with an insoluble macromolecule resin with covalent linkage form, then using this amino acid whose amino as starting point, forms peptide bond with the amino acid whose carboxyl effect of another molecule.Constantly repeat this process, namely can obtain target polypeptides product.After building-up reactions completes, remove protecting group, by peptide chain and resin isolation, namely obtain target product.Peptide systhesis is one to be repeated to add amino acid whose process, and solid phase synthesis order is from C end to the synthesis of N end.Synthesize complete, adopt high performance liquid chromatography to carry out purifying, liquid nitrogen flash freezer, vacuum lyophilization, obtain polypeptide finished product.
Final concentration is that the improvement on synthesis of 1-100 μ g/mL and normal people's erythrocyte mix by the present invention, hatches, damages after 2h, make cell haemolysis inhibiting rate reach 57.74% ~ 80.66% through AAPH.With after the improvement on synthesis process of 100 μ g/mL compared with the red corpuscle group only damaged with AAPH, its pattern is more smooth than simple AAPH treatment group, in order, SOD vigor rises to 5.2740mgprot/mL by 2.5976mgprot/mL, result shows, after improvement on synthesis process, erythrocytic SOD activity improves a lot, and can apply in the field such as biological medicine and makeup.
Concentration is that the improvement on synthesis of 1-10 μ g/mL adds in human skin fibroblast nutrient solution and hatches, through medium wave ultraviolet (UVB) 80mJ/cm by the present invention
2after damage, cell survival rate is made to improve 7.8-22.74%.Meanwhile, collagen protein yield rises to 14.0976 ± 1.4361 μ g/mL of improvement on synthesis group by 11.9512 ± 1.2067 μ g/mL of model group, and collagen protein yield improves 4.69-17.96%.
Compared with prior art, tool of the present invention has the following advantages and technique effect:
The present invention has synthesized this peptide first; and the Red Blood Cells of Normal Persons being applied to AAPH damage is protected; erythrocyte hemolysis rate is significantly reduced; SOD activity is greatly improved; simultaneously; the growth of improvement on synthesis to the human skin fibroblast that ultraviolet is damaged has promoter action, can promote the generation of its collagen protein simultaneously.
Accompanying drawing explanation
Fig. 1 is the ESI-MS collection of illustrative plates of improvement on synthesis Val-Thr-Ala-Pro-Ala-Ala-Ser-Val-Ala-Leu, and wherein X-coordinate is m/z (mass-to-charge ratio value), ordinate zou is RelativeAbundance (relative intensity).
Fig. 2 is the Red Blood Cells of Normal Persons haemolysis inhibiting rate change curve carrying out AAPH damage after improvement on synthesis adds.
Fig. 3 is the erythrocytic atomic force microscope of different treatment group (AFM) image.
Embodiment
Below in conjunction with specific examples, the invention will be further described, but enforcement of the present invention and protection domain are not limited thereto.For the processing parameter do not indicated especially, can refer to routine techniques and carry out.
solid-phase synthesis peptides
Select macromolecule resin (Chinese Peptide Co., Ltd.), according to aminoacid sequence
The feature of Val-Thr-Ala-Pro-Ala-Ala-Ser-Val-Ala-Leu, first the carboxyl of Leu is connected with a resin with the form of covalent linkage, then the amino of Phe and the carboxyl of Phe shrink and react, after process, add Glu again, the amino of Phe and the carboxyl reaction of Glu, add amino acid successively from right to left, after having added last Phe amino acid, then excise resin and namely obtain target polypeptides.High-efficient liquid phase chromatogram purification obtains last product, and use SepaxGP-C18 chromatographic column, size 4.6*150mm, liquid-phase condition is as follows, mobile phase A: the water containing 0.1% trifluoroacetic acid (TFA); Mobile phase B: the solution (80% acetonitrile+20% water) containing 0.09%TFA, elution flow rate is that in 1.0mL/min, 20min, B Phase Proportion rises to 43% by 23%, determined wavelength 220nm.Liquid nitrogen flash freezer, lyophilize, purity reaches more than 90%, and identifies structure (as shown in Figure 1) through ESI-MS.
the protection application that improvement on synthesis damages human skin fibroblast UVB
Human skin fibroblast cultivate in perfect medium, perfect medium by basic medium DMEM in high glucose, 10% foetal calf serum (v/v), and 1% dual anti-(being made up of penicillin and Streptomycin sulphate, v/v) composition.Be placed in 37 DEG C, CO
2volume fraction is in the saturated humidity incubator of 5%.Liquid is changed 1 time every 2d.Treat that cell covers with about 90% of culturing bottle, get it and be inoculated in 96 well culture plates, every hole 100 μ L, concentration is 5 × 10
4cells/mL.After Growth of Cells 24h, inhale and abandon nutrient solution, wash 1 time with 200 μ LPBS, add 200 μ LPBS, use 80mJ/cm
2uVB irradiates, and inhale and abandon PBS, every hole adds 200 μ L samples (zero-dose DMEM in high glucose replaces, and is normal control), continues to cultivate 72h, inhales and abandon nutrient solution, adopts mtt assay to detect cell survival rate (the results are shown in Table 1).
Table 1
| UVB | Improvement on synthesis+UVB | |
| Human skin fibroblast survival rate | 1 | 1.2274 |
improvement on synthesis promotes the application that the human skin fibroblast collagen protein of UVB damage produces
Get the cell of above-mentioned treatment group, inhale and abandon nutrient solution, with aseptic washing cell surface twice, add ice-cold 70% ethanol 200 μ L and be fixed ,-80
oat least 10min placed by C refrigerator, and after taking-up, with aseptic washing cell surface twice, after air-dried moisture, every hole adds the saturated picric acid of 200 μ L1%-scarlet dye liquor (m/v), in 4
ogently shake 24h under C condition, inhale and abandon dye liquor, with aseptic washing 3 times, till not having staining fluid to wash out, add 150 μ L1MNaOH solution, 150r/min, concussion 15min, every hole is taken out 100 μ L and is placed in 96 orifice plates, measures the absorbance (the results are shown in Table 2) at 492nm place.
Table 2
| UVB | Improvement on synthesis+UVB | |
| Human skin fibroblast collagen protein productive rate (μ g/mL) | 11.9512±1.2067 | 14.0976 ±1.4361 |
the protection application that improvement on synthesis damages Red Blood Cells of Normal Persons AAPH
Extract health adult (less than 30 years old) blood with the anticoagulant tube (antithrombotics Trisodium Citrate: blood=1:9, v/v) containing Trisodium Citrate and be put in 4 DEG C of Refrigerator stores, use in one week.Face the used time, blood to be placed in centrifuge tube in the centrifugal 8-15min of 1000 ~ 1500g, to remove the blood plasma on upper strata, red corpuscle PBS(pH=7.4) wash 2-3 time, until supernatant liquor is colourless.Last in whizzer the centrifugal 8-15min of 1000 ~ 1500g, remove supernatant liquor, obtain pcv closely, being diluted to concentration with PBS is 20%(volume, v/v) red cell suspension.The improvement on synthesis process red corpuscle of independent use 100 μ g/mL, jointly hatches 2h as blank group using 0.1mL20% red cell suspension and 0.3mLPBS, determines that sample does not have hemolytic.
application Example 1
The improvement on synthesis that 0.1mL20% red cell suspension is 0 μ g/mL through 0.1mL concentration (replaces with PBS, be model group) after pre-treatment 20min, add the AAPH solution that 0.2mL final concentration is 100mM, 2h is hatched in microseism, lucifuge, the reactant solution 50 μ L PBS damping fluid getting each treatment group is diluted to 1mL, the centrifugal 12min of 1500g, get supernatant liquor in 96 orifice plates, its absorbancy is surveyed at 540nm place by microplate reader, similarly, contrast as full haemolysis with distilled water diluting reaction mixture, calculate hemolysis rate.(the results are shown in Figure 2) simultaneously, by each treatment group cell whizzer in the centrifugal 12min of 1500g, collecting cell precipitate, with PBS wash 3 times centrifugal, abandoning supernatant, again resuspended.During film-making, getting 10 μ L red corpuscle re-suspension liquid is evenly applied on clean sheet mica (require cell zero lap, do not reunite), then 2.5%(volume is used, v/v) glutaraldehyde fixed cell, after 5min, with ultrapure water silicon chip 3 times, natural air drying silicon chip, finally be placed in atomic force microscope, scanning cell morphology under tapping-mode, by NanoScope software analysis experimental data (the results are shown in Figure 3).
Fig. 2 is the Red Blood Cells of Normal Persons haemolysis inhibiting rate change curve carrying out AAPH damage after improvement on synthesis adds.Result shows, within the scope of 1-10 μ g/mL, the concentration of improvement on synthesis and erythrocytic haemolysis inhibiting rate present the mode that concentration dependent significantly increases, and continues to increase concentration to 100 μ g/mL, and haemolysis inhibiting rate does not have significance to change.Wherein X-coordinate is Concentration (concentration), ordinate zou is Hemolysisinhibition (haemolysis inhibiting rate).
Fig. 3 is the erythrocytic atomic force microscope of different treatment group (AFM) image.Wherein a is normoerythrocyte, and b is the red corpuscle of the AAPH process 2h of 100mM, and c adds the red corpuscle that 100mMAAPH cultivates 2h again after being the synthetic peptide Val-Thr-Ala-Pro-Ala-Ala-Ser-Val-Ala-Leu pre-treatment 20min with 100 μ g/mL.Result shows, normoerythrocyte has typical bi-concave structure, and cell surface is smooth, and surrounding height is basically identical.AAPH treatment group cell surface becomes coarse, and cell seriously subsides, height reduction, out-of-shape.The pretreated protection group of improvement on synthesis, cell injury degree obviously weakens, and surrounding height obviously increases, and presents circular configuration.
application Example 2
0.1mL20% red cell suspension is after the improvement on synthesis pre-treatment 20min that 0.1mL concentration is 1 μ g/mL, add the AAPH solution that 0.2mL final concentration is 100mM, 2h is hatched in microseism, lucifuge, the reactant solution 50 μ L PBS damping fluid getting each treatment group is diluted to 1mL, the centrifugal 12min of 1500g, gets supernatant liquor in 96 orifice plates, its absorbancy is surveyed at 540nm place by microplate reader, similarly, contrast as full haemolysis with distilled water diluting reaction mixture, calculate hemolysis rate (the results are shown in Figure 2).
application Example 3
0.1mL20% red cell suspension is after the improvement on synthesis pre-treatment 20min that 0.1mL concentration is 5 μ g/mL, add the AAPH solution that 0.2mL final concentration is 100mM, 2h is hatched in microseism, lucifuge, the reactant solution 50 μ L PBS damping fluid getting each treatment group is diluted to 1mL, the centrifugal 12min of 1500g, gets supernatant liquor in 96 orifice plates, its absorbancy is surveyed at 540nm place by microplate reader, similarly, contrast as full haemolysis with distilled water diluting reaction mixture, calculate hemolysis rate (the results are shown in Figure 2).
application Example 4
0.1mL20% red cell suspension is after the improvement on synthesis pre-treatment 20min that 0.1mL concentration is 10 μ g/mL, add the AAPH solution that 0.2mL final concentration is 100mM, 2h is hatched in microseism, lucifuge, the reactant solution 50 μ L PBS damping fluid getting each treatment group is diluted to 1mL, the centrifugal 12min of 1500g, gets supernatant liquor in 96 orifice plates, its absorbancy is surveyed at 540nm place by microplate reader, similarly, contrast as full haemolysis with distilled water diluting reaction mixture, calculate hemolysis rate (the results are shown in Figure 2).
application Example 5
0.1mL20% red cell suspension is after the improvement on synthesis pre-treatment 20min that 0.1mL concentration is 100 μ g/mL, add the AAPH solution that 0.2mL final concentration is 100mM, 2h is hatched in microseism, lucifuge, the reactant solution 50 μ L PBS damping fluid getting each treatment group is diluted to 1mL, the centrifugal 12min of 1500g, gets supernatant liquor in 96 orifice plates, its absorbancy is surveyed at 540nm place by microplate reader, similarly, contrast as full haemolysis with distilled water diluting reaction mixture, calculate hemolysis rate.(the results are shown in Figure 2) simultaneously, by each treatment group cell whizzer in the centrifugal 12min of 1500g, collecting cell precipitate, with PBS wash 3 times centrifugal, abandoning supernatant, again resuspended.During film-making, getting 10 μ L red corpuscle re-suspension liquid is evenly applied on clean sheet mica (require cell zero lap, do not reunite), then the glutaraldehyde fixed cell of 2.5% is used, after 5min, with ultrapure water silicon chip 3 times, natural air drying silicon chip, is finally placed in atomic force microscope, scanning cell morphology under tapping-mode, by NanoScope software analysis experimental data (the results are shown in Figure 3).
application Example 6
0.1mL20% red cell suspension is that 0 μ g/mL(PBS replaces through 0.1mL concentration, be Normal group) improvement on synthesis pre-treatment 20min after, adding 0.2mL final concentration is that the AAPH solution of 0mM (replaces with PBS, be normal control), 2h is hatched in microseism, lucifuge, the reactant solution 50 μ L PBS damping fluid getting each treatment group is diluted to 1mL, the centrifugal 12min of 1500g, get supernatant liquor in 96 orifice plates, its absorbancy is surveyed at 540nm place by microplate reader, similarly, contrast as full haemolysis with distilled water diluting reaction mixture, calculate hemolysis rate.(the results are shown in Figure 2) simultaneously, by each treatment group cell whizzer in the centrifugal 12min of 1500g, collecting cell precipitate, with PBS wash 3 times centrifugal, abandoning supernatant, again resuspended.During film-making, getting 10 μ L red corpuscle re-suspension liquid is evenly applied on clean sheet mica (require cell zero lap, do not reunite), then the glutaraldehyde fixed cell of 2.5% is used, after 5min, with ultrapure water silicon chip 3 times, natural air drying silicon chip, is finally placed in atomic force microscope, scanning cell morphology under tapping-mode, by NanoScope software analysis experimental data (the results are shown in Figure 3).
application Example 7
Table 3
| AAPH | Improvement on synthesis+AAPH | |
| T-SOD activity (mgprot/mL) | 2.5976 | 5.2740 |
0.1mL20% red cell suspension is that 5 μ g/mL(PBS replace through 0.1mL concentration, be Normal group) improvement on synthesis pre-treatment 20min after, adding 0.2mL final concentration is that the AAPH solution of 0mM (replaces with PBS, be normal control), 2h is hatched in microseism, lucifuge, and by each treatment group cell whizzer in the centrifugal 12min of 1500g, collecting cell precipitates, with PBS wash 3 times centrifugal, add 4
othe ultrapure water of C precooling, 150r/min shakes the centrifugal 30min of 10min, 10000g, collects supernatant liquor for subsequent use, carries out the SOD activity (the results are shown in Table 3) measured wherein according to the specification sheets of test kit (Nanjing is built up).
Claims (6)
1. a decapeptide, is characterized in that the aminoacid sequence of this synthesis decapeptide is Val-Thr-Ala-Pro-Ala-Ala-Ser-Val-Ala-Leu.
2. the application of a kind of decapeptide according to claim 1, is characterized in that described decapeptide to mix with red corpuscle, and under the effect of AAPH, after hatching 2h, make cell haemolysis inhibiting rate be 57.74% ~ 80.66%, its pattern is more smooth, orderly than simple AAPH treatment group; The concentration of described decapeptide is 1-100 μ g/mL.
3. application according to claim 2, is characterized in that described decapeptide can make cell haemolysis inhibiting rate up to 80.66 ± 1.09%.
4. application according to claim 2, is characterized in that described decapeptide can make cell SOD activity rise to 5.2740mgprot/mL by 2.5976mgprot/mL; Described decapeptide concentration is 100 μ g/mL.
5. the application of a kind of decapeptide according to claim 1, it is characterized in that, under the effect of UVB, described decapeptide is mixed with human skin fibroblast, after hatching 72h, cell survival rate is made to improve 7.8-22.74%, simultaneously, collagen protein yield improves 4.69-17.96%, and the concentration of described decapeptide is 1-10 μ g/mL.
6. the application of a kind of decapeptide according to claim 1 in preparation biological medicine or makeup.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201510634074.5A CN105153282B (en) | 2015-09-28 | 2015-09-28 | A kind of decapeptide and its application |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201510634074.5A CN105153282B (en) | 2015-09-28 | 2015-09-28 | A kind of decapeptide and its application |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN105153282A true CN105153282A (en) | 2015-12-16 |
| CN105153282B CN105153282B (en) | 2018-02-23 |
Family
ID=54794363
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201510634074.5A Active CN105153282B (en) | 2015-09-28 | 2015-09-28 | A kind of decapeptide and its application |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN105153282B (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR101753874B1 (en) | 2015-12-30 | 2017-07-19 | 주식회사 차밍코스메틱 | A cosmetic composition comprising a decapeptide as an active ingredient |
| CN117247427A (en) * | 2023-05-16 | 2023-12-19 | 杭州禾泰健宇生物科技有限公司 | Peptide compound, composition and application thereof |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2012150968A1 (en) * | 2011-05-02 | 2012-11-08 | Renewuel Llc | System and method of co-cultivating microalgae with fungus |
| CN102875640A (en) * | 2012-09-29 | 2013-01-16 | 北京林业大学 | Method for extracting small-molecule peptides of spirulina |
| WO2014058322A1 (en) * | 2012-10-11 | 2014-04-17 | Institutt For Energiteknikk | Method for the production of aqueous nutrient source for algae aquaculture farming |
| CN104561208A (en) * | 2015-01-21 | 2015-04-29 | 华南理工大学 | Triple-enzyme hydrolysis preparation method of anti-tumor polypeptides of spirulina |
-
2015
- 2015-09-28 CN CN201510634074.5A patent/CN105153282B/en active Active
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2012150968A1 (en) * | 2011-05-02 | 2012-11-08 | Renewuel Llc | System and method of co-cultivating microalgae with fungus |
| CN102875640A (en) * | 2012-09-29 | 2013-01-16 | 北京林业大学 | Method for extracting small-molecule peptides of spirulina |
| WO2014058322A1 (en) * | 2012-10-11 | 2014-04-17 | Institutt For Energiteknikk | Method for the production of aqueous nutrient source for algae aquaculture farming |
| CN104561208A (en) * | 2015-01-21 | 2015-04-29 | 华南理工大学 | Triple-enzyme hydrolysis preparation method of anti-tumor polypeptides of spirulina |
Non-Patent Citations (7)
| Title |
|---|
| CHEYLA ROMAY等: "Phycocyanin is an Antioxidant Protector of Human Erythrocytes Against Lysis by Peroxyl Radicals", 《J. PHARM. PHARMACOL.》 * |
| HUA-MING CHEN等: "Antioxidant Activity of Designed Peptides Based on the Antioxidative Peptide Isolated from Digests of a Soybean Protein", 《J. AGRIC. FOOD CHEM.》 * |
| RYAN J. ELIAS等: "Antioxidant Activity of Proteins and Peptides", 《CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION》 * |
| 严群芳等: "大豆抗氧化肽抗氧化的活性研究", 《动物营养与饲料研究——第五届全国饲料营养学术研讨会论文集》 * |
| 孙宜君等: "双酶法制备螺旋藻多肽的工艺研究", 《天然产物研究与开发》 * |
| 欧贇等: "螺旋藻抗氧化肽的制备及其体外活性研究", 《食品与生物技术学报》 * |
| 王莉等: "魔芋多肽的物理特性和抗氧化特性", 《西北农业学报》 * |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR101753874B1 (en) | 2015-12-30 | 2017-07-19 | 주식회사 차밍코스메틱 | A cosmetic composition comprising a decapeptide as an active ingredient |
| CN117247427A (en) * | 2023-05-16 | 2023-12-19 | 杭州禾泰健宇生物科技有限公司 | Peptide compound, composition and application thereof |
Also Published As
| Publication number | Publication date |
|---|---|
| CN105153282B (en) | 2018-02-23 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN105131086A (en) | Hexapeptide and application thereof | |
| AU2010213094B2 (en) | Peptides used in the treatment and/or care of the skin, mucous membranes and/or scalp and their use in cosmetic or pharmaceutical compositions | |
| KR101813294B1 (en) | Peptides used in the treatment and/or care of the skin, mucous membranes and/or hair and its use in cosmetic or pharmaceutical compositions | |
| US20090082280A1 (en) | Plant-derived elastin binding protein ligands and methods of using the same | |
| CN105218639A (en) | A kind of seven peptides and application thereof | |
| AU2019317812B2 (en) | Compounds useful for the treatment and/or care of the skin, hair, nails and/or mucous membranes | |
| AU2020217620A1 (en) | Compounds useful for the treatment and/or care of the skin, hair, nails and/or mucous membranes | |
| CN116829169A (en) | Synthetic peptides, and cosmetic or pharmaceutical compositions and uses thereof | |
| CN105131085A (en) | Pentapeptide and application thereof | |
| CN105175507A (en) | Pentadecapeptide and application thereof | |
| CN105153282A (en) | Decapeptide and application thereof | |
| CN113930471A (en) | Bird's nest active peptide and preparation method and application thereof | |
| CN116535463B (en) | Active peptide, composition and use thereof | |
| CN117050146A (en) | Hyaluronic acid modified cosmetic peptide, preparation method and application thereof | |
| CN102558298A (en) | Method for synthesizing tetrapeptide isomers by using solid phase peptide synthesis method and applications of tetrapeptide isomers | |
| CN105175497A (en) | Octapeptide and application thereof | |
| Choi et al. | Design and efficient synthesis of novel ascorbyl conjugated peptide with high collagen biosynthesis stimulating effects | |
| KR101224809B1 (en) | Retinoic acid derivative, process for preparing the same, and cosmetic composition comprising the same | |
| CN101265292B (en) | Polypeptides substances, preparing method and use thereof | |
| CN117304266B (en) | Skin treatment polypeptide, composition and application thereof | |
| CN117304265B (en) | Skin care polypeptide, composition and application thereof | |
| CN115785257A (en) | Pentadecapeptide based on giant salamander hydrolyzed collagen and application thereof | |
| CN106916204B (en) | Acetamidoated heptapeptide, and purification method and application thereof | |
| CN105175496A (en) | Heptapeptide PGKPLFL and application thereof | |
| CN118063547A (en) | Cyclic octapeptide and compositions and uses thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant | ||
| TR01 | Transfer of patent right |
Effective date of registration: 20210125 Address after: 523808 Room 203, unit 2, building 38, No.4, Keji 10th Road, Songshanhu Park, Dongguan City, Guangdong Province Patentee after: Guangdong geometric Cell Biotechnology Co.,Ltd. Address before: 511458 Guangdong, Guangzhou, Nansha District, 25 South Road, South China Road, Guangzhou, China Patentee before: SOUTH CHINA University OF TECHNOLOGY |
|
| TR01 | Transfer of patent right |