CN105153282B - A kind of decapeptide and its application - Google Patents
A kind of decapeptide and its application Download PDFInfo
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Abstract
The invention discloses a kind of decapeptide and its application, the amino acid sequence of the synthesis polypeptide is as follows：Val Thr Ala Pro Ala Ala Ser Val Ala Leu, are abbreviated as VTAPAASVAL, molecular weight 899.4, purity 93.8%.The polypeptide of the present invention uses Peptide synthesizer, is synthesized using solid-phase synthesis.The purpose of invention is to provide a kind of synthetic method of polypeptide caused by propagation for having protection erythrocyte hemolysis and promoting human skin fibroblasts and collagen, is laid the foundation for its application in fields such as bio-pharmaceuticals, cosmetics.
Description
Technical field
The present invention relates to the field such as bio-pharmaceuticals and cosmetics, and in particular to a kind of synthesis polypeptide and its application.
Background technology
Biologically active peptide is that have a variety of body metabolisms and physiological regulation function, absorption easy to digest, have promote immunological regulation,
The dipeptides of the effect such as antibacterial, hypotensive, anticancer, anti-oxidant to complexity linear, loop configuration different peptides general name, by 25
Individual natural amino acid is made up of peptide bond with different form with arrangement mode.Active peptide security is high, is current international food
The function factor of the most popular research topic in boundary and great development prospect.Modern nutriology shows that protein is made through digestive enzyme
Not fully absorbed in the form of free amino acid after, absorbed mostly in the form of low peptide, and low peptide specific ionization amino acid
With higher nutritive value and biological value.
Structure cell oxidative damage model be evaluate sample whether have oxidation resistance common method, and red blood cell by
It is the common used material in external biological experiment in abundance, convenient material drawing.Free radical casts the first stone the lipid on erythrocyte membrane
And protein, make cell membrane damaged, discharge the hemoglobin in red blood cell, referred to as erythrocyte hemolysis.AAPH、H2O2With
Hemin is the material of conventional induction erythrocyte hemolysis.
AFM (AFM) is a kind of high-resolution new imaging tool, has been used extensively on biomedical boundary
In cell morphology and its sign of ultra microstructure, its principle is mutual between caused atom when scanning sample by detection probe
Active force obtains sample topography structural information, is imaged through computer software processing.Free radical attack cells film be allowed to structure and
Function is lost, and cell haemolysis occurs.This conclusion is by using AFM（AFM）Observe control group, damage group and protection
Group red blood cell pattern is further verified.
Skin aging be mainly people genetic predisposition (also referred to as age aging) and people to the physiological reaction of environmental stress
The result of (also referred to as light aging).Light aging is effect of the external environment to the biological answer-reply of skin.Skin is to light aging
Shortage, skin sagging and lines and wrinkled appearance of the response generally with normal aquation are relevant.UVB irradiations can make into
Fiber finer intracellular reactive oxygen species generation (reactive oxygen species, ROS) accumulate, exceeded its Scavenging activity, break oxidation with
Anti-oxidant balance, response to oxidative stress occurs, adjust a series of cell effect of sequencing, or even the signal that regulation and control aging is related
Path, promote the generation of cell ageing.Numerous studies show that the accumulations of ROS in the cell are skin photoage occurrence and development
Important step in journey.Human skin fibroblasts be application on human skin production collagen main place, its quantity number and it is thin
The yield of born of the same parents' collagen and skin senescence state are closely bound up.Therefore, the survival rate of human skin fibroblasts and collagen egg
White yield is a kind of model for the evaluation skin senescence state being widely recognized as.
The content of the invention
It is an object of the invention to provide a kind of increasing for having protection erythrocyte hemolysis and promoting human skin fibroblasts
Grow with collagen caused by synthesis polypeptide, can be applied to the field such as bio-pharmaceuticals and cosmetics.
The present invention is more to evaluate with the erythrocyte hemolysis experiment of APPH inductions and ultraviolet damage human skin fibroblasts
The anti-oxidant and anti aging effect of peptide is active.
Synthesis polypeptide 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 corresponding residue of the amino acid of valine；
Thr represents that English name is Threonine, and Chinese is the corresponding residue of the amino acid of threonine；
Ala represents that English name is Alanine, and Chinese is the corresponding residue of the amino acid of alanine；
Pro represents that English name is proline, and Chinese is the corresponding residue of the amino acid of proline；
Ser represents that English name is Serine, and Chinese is the corresponding residue of the amino acid of serine；
Leu represents that English name is Leucine, and Chinese is the corresponding residue of the amino acid of leucine.
Amino acid sequence of the present invention uses standard Fmoc schemes, and by the screening of resin, rational polypeptide closes
Into method.The C- end carboxyls of target polypeptides are connected in the form of covalent bond with an insoluble macromolecule resin, then with this
The amino of individual amino acid acts on forming peptide bond as starting point with the carboxyl of another molecule amino acid.This process is constantly repeated, i.e.,
Target polypeptides product can be obtained.After the completion of synthetic reaction, protection group is removed, peptide chain is separated with resin, that is, obtain target production
Thing.Peptide systhesis is the process that amino acid is added in a repetition, and synthesis in solid state order synthesizes from C-terminal to N ends.Synthesis finishes, and adopts
Purified with high performance liquid chromatography, liquid nitrogen flash freezer, vacuum freeze drying, obtain polypeptide finished product.
The present invention mixes final concentration of 1-100 μ g/mL synthesis polypeptide and normal human red cell, is incubated, warp
After AAPH damages 2 h so that cell haemolysis inhibiting rate reaches 57.74% ~ 80.66%.Handled with 100 μ g/mL synthesis polypeptide
Afterwards with only with AAPH damage red blood cell group compared with, its pattern is more smooth than simple AAPH treatment groups, in order, SOD vigor by
2.5976 mgprot/mL rise to 5.2740 mgprot/mL, the results showed that, the SOD activity of red blood cell after synthesis polypeptide processing
Improve a lot, can be applied in the field such as biological medicine and cosmetics.
The synthesis polypeptide that concentration is 1-10 μ g/mL is added in human skin fibroblasts nutrient solution and is incubated by the present invention, is passed through
Medium wave is ultraviolet（UVB）80mJ/cm2After damage so that cell survival rate improves 7.8-22.74%.Meanwhile collagen yield
14.0976 ± 1.4361 μ g/mL of synthesis polypeptide group, collagen are risen to by 11.9512 ± 1.2067 μ g/mL of model group
Albumen yield improves 4.69-17.96%.
Compared with prior art, the invention has the advantages that and technique effect：
The present invention has synthesized the peptide first, and is protected applied to the Red Blood Cells of Normal Persons of AAPH damages so that red
Cell hemolysis rate significantly reduces, and SOD activity is greatly improved, meanwhile, synthesis polypeptide is to the application on human skin of ultraviolet damage into fiber
The growth of cell has facilitation, while can promote the generation of its collagen.
Brief description of the drawings
Fig. 1 is synthesis polypeptide Val-Thr-Ala-Pro-Ala-Ala-Ser-Val-Ala-Leu ESI-MS collection of illustrative plates, its
Middle abscissa is m/z (mass-to-charge ratio value), ordinate is Relative Abundance (relative intensity).
Fig. 2 is the Red Blood Cells of Normal Persons haemolysis inhibiting rate change curve of progress AAPH damages after synthesis polypeptide addition.
Fig. 3 is the AFM of different disposal group red blood cell（AFM）Image.
Embodiment
Below in conjunction with instantiation, the invention will be further described, but the implementation of the present invention and protection domain are not limited to
This.For especially not dated technological parameter, routine techniques progress can refer to.
Solid-phase synthesis peptides
From macromolecule resin（Chinese Peptide Co., Ltd.）, according to amino acid sequence
Val-Thr-Ala-Pro-Ala-Ala-Ser-Val-Ala-Leu feature, first by Leu carboxyl with covalent bond
Form be connected with a resin, then Phe amino and Phe carboxyl shrink reaction, after processing, then add Glu, Phe's
The carboxyl reaction of amino and Glu, adds amino acid from right to left successively, after having added last Phe amino acid, then cuts off resin
Obtain target polypeptides.High-efficient liquid phase chromatogram purification obtains product to the end, uses SepaxGP-C18 chromatographic columns, size 4.6*
150mm, liquid-phase condition is as follows, mobile phase A:Contain 0.1% trifluoroacetic acid（TFA）Water；Mobile phase B:Contain 0.09%TFA's
Solution (water of 80% acetonitrile+20%), B Phase Proportions rise to 43% by 23% in elution flow rate 1.0mL/min, 20 min, detect ripple
Long 220nm.Liquid nitrogen flash freezer, freeze-drying, purity reaches more than 90%, and identifies structure through ESI-MS（As shown in Fig. 1）.
The protection application that synthesis polypeptide is damaged to human skin fibroblasts UVB
Human skin fibroblasts culture in complete medium, complete medium by basal medium DMEM in high glucose,
10% hyclone（v/v）, and 1% dual anti-(being made up of penicillin and streptomysin, v/v) composition.It is placed in 37 DEG C, CO2Body
Fraction is in 5% saturated humidity incubator.Liquid is changed every 2 d 1 time.Treat that cell covers with 90% of blake bottle or so, take it
It is inoculated in 96 well culture plates, per the μ L of hole 100, concentration is 5 × 104cells/mL.After the h of cell growth 24, culture is abandoned in suction
Liquid, washed 1 time with 200 μ L PBS, 200 μ L PBS are added, with 80 mJ/cm2UVB is irradiated, and PBS is abandoned in suction, and 200 μ L are added per hole
Sample (zero-dose is substituted with DMEM in high glucose, as normal control), continue to cultivate 72 h, nutrient solution is abandoned in suction, is examined using MTT methods
Survey cell survival rate（It the results are shown in Table 1）.
Table 1
| UVB | Synthesis polypeptide+UVB | |
| Human skin fibroblasts survival rate | 1 | 1.2274 |
Synthesis polypeptide promotes to apply caused by the human skin fibroblasts collagen of UVB damages
The cell of above-mentioned treatment group is taken, nutrient solution is abandoned in suction, adds ice-cold 70% ethanol with sterile washing cell surface twice
200 μ L are fixed, -80oC refrigerators place at least 10min, after taking-up, air-dry water with sterile washing cell surface twice
After point, the saturation picric acid of 200 μ L 1%-scarlet dye liquor is added per hole（m/v）, in 4o24 h are gently shaken under the conditions of C, dye liquor is abandoned in suction,
Washed 3 times with sterile, untill being washed out without dyeing liquor, add 150 μ L 1M NaOH solutions, 150 r/min, concussion 15
Min, 100 μ L are taken out per hole and are placed in 96 orifice plates, determine the absorbance at 492nm（It the results are shown in Table 2）.
Table 2
| UVB | Synthesis polypeptide+UVB | |
| Human skin fibroblasts collagen yield（µg/mL） | 11.9512±1.2067 | 14.0976 ±1.4361 |
The protection application that synthesis polypeptide is damaged to Red Blood Cells of Normal Persons AAPH
With anticoagulant tube (the anti-coagulants sodium citrate containing sodium citrate：Blood=1：9, v/v) health adult is extracted（30 years old
Below）Blood is put in 4 DEG C of refrigerators and preserved, and is used in one week.Face the used time, blood is placed in centrifuge tube in 1000 ~ 1500 g
8-15 min are centrifuged, remove the blood plasma on upper strata, red blood cell PBS（pH=7.4）Wash 2-3 times, until supernatant is colourless.
8-15 min most are centrifuged after 1000 ~ 1500 g in centrifuge, supernatant is removed, obtains close packed cell volume, use PBS
Concentration is diluted to as 20%（Volume, v/v）Red cell suspension.Red blood cell individually is handled with 100 μ g/mL synthesis polypeptide, with
The red cell suspensions of 0.1 mL 20% and 0.3 mL PBS are incubated 2 h as blank control group jointly, determine that sample does not have
Hemolytic.
Application Example 1
Synthesis polypeptide of the red cell suspensions of 0.1 mL 20% through 0.1 mL concentration for 0 μ g/mL（Substituted with PBS, be
Model group）After pre-processing 20 min, final concentration of 100 mM of 0.2 mL AAPH solution is added, microseism, lucifuge are incubated
2 h are educated, take the μ L of reactant solution 50 of each treatment group to be diluted to 1 mL, 1500 g centrifugations 12 with PBS buffer solutions
Min, supernatant is taken in 96 orifice plates, its absorbance is surveyed at 540 nm with ELIASA, it is similarly, anti-with distilled water diluting
Answer mixture to be compareed as full haemolysis, calculate hemolysis rate.（As a result Fig. 2 is seen）Meanwhile by each treatment group cell centrifuge in
1500 g centrifuge 12 min, collect cell precipitation, wash 3 centrifugations with PBS, abandoning supernatant, are resuspended again.During film-making, 10 are taken
μ L red blood cells re-suspension liquids are uniformly applied on the mica sheet of cleaning（It is required that cell is non-overlapping, does not reunite）, then with 2.5%（Volume,
v/v）Glutaraldehyde fix cell, after 5 min, with ultrapure water silicon chip 3 times, natural air drying silicon chip, be finally placed in atomic force
On microscope, the scanning cell morphology under tapping-mode, with NanoScope software analysis experimental datas（As a result Fig. 3 is seen）.
Fig. 2 is the Red Blood Cells of Normal Persons haemolysis inhibiting rate change curve of progress AAPH damages after synthesis polypeptide addition.As a result
Show, in the range of 1-10 μ g/mL, the concentration of synthesis polypeptide and the haemolysis inhibiting rate of red blood cell are presented concentration dependent and dramatically increased
Mode, continue increase concentration there is no conspicuousness change to 100 μ g/mL, haemolysis inhibiting rate.Wherein abscissa is
Concentration (concentration), ordinate are Hemolysis inhibition (haemolysis inhibiting rate).
Fig. 3 is the AFM of different disposal group red blood cell（AFM）Image.Wherein a is normocyte, b
2 h red blood cell is handled for 100 mM AAPH, c is the synthetic peptide Val-Thr-Ala-Pro- with 100 μ g/mL
Ala-Ala-Ser-Val-Ala-Leu pre-processes the red blood cell for adding 100 mM AAPH to cultivate 2 h again after 20 min.
As a result show, normocyte has typical bi-concave structure, and cell surface is smooth, and surrounding is highly basically identical.At AAPH
Reason group cell surface becomes coarse, and cell seriously collapses, height reduction, in irregular shape.The protection group of synthesis polypeptide pretreatment,
Cellular damage degree substantially weakens, and the obvious increase of surrounding height, circular configuration is presented.
Application Example 2
The red cell suspensions of 0.1 mL 20% pre-process 20 min through the synthesis polypeptide that 0.1 mL concentration is 1 μ g/mL
Afterwards, final concentration of 100 mM of 0.2 mL AAPH solution is added, microseism, lucifuge are incubated 2 h, take the anti-of each treatment group
The μ L of thing solution 50 are answered to be diluted to 1 mL with PBS buffer solutions, 1500 g centrifuge 12 min, take supernatant in 96 orifice plates
In, its absorbance is surveyed at 540 nm with ELIASA, similarly, full haemolysis pair is used as by the use of distilled water diluting reactant mixture
According to calculating hemolysis rate（As a result Fig. 2 is seen）.
Application Example 3
The red cell suspensions of 0.1 mL 20% pre-process 20 min through the synthesis polypeptide that 0.1 mL concentration is 5 μ g/mL
Afterwards, final concentration of 100 mM of 0.2 mL AAPH solution is added, microseism, lucifuge are incubated 2 h, take the anti-of each treatment group
The μ L of thing solution 50 are answered to be diluted to 1 mL with PBS buffer solutions, 1500 g centrifuge 12 min, take supernatant in 96 orifice plates
In, its absorbance is surveyed at 540 nm with ELIASA, similarly, full haemolysis pair is used as by the use of distilled water diluting reactant mixture
According to calculating hemolysis rate（As a result Fig. 2 is seen）.
Application Example 4
The red cell suspensions of 0.1 mL 20% pre-process 20 min through the synthesis polypeptide that 0.1 mL concentration is 10 μ g/mL
Afterwards, final concentration of 100 mM of 0.2 mL AAPH solution is added, microseism, lucifuge are incubated 2 h, take the anti-of each treatment group
The μ L of thing solution 50 are answered to be diluted to 1 mL with PBS buffer solutions, 1500 g centrifuge 12 min, take supernatant in 96 orifice plates
In, its absorbance is surveyed at 540 nm with ELIASA, similarly, full haemolysis pair is used as by the use of distilled water diluting reactant mixture
According to calculating hemolysis rate（As a result Fig. 2 is seen）.
Application Example 5
The red cell suspensions of 0.1 mL 20% pre-process 20 min through the synthesis polypeptide that 0.1 mL concentration is 100 μ g/mL
Afterwards, final concentration of 100 mM of 0.2 mL AAPH solution is added, microseism, lucifuge are incubated 2 h, take the anti-of each treatment group
The μ L of thing solution 50 are answered to be diluted to 1 mL with PBS buffer solutions, 1500 g centrifuge 12 min, take supernatant in 96 orifice plates
In, its absorbance is surveyed at 540 nm with ELIASA, similarly, full haemolysis pair is used as by the use of distilled water diluting reactant mixture
According to calculating hemolysis rate.（As a result Fig. 2 is seen）Meanwhile each treatment group cell centrifuge is centrifuged into 12 min in 1500 g, collect thin
Born of the same parents are precipitated, and wash 3 centrifugations with PBS, abandoning supernatant, are resuspended again.During film-making, 10 μ L red blood cell re-suspension liquids are taken uniformly to be applied to
On clean mica sheet（It is required that cell is non-overlapping, does not reunite）, then cell is fixed with 2.5% glutaraldehyde, after 5 min, with super
Pure water rinsing silicon chip 3 times, natural air drying silicon chip, is finally placed on AFM, the scanning cell under tapping-mode
Pattern, with NanoScope software analysis experimental datas（As a result Fig. 3 is seen）.
Application Example 6
The red cell suspensions of 0.1 mL 20% are 0 μ g/mL through 0.1 mL concentration（Substituted with PBS, as normal control
Group）Synthesis polypeptide pre-process 20 min after, add 0.2 mL final concentration of 0 mM AAPH solution（Taken with PBS
Generation, as normal control）, microseism, lucifuge are incubated 2 h, take the μ L PBS buffer solutions of reactant solution 50 of each treatment group
1 mL is diluted to, 1500 g centrifuge 12 min, take supernatant in 96 orifice plates, it is surveyed at 540 nm with ELIASA
Absorbance, similarly, compareed by the use of distilled water diluting reactant mixture as full haemolysis, calculate hemolysis rate.（As a result Fig. 2 is seen）Together
When, each treatment group cell centrifuge is centrifuged into 12 min in 1500 g, collects cell precipitation, 3 centrifugations is washed with PBS, discards
Supernatant, it is resuspended again.During film-making, 10 μ L red blood cells re-suspension liquids are taken uniformly to be applied on the mica sheet of cleaning（It is required that cell is without weight
Fold, do not reunite）, then cell is fixed with 2.5% glutaraldehyde, after 5 min, with ultrapure water silicon chip 3 times, natural air drying silicon
Piece, finally it is placed on AFM, the scanning cell morphology under tapping-mode, it is real with NanoScope software analysis
Test data（As a result Fig. 3 is seen）.
Application Example 7
Table 3
| AAPH | Synthesis polypeptide+AAPH | |
| T-SOD activity (mgprot/mL) | 2.5976 | 5.2740 |
The red cell suspensions of 0.1 mL 20% are 5 μ g/mL through 0.1 mL concentration（Substituted with PBS, as normal control
Group）Synthesis polypeptide pre-process 20 min after, add 0.2 mL final concentration of 0 mM AAPH solution（Taken with PBS
Generation, as normal control）, microseism, lucifuge 2 h of incubation, each treatment group cell centrifuge is centrifuged into 12 min in 1500 g,
Cell precipitation is collected, 3 centrifugations is washed with PBS, adds 4oThe ultra-pure water of C precoolings, 150r/min concussion 10min, 10000g centrifugations
30min, collection supernatant is standby, according to kit（Nanjing is built up）Specification be measured SOD therein activity（As a result see
Table 3）.
Claims (6)
- A kind of 1. decapeptide, it is characterized in that the amino acid sequence of the decapeptide is Val-Thr-Ala-Pro-Ala-Ala-Ser-Val- Ala-Leu。
- 2. a kind of decapeptide described in claim 1 is being prepared for suppressing erythrocyte hemolysis, promoting human skin fibroblasts to increase Grow or improve the purposes of medicine caused by collagen.
- 3. purposes according to claim 2, it is characterised in that mix the decapeptide with red blood cell, in AAPH effect Under, after being incubated 2 h so that cell haemolysis inhibiting rate is 57.74% ~ 80.66%, and its pattern is more smooth than simple AAPH treatment groups, has Sequence；The concentration of the decapeptide is 1-100 μ g/mL.
- 4. purposes according to claim 3, it is characterised in that the decapeptide can make cell haemolysis inhibiting rate be up to 80.66 ± 1.09%。
- 5. purposes according to claim 3, it is characterised in that the decapeptide can make cell SOD activity by 2.5976 Mgprot/mL rises to 5.2740 mgprot/mL；Ten peptide concentration is 100 μ g/mL.
- 6. purposes according to claim 3, it is characterised in that in the presence of UVB, by the decapeptide and application on human skin into fibre Mixing with cells is tieed up, after being incubated 72 h so that cell survival rate improves 7.8-22.74%, meanwhile, collagen yield improves 4.69-17.96%, the concentration of the decapeptide is 1-10 μ g/mL.
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| 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 |
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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 |