CN113480626A - Antioxidant polypeptide with high skin permeability and application thereof - Google Patents

Antioxidant polypeptide with high skin permeability and application thereof Download PDF

Info

Publication number
CN113480626A
CN113480626A CN202110938735.9A CN202110938735A CN113480626A CN 113480626 A CN113480626 A CN 113480626A CN 202110938735 A CN202110938735 A CN 202110938735A CN 113480626 A CN113480626 A CN 113480626A
Authority
CN
China
Prior art keywords
antioxidant
polypeptide
component
skin permeability
high skin
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
Application number
CN202110938735.9A
Other languages
Chinese (zh)
Other versions
CN113480626B (en
Inventor
夏庆友
孙悦婷
林忠英
赵萍
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Chongqing Century Legend Technology Development Partnership LP
Original Assignee
Southwest University
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by Southwest University filed Critical Southwest University
Priority to CN202110938735.9A priority Critical patent/CN113480626B/en
Publication of CN113480626A publication Critical patent/CN113480626A/en
Application granted granted Critical
Publication of CN113480626B publication Critical patent/CN113480626B/en
Active legal-status Critical Current
Anticipated expiration legal-status Critical

Links

Images

Classifications

    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
    • C07K14/43563—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from insects
    • C07K14/43586—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from insects from silkworms
    • 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
    • A61Q19/08—Anti-ageing preparations
    • 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
    • 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
    • C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
    • A61K2800/40—Chemical, physico-chemical or functional or structural properties of particular ingredients
    • A61K2800/52—Stabilizers
    • A61K2800/522—Antioxidants; Radical scavengers

Abstract

The invention discloses an antioxidant polypeptide with high skin permeability and application thereof, wherein the antioxidant polypeptide contains a polypeptide with an amino acid sequence shown as SEQ ID No. 1-6, and the antioxidant polypeptide is separated by using a 5kDa ultrafiltration membrane, so that the obtained antioxidant polypeptide has a higher permeation rate, can better permeate the skin, has more worried antioxidant capacity and a cell proliferation promoting effect, and has the potential of being used as a cosmetic raw material.

Description

Antioxidant polypeptide with high skin permeability and application thereof
Technical Field
The invention relates to the field of polypeptides, in particular to an antioxidant polypeptide with high skin permeability, and also relates to an application of the sericin polypeptide.
Background
The skin is a tissue with high metabolic activity, has a plurality of defense mechanisms, provides physical and biochemical protection for the organism and plays a key role in maintaining the steady state of the organism. With aging, human skin resists oxidationThe capacity of the chemodefense system is diminished, coupled with the deterioration of exogenous environmental factors, the production of large amounts of Reactive Oxygen Species (ROS), leading to oxidative damage to proteins, nucleic acids and lipids, disrupting important cellular physiological processes and inducing mutagenesis. The imbalance between ROS and antioxidant defense system makes the skin susceptible to oxidative stress, resulting in skin problems including pathological effects of skin inflammation, erythema, wrinkles, acne, melanin, etc[109]. The antioxidant can protect the skin from oxidative damage of ROS, a series of traditional antioxidants such as vitamin C, vitamin E, nicotinamide and arbutin which are added as cosmetic antioxidants have remarkable ROS removing capacity, but still have the problems of irritation, weak stability, skin permeability and the like.
Sericin has many effects such as moisture retention, whitening, oxidation resistance, and anti-inflammation, and thus has been regarded as important in the field of cosmetics. However, sericin has a large molecular weight and is not easily penetrated through the skin, so that the application of antioxidant value thereof is limited. Therefore, there is an urgent need to prepare sericin peptide with good permeability, and improve the application of sericin in the field of cosmetics.
Disclosure of Invention
In view of the above, an object of the present invention is to provide an antioxidant polypeptide with high skin permeability; the second purpose of the invention is to provide the application of the antioxidant polypeptide with high skin permeability in preparing antioxidants.
In order to achieve the purpose, the invention provides the following technical scheme:
1. an antioxidant polypeptide with high skin permeability, wherein the antioxidant polypeptide contains a polypeptide with an amino acid sequence shown as SEQ ID No. 1-6.
Preferably, the antioxidant polypeptide has a molecular weight of less than 5kda.
2. The antioxidant polypeptide with high skin permeability is applied to preparing antioxidants.
Preferably, the antioxidant polypeptide with high skin permeability is used as an antioxidant in preparation of protection H2O2Conversion to oxidative damageApplication in cosmetic raw materials.
Preferably, the antioxidant polypeptide with high skin permeability is used as an antioxidant in the preparation of a cosmetic raw material for reducing the accumulation of intracellular ROS.
Preferably, the antioxidant polypeptide having high skin permeability is used as an antioxidant in the preparation of a cosmetic raw material for increasing the level of intracellular antioxidant enzymes.
The invention has the beneficial effects that: the invention discloses an antioxidant polypeptide with high skin permeability, wherein an amino acid sequence of a sericin polypeptide composition is shown as a sequence in SEQ ID No. 1-6, and the polypeptide composition is separated by using a 5kDa ultrafiltration membrane, so that the obtained sericin polypeptide composition has higher permeation rate, can better permeate the skin, has more worried antioxidant capacity and cell proliferation promoting effect, and has potential as a cosmetic raw material.
Drawings
In order to make the object, technical scheme and beneficial effect of the invention more clear, the invention provides the following drawings for explanation:
FIG. 1 is a schematic diagram of the ultrafiltration composition.
FIG. 2 shows the content distribution of each component.
Fig. 3 is a graph showing the cumulative permeation of each component.
FIG. 4 is an in vitro analysis of the antioxidant capacity of each component (A: FRAP Total antioxidant capacity; B: OH scavenging capacity; C: ABTS +. scavenging capacity; D: DPPH scavenging capacity).
FIG. 5 shows the stability effect of temperature on S-3 component and VC (A: S-3 component; B: VC).
FIG. 6 shows the stability effect of pH on S-3 component (A) and VC (B) (A: S-3 component; B: VC).
FIG. 7 is a graph of the stability effect of light on S-3 component and VC.
FIG. 8 is a graph showing the toxicity assay of various concentrations of protein components on cells.
FIG. 9 is H2O2Effect on survival of HaCaT cells.
FIG. 10 shows the pairs of components H2O2Survival of oxidatively damaged HaCaT cells.
FIG. 11 shows the pairs of components H2O2Cellular morphological effects of oxidatively damaged HaCaT cells.
FIG. 12 shows the pairs of components H2O2ROS effects of oxidatively damaged HaCaT cells.
FIG. 13 shows the pairs of components H2O2ROS effects of oxidatively damaged HaCaT cells.
Detailed Description
The present invention is further described with reference to the following drawings and specific examples so that those skilled in the art can better understand the present invention and can practice the present invention, but the examples are not intended to limit the present invention.
Example 1 isolation of sericin antioxidant peptide
In order to obtain antioxidant peptides, sericin peptides with molecular weight of more than 30kDa, molecular weight of between 5kDa and 30kDa, and molecular weight of less than 5kDa after degrading silkworm cocoon through 0.2 μm filter membrane are respectively named as S-1, S-2 and S-3 components (FIG. 1). Meanwhile, high-pressure water-extracted sericin SS was set as a control group.
Freeze drying the separated components, and calculating to obtain the ratio of the content of each component in the total mass as shown in figure 2, wherein the S-1 component accounts for 35% of the total mass, the S-2 component accounts for 13% of the total mass, and the S-3 component accounts for 52% at most, which indicates that the molecular weight of most components in the silkworm cocoon is small (figure 2).
Example 2 determination of the amount of accumulated permeation of an Artificial Membrane
Skin permeation test was performed using an artificial membrane provided by Guangdong Boxi Biotechnology Ltd, and 7.0mL of a receiving solution (pH 7.2 to 7.4 in phosphate buffer) was added to a receiving chamber of a Franz diffusion cell, and the artificial membrane was fixed between a supply chamber and the receiving chamber with the smooth surface facing the supply chamber and the rough surface facing the receiving chamber; injecting 1mL of receiving solution into a receiving chamber through a sampling tube by using a sampler, exhausting air to ensure that the artificial membrane is tightly contacted with the receiving solution, and recording the actual volume; the effective permeation area S of 500. mu.L of the sample applied to the artificial membrane in the supply chamber was about 1.77cm2The sample is prepared by adopting a disposable gun headThe products are uniformly coated from the center of the film to the edge in a radial manner, and 3 samples are arranged in parallel; starting an electromagnetic stirrer to stir at the speed of 300rpm, keeping a constant-temperature water bath at (32 +/-1) DEG C, and ensuring that a water bath interlayer has no bubbles; sampling solutions at the time points of 2h, 4h, 8h and 24h are respectively taken, 2mL of receiving solution is extracted through a sampling tube by using a disposable syringe, then the receiving solution is placed in a 2mL centrifuge tube, and in addition, the same amount of receiving solution (phosphate buffer solution) is supplemented after each sampling. After 24h of permeation is finished, the content of the sample to be detected contained on the artificial membrane and under the artificial membrane at each time point of different experimental groups is detected, and the accumulated permeation quantity Q is calculated according to the following formula:
Q＝Cn×V+∑Ci×V0(i＝1…n-1)
note: q: accumulating the permeation amount; v: a receiving liquid volume in the receiving chamber; v0: the volume of each sample; ci: the concentration of the drug in the receiving solution from the 1 st to the last sampling; cn: the sample concentration measured at the nth sampling point is simulated in vitro by using an artificial membrane on the basis of the Franz diffusion cell principle to simulate the permeation condition of each component on human skin. As shown in fig. 3, the amount of each component permeating the artificial membrane is increased with the decrease of the molecular weight through statistics of the cumulative permeation amount at each time point, and the permeation amount of each low molecular weight component is significantly more than that of SS, indicating that substances with smaller molecular weight are easier to permeate through the skin; and the accumulated permeation quantity of the component S-3 is obviously more than that of other components, and the slope of the permeation quantity curve is also larger, so that the permeation rate of the component S-3 is higher, and further the S-3 component can better permeate the skin and has the potential of being used as a cosmetic raw material.
The amino acid sequence of the S-3 component detected by mass spectrometry was as follows: TDGVRSGNFAGF (SEQ ID NO. 1); SASSSKNDNVFVY (SEQ ID NO. 2); FPNGVVASLDNQF (SEQ ID NO. 3); LNSETSNVSQTSK (SEQ ID NO. 4); SVIAGALEYHGVPAY (SEQ ID NO. 5); EADCDPNCRR (SEQ ID NO. 6).
Example 3 antioxidant and stability of sericin antioxidant peptide
1) Oxidation resistance
The results of testing 4 kinds of in vitro antioxidant abilities, such as total antioxidant ability, hydroxyl radical (. OH) clearance, ABTS radical (ABTS +. cndot.) clearance, and DPPH radical (DPPH. cndot.) clearance of S-1, S-2, and S-3 components, and further analyzing the antioxidant activity of each component are shown in FIG. 4. The results show that the components S-1, S-2, S-3 and the control SS were formulated at concentrations of 0.1%, 0.5%, 1%, 2%, and 3% (w/v), respectively, and then the in vitro antioxidant capacity was determined separately. Wherein, A in figure 4 shows the measurement result of the total antioxidant capacity of FRAP, as shown in the figure, the total antioxidant capacity is increased along with the increase of the component concentration, and the total antioxidant capacity of the three components at the concentration of 3 percent is not greatly different and is obviously higher than that of SS. B in fig. 4 shows the measurement results of the OH clearance, which increases with increasing concentration for the three components, with the mean OH clearance for S-3 reaching 87.6633%, which is significantly higher than for S-1(mean 73.5188%) and S-2(mean 72.2156%). The ability of SS to scavenge OH is rather reduced with increasing concentration. FIG. 4C and FIG. 4D show the measurement results of ABTS +. clearance and DPPH.clearance, respectively, and the ABTS +. clearance and DPPH.clearance increase with the concentration of each component, and the ABTS +. clearance and DPPH.clearance of the three components are not much different but are all obviously higher than SS.
Through the determination of 4 kinds of in vitro antioxidant capacity, the results show that the in vitro antioxidant activity of the sericin extracted by high-pressure water is obviously lower than that of each component, which indicates that the antioxidant activity of the obtained polypeptide is increased; and the component S-3 with relatively small molecular weight has better in-vitro antioxidant capacity compared with other components, which shows that the antioxidant capacity of the sericin polypeptide is improved along with the increase of the hydrolysis degree.
2) Stability of
The S-3 component has high permeability of an artificial membrane, high ratio in mixed polypeptide and excellent antioxidant activity, so that the S-3 component has potential of being produced as a cosmetic antioxidant. However, biologically active peptides are susceptible to deamidation, oxidation, hydrolysis, racemization, denaturation, and the like. Resulting in instability of the polypeptide and a reduction in the associated biological activity. Therefore, the part researches the stability of the sericin antioxidant peptide S-3 component by detecting the influence of temperature, pH and illumination on the stability of the S-3 component and researching the influence of the S-3 component on the stability of a cosmetic system.
(1) Effect of temperature on the stability of the S-3 component
The S-3 component and the control VC solution are respectively treated for 2h, 4h and 6h at 4 ℃, 25 ℃, 40 ℃, 50 ℃ and 60 ℃, and the measured ABTS +. scavenging activity retention rates are shown in figure 5, wherein A in figure 5 represents the influence of temperature on the ABTS +. scavenging activity retention rate of the S-3 component, and B in figure 5 represents the influence of temperature on the VC ABTS +. scavenging activity retention rate. At different temperatures, the ABTS +. scavenging activity of VC gradually decreases with time, and the ABTS +. scavenging activity of S-3 component is relatively more stable. And with increasing temperature, the ABTS +. scavenging activity of VC gradually decreases, while the ABTS +. scavenging activity of S-3 component gradually increases, presumably temperature increase may facilitate exposure of amino acid side chain groups of polypeptide scavenging free radicals. From the above results, it can be seen that the influence of temperature on the S-3 component is smaller than that of VC, indicating that the S-3 component has a certain stability at different temperatures.
(2) Effect of pH on the stability of the S-3 component
The retention rates of ABTS +. scavenging activity of S-3 component and VC under different pH conditions are shown in FIG. 6, wherein A in FIG. 6 represents the influence of pH on the retention rate of ABTS +. scavenging activity of S-3 component, and B in FIG. 6 represents the influence of pH on the retention rate of ABTS +. scavenging activity of VC. Under the conditions of strong acid and strong alkali, the ABTS +. scavenging activity of the S-3 component is not greatly different; whereas the ABTS +. scavenging activity of VC decreased gradually with increasing pH, indicating that pH had less effect on the stability of the S-3 component.
(3) Effect of light illumination on the stability of the S-3 component
After the S-3 component and VC are subjected to light treatment for 24h and 48h, the measured ABTS +. scavenging activity retention rate is shown in figure 7, and the ABTS +. scavenging activity of the S-3 component and VC has no obvious change basically within 24 h; after 48h, VC began to decrease in oxidation resistance, while the S-3 component still maintained a more stable oxidation resistance, indicating that the stability of the S-3 component was not substantially affected over the exposure time range (24h-48h) of the cosmetic in use.
3) Cytotoxicity test
To test the skin irritation of each component, the density was 2X 10 at the logarithmic cell growth phase 5100 μ L/mL of HaCaT cells were added to each well of a 96-well plate and cultured in a cell incubator for 12h to ensure a relatively stable state after cell attachment. Preparing 2% of each component into a test group with 8 concentration gradients in a 2-fold dilution mode, taking a complete culture medium as a cell control group, loading 100 mu L of sample on each hole, after culturing for 24h, washing the cells once by using fresh PBS, adding a serum-free culture medium containing 10% of CCK-8, placing the cells in a cell culture box for incubation for half an hour, measuring OD450 by using a microplate reader, and calculating the cell survival rate according to the following formula:
cell survival (%) ([ a (dosed) -a (blank) ]/[ a (0 dosed) -a (blank) ] × 100
A (dosing): absorbance values of cells, drug and CCK-8;
a (blank): absorbance of cells-free, medium-containing and CCK-8;
a (0 dosing): no drug, cells, medium and absorbance of CCK-8.
The detection results are shown in fig. 8. The results show that the three components have certain inhibition effect on the growth of cells along with the increase of the concentration, and the toxicity of each component on HaCaT cells is as follows: s-1 is greater than S-2 is greater than S-3, the component S-3 can inhibit the growth of HaCaT cells at a higher concentration, and the component S-3 also has the effect of promoting cell proliferation at a low concentration (0.125% -0.0156%).
IC50Is the semi-inhibitory concentration of the drug, i.e., the concentration at which 50% of the cell death rate, IC, occurs50Higher indicates lower toxicity of the drug. Substituting the data of fig. 8 into GraphPad Prism 7.04, inhibition rates of the three components at each concentration can be calculated. Based on the results, the survival rate of the selected cells was 90% (IC)10) Subsequent experiments were performed at corresponding concentrations, where IC of S-110Is 0.01%, IC of S-210Is 0.13%, IC of S-310Is 0.42%.
To further investigate the components at the cellular levelAntioxidant activity, selected from H2O2HaCaT cells are processed to establish a skin cell oxidative damage model, and the cell model is further used to detect the antioxidant damage effect of each component on cells, and the result is shown in figure 9. The results show that 200-2O2Cell viability following H12H after HaCaT cells treatment2O2The concentration is increased and decreased when H2O2At a concentration of 600. mu.M, cell survival rate was significantly reduced compared to the control group, and H was present at this concentration2O2The damage to cells is moderate, therefore, 600. mu.M H is selected2O2To establish a model of cellular oxidative damage.
Pretreatment of each component of sericin antioxidant peptide on H2O2Survival effects of oxidatively damaged HaCaT cells: different components are added into cells in advance for co-culture, then oxidative damage is carried out, and the antioxidant activity of each component is further reflected by the determination of the survival rate. The results are shown in FIG. 10, and H2O2Compared with the damaged group, the survival rate of HaCaT cells can be obviously improved by different components and SS, and H is shown2O2Protection of oxidatively damaged HaCaT cells; in addition, it was found that the protective effect of the S-3 fraction on cells compared with other fractions is more effective in promoting cells in an oxidative damage state to a normal cell state by treating the fractions with different fractions than the normal cell fraction. And further observing the number and morphology of cells by microscope (FIG. 11), wherein H2O2The number of cells in the damaged group is obviously reduced and the tentacles of the cells are retracted; the number and morphology of cells in the SS and S-1 component treatment groups also changed significantly; the number of cells in the S-2 and S-3 component treated groups was relatively greater, and the cells in the S-3 component treated group were very similar in number and morphology to those in the normal cell group, indicating that the S-3 component was effective in protecting HaCaT cells from oxidative damage.
Pretreatment of each component of the sericin antioxidant peptide reduces the accumulation of intracellular ROS: h2O2Can generate ROS in cells to damage cells, in part by the reactive oxygen species level in cellsAnd (4) measuring to further reflect the antioxidant activity of each component. After pretreatment of cells with fractions and SS for 12H, H was added2O2Oxidative damage was performed, followed by loading of cells with DCFH-DA fluorescent probe. The results of measuring the ROS level are shown in FIG. 12. The results show that2O2Compared with the damaged group, the S-3 component remarkably reduces the accumulation of intracellular ROS compared with other components, and the result shows that the component S-3 can reduce the accumulation of reactive oxygen species in HaCaT cells, so that the skin can be protected from oxidative damage.
The influence of pretreatment of each component of the sericin antioxidant peptide on MDA, SOD and CAT: ROS can cause cellular lipid oxidation, and its product Malondialdehyde (MDA) is highly damaging to the skin. The antioxidant activity of each component was compared by detecting the level of MDA in HaCaT cells. FIG. 13, A reflects the oxidation of cellular lipids in each treatment group, where H2O2MDA levels in the injured group were much higher than in the normal cell group; each component treatment group and H2O2Compared with the damaged group, the MDA content is obviously reduced, which shows that each component can effectively inhibit lipid oxidation in cells, and the inhibition effect of the S-1 and S-3 components is more obvious.
The skin itself presents a series of antioxidant enzymes to protect against oxidative damage. This section compares the antioxidant activity of each component by detecting the levels of superoxide dismutase (SOD) and Catalase (CAT) in HaCaT cells. In FIG. 13, B and C show the levels of SOD and CAT, respectively, and the S-3 fraction significantly increased the level of intracellular antioxidant enzymes to reduce H compared to the other fractions under oxidative stress conditions2O2The resulting oxidative damage.
The above-mentioned embodiments are merely preferred embodiments for fully illustrating the present invention, and the scope of the present invention is not limited thereto. The equivalent substitution or change made by the technical personnel in the technical field on the basis of the invention is all within the protection scope of the invention. The protection scope of the invention is subject to the claims.
Sequence listing
<110> university of southwest
<120> antioxidant polypeptide with high skin permeability and application thereof
<160> 6
<170> SIPOSequenceListing 1.0
<210> 1
<211> 12
<212> PRT
<213> silkworm (Bombyx mori)
<400> 1
Thr Asp Gly Val Arg Ser Gly Asn Phe Ala Gly Phe
1 5 10
<210> 2
<211> 13
<212> PRT
<213> silkworm (Bombyx mori)
<400> 2
Ser Ala Ser Ser Ser Lys Asn Asp Asn Val Phe Val Tyr
1 5 10
<210> 3
<211> 13
<212> PRT
<213> silkworm (Bombyx mori)
<400> 3
Phe Pro Asn Gly Val Val Ala Ser Leu Asp Asn Gln Phe
1 5 10
<210> 4
<211> 13
<212> PRT
<213> silkworm (Bombyx mori)
<400> 4
Leu Asn Ser Glu Thr Ser Asn Val Ser Gln Thr Ser Lys
1 5 10
<210> 5
<211> 15
<212> PRT
<213> silkworm (Bombyx mori)
<400> 5
Ser Val Ile Ala Gly Ala Leu Glu Tyr His Gly Val Pro Ala Tyr
1 5 10 15
<210> 6
<211> 10
<212> PRT
<213> silkworm (Bombyx mori)
<400> 6
Glu Ala Asp Cys Asp Pro Asn Cys Arg Arg
1 5 10

Claims (6)

1. An antioxidant polypeptide with high skin permeability, which is characterized in that: the antioxidant polypeptide contains polypeptide with an amino acid sequence shown as SEQ ID NO. 1-6.
2. The antioxidant polypeptide with high skin permeability as claimed in claim 1, wherein: the molecular weight of the antioxidant polypeptide is less than 5kDa.
3. Use of the antioxidant polypeptide having high skin permeability according to claim 1 or 2 for the preparation of an antioxidant.
4. Use according to claim 1, characterized in that: the antioxidant polypeptide with high skin permeability is used as antioxidant in preparation of protective H2O2Application in cosmetic raw materials for oxidative damage is provided.
5. Use according to claim 1, characterized in that: the use of said antioxidant polypeptide with high skin permeability as an antioxidant for the preparation of a cosmetic raw material reducing the accumulation of intracellular ROS.
6. Use according to claim 1, characterized in that: the antioxidant polypeptide with high skin permeability is used as an antioxidant in the preparation of cosmetic raw materials for increasing the level of intracellular antioxidant enzymes.
CN202110938735.9A 2021-08-16 2021-08-16 Antioxidant polypeptide with skin permeability and application thereof Active CN113480626B (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
CN202110938735.9A CN113480626B (en) 2021-08-16 2021-08-16 Antioxidant polypeptide with skin permeability and application thereof

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
CN202110938735.9A CN113480626B (en) 2021-08-16 2021-08-16 Antioxidant polypeptide with skin permeability and application thereof

Publications (2)

Publication Number Publication Date
CN113480626A true CN113480626A (en) 2021-10-08
CN113480626B CN113480626B (en) 2022-06-24

Family

ID=77946556

Family Applications (1)

Application Number Title Priority Date Filing Date
CN202110938735.9A Active CN113480626B (en) 2021-08-16 2021-08-16 Antioxidant polypeptide with skin permeability and application thereof

Country Status (1)

Country Link
CN (1) CN113480626B (en)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN116444641A (en) * 2023-02-23 2023-07-18 西南大学 Extracellular matrix synthesis promoting polypeptide and application thereof

Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20110305765A1 (en) * 2008-11-21 2011-12-15 Board Of Regents, The University Of Texas System Preparation and methodology of silk fibroin nanoparticles
CN108578771A (en) * 2018-04-04 2018-09-28 西南大学 Preparation method and products thereof with the FGF1 sericin gels for promoting cell-proliferation activity
CN110719732A (en) * 2017-03-30 2020-01-21 犹他州立大学 Transgenic silkworm expressing spider silk
WO2020247594A1 (en) * 2019-06-04 2020-12-10 Cocoon Biotech Inc. Silk-based products, formulations, and methods of use

Patent Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20110305765A1 (en) * 2008-11-21 2011-12-15 Board Of Regents, The University Of Texas System Preparation and methodology of silk fibroin nanoparticles
CN110719732A (en) * 2017-03-30 2020-01-21 犹他州立大学 Transgenic silkworm expressing spider silk
CN108578771A (en) * 2018-04-04 2018-09-28 西南大学 Preparation method and products thereof with the FGF1 sericin gels for promoting cell-proliferation activity
WO2020247594A1 (en) * 2019-06-04 2020-12-10 Cocoon Biotech Inc. Silk-based products, formulations, and methods of use

Non-Patent Citations (8)

* Cited by examiner, † Cited by third party
Title
CHENG F Y等: "The in vitro antioxidant properties of alcalase hydrolysate prepared from silkie fowl (Gallus gallus) blood protein", 《ANIMAL SCIENCE JOURNAL》 *
KIM等: "Intronic sequences of the silkworm strains of Bombyx mori (Lepidoptera: Bombycidae): High variability and potential for strain identification", 《 EUROPEAN JOURNAL OF ENTOMOLOGY》 *
LI LI等: "Different Types of Peptide Detected by Mass Spectrometry among Fresh Silk and Spectrometry among Fresh Silk and Distinguishing Modern Contamination", 《PLOS ONE》 *
NCBI: "Sequence 92 from patent US 8288347", 《GENBANK DATABASE》 *
李力: "贾湖遗址墓葬土壤中蚕丝蛋白残留物的鉴定与分析", 《中国优秀博硕士学位论文全文数据库(博士) 工程科技Ⅰ辑》 *
范金波等: "丝胶肽体外抗氧化活性的研究", 《食品与发酵科技》 *
范金波等: "丝胶蛋白抗氧化肽的酶法制备及功能评价", 《农业工程学报》 *
韩冬等: "家蚕拟抗微生物肽Gloverins基因(Bmglv)的原核表达及抗菌活性鉴定", 《昆虫学报》 *

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN116444641A (en) * 2023-02-23 2023-07-18 西南大学 Extracellular matrix synthesis promoting polypeptide and application thereof
CN116444641B (en) * 2023-02-23 2024-04-02 西南大学 Extracellular matrix synthesis promoting polypeptide and application thereof

Also Published As

Publication number Publication date
CN113480626B (en) 2022-06-24

Similar Documents

Publication Publication Date Title
CN108753708B (en) A kind of preparation method of Stem Cell Activity factor freeze-dried powder
CN113842334B (en) Composition for promoting skin multi-dimensional defense and repair and preparation method thereof
CN113480626B (en) Antioxidant polypeptide with skin permeability and application thereof
CN110590913A (en) Antioxidant damage skin protection active polypeptide AOP-P1 and preparation method and application thereof
CN110151679A (en) A kind of excretion body freeze-dried powder and the preparation method and application thereof
CN105218639B (en) A kind of heptapeptide and its application
CN113318003A (en) Jellyfish polypeptide and application thereof
KR20210153302A (en) Cosmetic composition for anti-wrinkle and whitening
CN113750216B (en) Anti-aging cosmetic or medicine
CN113876928B (en) Preparation of fibroblast outer vesicle and application of fibroblast outer vesicle in beauty treatment and medicines
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
KR101608687B1 (en) Cosmetic composition containing cyclic lipopeptide for antioxidant and antiaging
CN109793703A (en) A kind of preparation method of skin anti-aging cell-secretion factor cosmetics
CN111732634B (en) Application of earthworm active peptide for inhibiting melanocyte proliferation in preparation of medicines or cosmetics
CN110812469B (en) Application of polypeptide AR12 in preparation of antioxidant
CN113599297A (en) Cosmetic containing polypeptide composition with good stability, and preparation method and application thereof
CN115894625A (en) Polypeptide with anti-aging effect and application thereof
CN113520900B (en) Hypoallergenic and anti-aging yak collagen composition and application thereof
CN114989248A (en) Clinacanthus nutans polypeptide with anti-inflammatory and antioxidant activities as well as preparation method and application thereof
CN114644705A (en) Active polypeptide for preventing acute photodamage of skin and application thereof
KR101821738B1 (en) Anti-wrinkle and anti-skin sagging cosmetic composition containing extracts of hypsizigus marmoreus
CN111437292A (en) Bombyx Batryticatus water extract and application thereof
CN109692130B (en) Mask liquid containing defensins and preparation method thereof
He et al. Components and Antioxidant Activity of the Polysaccharide from Streptomyces virginia H03

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
TR01 Transfer of patent right

Effective date of registration: 20240415

Address after: 402160 No. 801 Heshun Avenue, Yongchuan District, Chongqing (1st Floor, Building 3, Zone C, Yongchuan District Big Data Industrial Park)

Patentee after: Chongqing century legend technology development partnership (L.P.)

Country or region after: China

Address before: 400715 No. 2, natural road, Beibei District, Chongqing

Patentee before: SOUTHWEST University

Country or region before: China