New use of polypeptides in preparing compositions for soothing skin

Abstract

The present invention provides a use of a polypeptide or a salt thereof in preparing a composition for soothing skin, wherein the soothing skin comprises one or more of inhibiting hyaluronidase activity, reducing the skin's neurological response to irritants, or enhancing skin tolerance. The sequence of the polypeptide of the present invention is Ac‑Phe‑Phe‑Trp‑Phe‑Lys‑Val‑NH2, which can inhibit the activity of hyaluronidase, maintain the content of hyaluronic acid in the body, thereby reducing the skin's neurological response to irritants, enhancing skin tolerance, improving skin sensitivity, having a good soothing effect, and can be applied to products for soothing skin.

Description

Technical Field

[0001] The present invention belongs to the technical field of active polypeptides, and in particular relates to a new use of polypeptides in preparing a composition for soothing skin. Background Art

[0002] The occurrence of skin irritation is a complex process involving the skin barrier, the skin nervous system, and the skin immune cells. Under the combined effects of internal and external factors such as excessive "exfoliation" and "skin resurfacing", the skin barrier function is damaged, causing an increase in sensory nerve afferent signals, resulting in increased skin reactivity to external stimuli, and then triggering skin immune responses. After the skin barrier function is damaged, some cytokines are often released at the damaged site. These cytokines will further promote the sensitization of local sensory cells and delay barrier repair, thus forming a vicious cycle and causing skin sensitivity to persist. According to surveys, people with sensitive skin account for 30%-40% of the total population. Products with soothing effects have become an important research direction for daily chemical products because they can effectively reduce the degree of skin irritation and improve skin sensitivity.

[0003] Studies have shown that inhibiting the activity of hyaluronidase is beneficial for soothing the skin. Hyaluronidase is a specific cleavage enzyme of hyaluronic acid, which is the most abundant and largest component in the extracellular matrix. It can maintain the volume of the extracellular matrix, regulate the secretion of cell growth factors and cytokines, and affect cell adhesion, growth, proliferation and differentiation. Therefore, hyaluronic acid plays an important role in maintaining skin moisture and elasticity, wound healing and angiogenesis. Under the influence of adverse factors such as ultraviolet radiation and exogenous stimulation, mast cells are activated and release histamine, which leads to increased hyaluronidase activity. The increase in hyaluronidase activity promotes the degradation of hyaluronic acid, causing allergic reactions in the skin.

[0004] Therefore, by inhibiting the activity of hyaluronidase, the skin's neurological response to irritants can be reduced, the skin's tolerance can be enhanced, the skin's sensitivity can be fundamentally improved, and sensitive skin problems can be solved, thereby meeting the growing demand for skin treatment or care. Summary of the invention

[0005] The inventors conducted experimental studies and found that a polypeptide can inhibit the activity of hyaluronidase and has the effect of soothing the skin, thereby completing the present invention.

[0006] Therefore, the present invention aims to provide a use of a polypeptide or a salt thereof in preparing a composition for soothing skin, wherein the soothing skin comprises one or more of inhibiting hyaluronidase activity, reducing the skin's neurological response to irritants, or enhancing skin tolerance.

[0007] The sequence of the polypeptide of the present invention is Ac-Phe-Phe-Trp-Phe-Lys-Val-NH2.

[0008] The polypeptides of the invention may exist as stereoisomers or mixtures of stereoisomers; for example, the amino acids comprising them may have the L-, D-configuration, or be racemic independently of one another. Thus, it is possible to obtain isomeric mixtures as well as racemic mixtures or diastereomeric mixtures, or pure diastereomers or enantiomers, depending on the number of asymmetric carbons and what isomers or isomeric mixtures are present. Preferred structures of the polypeptides of the invention are pure isomers, i.e., enantiomers or diastereomers.

[0009] For example, when -Lys- is described in the present invention, it should be understood that -Lys- is selected from -L-Lys-, -D-Lys- or a mixture of the two, and is racemic or non-racemic. The preparation methods described in this document enable a person skilled in the art to obtain each stereoisomer of the polypeptide of the present invention by selecting amino acids with the correct configuration.

[0010] The present invention also includes all suitable isotopic variants of the polypeptides. Isotopic variants of these polypeptides of the present invention are understood here to mean compounds in which at least one atom in the polypeptide of the present invention is replaced by another atom of the same atomic number, but the atomic mass of the other atom is different from the atomic mass usually or predominantly present in nature. Examples of isotopes that can be incorporated into the polypeptides of the present invention are those of hydrogen, carbon, nitrogen or oxygen, e.g. 2 H (deuterium), 3 H (tritium), 13 C. 14 C. 15 N. 17 O or 18 O. Certain isotopic variants of the polypeptides of the invention (particularly those into which one or more radioactive isotopes have been incorporated) may be useful, for example, for examining the mechanism of action or distribution of the active compound in vivo; due to the relative ease of preparation and detectability, particularly with 3 H or 14 Compounds labeled with C isotopes are suitable for this purpose. In addition, due to the stronger metabolic stability of the compound, the incorporation of isotopes (e.g., deuterium) can produce specific therapeutic benefits, such as an extension of the half-life in vivo or a reduction in the required active dose; therefore, in some cases, such modifications of the polypeptides of the present invention may also constitute a preferred embodiment of the present invention. Isotopic variants of the polypeptides of the present invention can be prepared by methods known to those skilled in the art, such as by the methods further described below and in the examples, by using the respective reagents and / or corresponding isotopic modifications of the starting materials.

[0011] In addition, the present invention also includes prodrugs of the polypeptides of the present invention. The term "prodrug" herein means such compounds: they themselves may be biologically active or inactive, but during their residence time in the body, they react (e.g., metabolize or hydrolyze) to generate the compounds of the present invention.

[0012] Optionally, the composition comprises a polypeptide or a salt thereof at a mass percentage concentration of 0.0001%-5%;

[0013] Optionally, the composition comprises a polypeptide or a salt thereof at a mass percentage concentration of 0.0005%-1%;

[0014] Optionally, the composition comprises a polypeptide or a salt thereof at a mass percentage concentration of 0.001%-0.1%;

[0015] Optionally, the composition comprises the polypeptide or its salt in a mass percentage concentration of 0.005%-0.01%.

[0016] The above-mentioned polypeptide can inhibit the activity of hyaluronidase and maintain the content of hyaluronic acid in the body, thereby reducing the skin's neurological response to irritants, enhancing skin tolerance, improving skin sensitivity, and has a good skin soothing effect, and can be used in soothing products.

[0017] Optionally, the salt of the polypeptide comprises a metal salt of the polypeptide, wherein the metal comprises: lithium, sodium, potassium, calcium, magnesium, manganese, copper, zinc or aluminum;

[0018] Optionally, the salt of the polypeptide includes a salt formed by the polypeptide and an organic base, and the organic base includes: ethylamine, diethylamine, ethylenediamine, ethanolamine, diethanolamine, arginine, lysine, histidine or piperazine;

[0019] Optionally, the salt of the polypeptide includes a salt formed by the polypeptide and an inorganic acid or an organic acid, and the organic acid includes: acetic acid, citric acid, lactic acid, malonic acid, maleic acid, tartaric acid, fumaric acid, benzoic acid, aspartic acid, glutamic acid, succinic acid, oleic acid, trifluoroacetic acid, oxalic acid, pamoic acid or gluconic acid;

[0020] Optionally, the inorganic acid includes hydrochloric acid, sulfuric acid, boric acid or carbonic acid.

[0021] The above-mentioned polypeptide or its salt of the present invention can be obtained according to conventional methods known in the prior art, such as solid phase synthesis, liquid phase synthesis or a combination of solid phase and liquid phase, and can also be prepared by biotechnology methods aimed at producing the desired sequence, or by controlled hydrolysis of proteins with animal, fungal or plant origin.

[0022] For example, a method for obtaining a polypeptide comprises the following steps:

[0023] - coupling an amino acid having a protected N-terminus and a free C-terminus with an amino acid having a free N-terminus and a C-terminus that is protected or bound to a solid support;

[0024] - Elimination of the group protecting the N-terminus;

[0025] - repeating this coupling sequence and eliminating the group protecting the N-terminus until the desired peptide sequence is obtained;

[0026] - Elimination of the group protecting the C-terminus or cleavage from the solid support.

[0027] Preferably, the C-terminus is bound to a solid support and the method is carried out on a solid phase, comprising coupling an amino acid having a protected N-terminus and a free C-terminus with an amino acid having a free N-terminus and a C-terminus bound to a polymer support; eliminating the group protecting the N-terminus; and repeating this sequence as many times as required in order to thereby obtain a polypeptide of the desired length, followed by cleavage of the synthesized polypeptide from the initial polymer support.

[0028] The functional groups of the amino acid side chains remain fully protected with temporary or permanent protecting groups throughout the synthesis and can be deprotected simultaneously or orthogonally to the process of cleavage of the peptide from the polymer support.

[0029] The method may include the additional steps of deprotecting the N-terminus and C-terminus and / or cleaving the peptide from the polymer support in an undefined order using standard conditions and methods known in the art, and then modifying the functional groups at the termini. The optional modification of the N-terminus and C-terminus may be performed on the polypeptide bound to the polymer support, or after the peptide has been cleaved from the polymer support.

[0030] The above polypeptide or its salt can be incorporated into a cosmetically or pharmaceutically acceptable delivery system or sustained-release system to achieve better penetration of the active ingredient and / or improve its pharmacokinetic and pharmacodynamic properties. The above polypeptide or its salt or the above composition can be applied to the skin and / or mucosa, or orally or parenterally administered as needed to treat and / or care for a condition, disorder and / or disease.

[0031] The frequency of administration or dosing can vary widely, depending on the needs of each subject, with suggested administration or dosing ranging from once a month to 10 times a day, preferably from once a week to 4 times a day, more preferably from 3 times a week to 3 times a day, and even more preferably once or twice a day.

[0032] The term "delivery system" refers to a diluent, adjuvant, excipient or carrier used together with the compound of the present invention, which is selected from: water, oil or surfactant, including those of petroleum origin, animal origin, plant origin, or synthetic origin, such as and not limited to peanut oil, soybean oil, mineral oil, sesame oil, castor oil, polysorbate, sorbitan esters, ether sulfates, sulfates, betaines, glucosides, maltosides, fatty alcohols, nonoxynol ethers, poloxamers, polyoxyethylene, polyethylene glycol, dextrose, glycerol, digitonin and the like. Those of ordinary skill in the art are known to diluents that can be used in different delivery systems in which the compound of the present invention can be administered.

[0033] The term "sustained release" is used in its conventional sense to refer to a delivery system that provides for gradual release of a compound over a period of time, and preferably, but not necessarily, with a relatively constant level of compound released over the entire period of time.

[0034] Examples of delivery systems or sustained release systems are liposomes, oleosomes, nonionic surfactant liposome vesicles, ethosomes, millicapsules, microcapsules, nanocapsules, nanostructured lipid carriers, sponges, cyclodextrins, lipid vesicles, micelles, millispheres, microspheres, nanospheres, lipid spheres, microemulsions, nanoemulsions, milliparticles, microparticles or nanoparticles. Preferred delivery systems or sustained release systems are liposomes and microemulsions, more preferably water-in-oil microemulsions with an internal structure of reverse micelles.

[0035] Sustained release system can be prepared by methods known in the prior art, and can be given, for example, in the following manner: by topical or transdermal administration, including adhesive patch, non-adhesive patch, closure patch and microelectronic patch; or by systemic administration, for example and not limited to, oral or parenteral route, including nose, rectum, subcutaneous implantation or injection or directly implanted or injected into a specific body part, and preferably these compounds of the present invention of a relatively constant amount should be released. The amount of the compound included in the sustained release system will depend on the release kinetics and duration of the position, compound of the present invention, and the condition to be treated and / or the property of care, illness and / or disease, at which the composition will be given, for example.

[0036] The above polypeptide or its salt may also be adsorbed on a solid organic polymer or a solid inorganic support, such as but not limited to talc, bentonite, silicon dioxide, starch, or maltodextrin.

[0037] Optionally, the composition is a cosmetic composition or a pharmaceutical composition.

[0038] The composition is formulated to be selected from the group consisting of cream, oil, balm, foam, lotion, gel, liniment, slurry, ointment, mousse, powder, stick, pen, spray, aerosol, capsule, tablet, granule, solution, suspension, emulsion, elixir, polysaccharide film, jelly or gelatin.

[0039] Optionally, the composition further comprises at least one other active agent for enhancing the soothing effect, wherein the other active agent is selected from peptides, natural plant ingredients, urea capsules or dipotassium glycyrrhizinate.

[0040] In order to facilitate the understanding of the present invention, the meanings of some terms and expressions used in the present invention are explained as follows:

[0041] In the present invention, the term "skin" is understood to mean the multiple layers that make it up, from the uppermost layer or stratum corneum to the lowermost layer or subcutaneous tissue, both ends are included. These layers are composed of different types of cells, such as keratinocytes, fibroblasts, melanocytes, and / or adipocytes, etc. In the present invention, the term "skin" includes the scalp.

[0042] The amino acid abbreviations used in the present invention follow the rules specified by the IUPAC-IUB Biochemical Nomenclature Commission in the European Journal of Biochemistry (Eur. J. Biochem. 1984, 138: 9-37).

[0043] For example, Lys represents NH2-CH(CH2CH2CH2CH2NH2)-COOH, Lys- represents NH2-CH(CH2CH2CH2CH2NH2)-CO-, -Lys represents -NH-CH(CH2CH2CH2CH2NH2)-COOH, and -Lys- represents -NH-CH(CH2CH2CH2CH2NH2)-CO-. Thus, the hyphen representing a peptide bond eliminates the OH in the 1-carboxyl group of an amino acid (represented here in conventional non-ionized form) when located on the right side of the symbol, and eliminates the H in the 2-amino group of an amino acid when located on the left side of the symbol; both modifications can be applied to the same symbol (see Table 1).

[0044] Table 1 Structures of amino acid residues and their one-letter and three-letter abbreviations

[0045]

[0046] The beneficial effects achieved by the present invention compared with the prior art include:

[0047] 1. The polypeptide of the present invention is obtained by artificial design, is easy to synthesize, is safe and non-irritating to the human body, and can be applied to the field of cosmetics.

[0048] 2. The polypeptide or salt thereof described in the present invention can inhibit the activity of hyaluronidase, maintain the content and function of hyaluronic acid in the body, thereby reducing the skin's neurological response to irritants, enhancing skin tolerance, improving skin sensitivity, having a good soothing effect, and can be used in skin soothing products. BRIEF DESCRIPTION OF THE DRAWINGS

[0049] Figure 1 It is Ac-Phe-Phe-Trp-Phe-Lys-Val-NH2 (molecular formula C 51 H 63 N9O7) mass spectrum, [M+H] + The mass-to-charge ratio (m / z) of the quasi-molecular ion peak is 914.5160, and the molecular weight measured by mass spectrometry is 913.52.

[0050] Figure 2 This is a graph showing the effect of the test samples on hyaluronidase activity. DETAILED DESCRIPTION

[0051] In order to better understand the present invention, the invention is described in detail below in conjunction with embodiments and drawings. However, it should be understood that these embodiments and drawings are only used for illustrative purposes and are not intended to limit the scope of the present invention.

[0052] abbreviation

[0053] The abbreviations used for amino acids follow the rules specified by the Biochemical Nomenclature Commission of the IUPAC-IUB in Eur J. Biochem. (1984) 138:9-37 and J. Chem (1989) 264:633-673.

[0054] Amide Resin: a starting resin for peptide synthesis (cross-linking degree 1%, substitution degree 1.42mmol / g); Fmoc-Linker: 4-[(2,4-dimethoxyphenyl)(Fmoc-amino)methyl]phenoxyacetic acid; Ac2O: acetic anhydride; DMF: N,N-dimethylformamide; DIPEA: diisopropylethylamine; DIC: diisopropylcarbodiimide; piperidine: piperidine; HOBt: 1-hydroxybenzotriazole; TFA: trifluoroacetic acid; TIS: triisopropylsilane; EDT: 1,2-ethanedithiol; Phe: phenylalanine; Trp: tryptophan; Lys: lysine; Val: valine; Fmoc: 9-fluorenylmethoxycarbonyl; Boc: tert-butoxycarbonyl.

[0055] Example 1 Preparation of Ac-Phe-Phe-Trp-Phe-Lys-Val-NH2

[0056] 1.1 Resin treatment

[0057] Weigh 5 g of Amide Resin resin into a solid phase synthesis reaction column, swell it with DMF, wash the resin, and remove the solvent.

[0058] Weigh 8.3 g of Fmoc-Linker and 2.517 g of HOBt into a dry conical flask, dissolve them in DMF solvent, cool them in an ice-water bath for 2 min, and add 3.187 mL of DIC to activate them for 3 min, avoiding moisture.

[0059] The activated Fmoc-Linker was added to the swollen resin and reacted for 3.5 h. The reaction solution was removed, the resin was washed, and the solvent was removed.

[0060] Ac2O and DIPEA were added to cap the reaction mixture for 1.5 h. The resin was washed and the solvent was removed.

[0061] 1.2 Removal of Fmoc

[0062] Fmoc-Linker-Amide Resin was de-Fmoced twice with 20% piperidine / DMF, each time for 10 min, and samples were taken for K testing, showing dark blue color. The resin was washed with DMF for 6 times, and the solvent was removed.

[0063] 1.3 Feeding reaction

[0064] Weigh 6.3g of Fmoc-Val-OH and 3.011g of HOBt into a dry conical flask, add DMF to dissolve it, seal it and place it in a -18℃ refrigerator for 30min. Add 3.8mL of DIC to activate for 3min, avoiding moisture. Add the activated amino acid to the deprotected resin and react for 2h, then remove the reaction solution. The K test resin is colorless and transparent, indicating that the reaction is complete.

[0065] The N-terminal Fmoc group was deprotected, and 8.7 g of the activated Fmoc-Lys(Boc)-OH was coupled to the peptidyl resin using DMF as solvent in the presence of 3.011 g HOBt and 3.8 mL DIC, and the reaction was continued for 2 h. The resins were then washed and the deprotection of the Fmoc group was repeated to couple the next amino acid. In each coupling, 7.2 g of Fmoc-Phe-OH; 9.8 g of Fmoc-Trp(Boc)-OH; 7.2 g of Fmoc-Phe-OH and then 7.2 g of Fmoc-Phe-OH were sequentially coupled in the presence of 3.011 g HOBt and 3.8 mL DIC using DMF as solvent; after the reaction was complete, the resin was washed and the solvent was removed.

[0066] Deprotect the N-terminal Fmoc group of the peptide resin by using 20% ​​piperidine / DMF for two times, each time for 10 minutes, and take a sample for K test, the color is dark blue. Wash the resin with DMF for 6 times, and remove the solvent.

[0067] In the presence of DIPEA, 3.8 g of Ac2O was coupled to the peptidyl resin using DMF as solvent. The reaction was continued for 1.5 h. The resin was washed, the solvent was removed, and 10 g of Ac-Phe-Phe-Trp(Boc)-Phe-Lys(Boc)-Val-Linker-Amide Resin was obtained after shrinkage and drying.

[0068] 1.4 Lysis

[0069] Measure 38.5 mL of TFA, 1.05 mL of TIS, 1.05 mL of water and 1.05 mL of EDT, mix and stir evenly to obtain a cleavage solution, seal it and place it in a -18°C refrigerator for later use; place isopropyl ether in a -18°C refrigerator for later use.

[0070] Weigh 10g of Ac-Phe-Phe-Trp(Boc)-Phe-Lys(Boc)-Val-Linker-Amide Resin, add it to a round-bottom flask, add the frozen lysate, and stir to react for 2.5h. Filter by suction, collect the filtrate, concentrate, add isopropyl ether, stir, centrifuge and wash 6 times until the pH value is 3-4, and vacuum dry to obtain 5.5g of Ac-Phe-Phe-Trp-Phe-Lys-Val-NH2 crude peptide.

[0071] 1.5 Purification

[0072] Weigh 5.5 g of crude peptide and dissolve it in 200 mL of methanol: acetic acid: water (V:V:V = 8:1:1). Filter with a microporous filter membrane with a pore size of 0.22 μm to obtain a clear and transparent solution. Purify it by reverse phase HPLC. The purification gradient is as follows:

[0073]

[0074]

[0075] The filtered sample was injected for purification, and the fractions were collected, concentrated and freeze-dried to obtain the polypeptide Ac-Phe-Phe-Trp-Phe-Lys-Val-NH2 with a purity of 99.027%.

[0076] The molecular weight of the peptide was determined by ESI-MS. The test results are shown in Figure 1 The molecular weight mass spectrometry analysis result is 913.52.

[0077] Example 2 Hyaluronidase inhibition experiment

[0078] 2.1 Reagents and Materials

[0079] Hyaluronic acid, hyaluronidase, water.

[0080] 2.2 Instruments

[0081] ELISA instrument, electric constant temperature water bath.

[0082] 2.3 Samples to be tested

[0083] Peptide (Ac-Phe-Phe-Trp-Phe-Lys-Val-NH2), tested concentrations were 25ppm, 50ppm, 100ppm, 200ppm, and 400ppm.

[0084] 2.4 Experimental methods

[0085] The Elson-Morgan modified method was used to determine the inhibitory effect of the peptide on hyaluronidase. The experiment was divided into 3 groups: blank control group A1 (water + hyaluronic acid + hyaluronidase), blank control group A2 without enzyme (water + hyaluronic acid), sample group B1 (test samples of different concentrations + hyaluronic acid + hyaluronidase), and sample group B2 without enzyme (test samples of different concentrations + hyaluronic acid). The total reaction volume of each group was the same. The OD value of the sample was measured at a wavelength of 570nm using an enzyme reader. Each concentration of the sample was measured 4 times in parallel, and the average value was taken to calculate the inhibition rate of the peptide on hyaluronidase.

[0086] The hyaluronidase inhibition rate was calculated according to the following formula:

[0087] Hyaluronidase inhibition rate = [(A1-A2)-(B1-B2)] / (A1-A2)×100%.

[0088] 2.5 Experimental Results

[0089] Hyaluronidase is a specific cleavage enzyme of hyaluronic acid, and hyaluronic acid is related to skin soothing. Inhibiting the activity of hyaluronidase is beneficial to maintaining the normal content and function of hyaluronic acid. Therefore, inhibiting the activity of hyaluronidase can achieve a soothing effect. The higher the hyaluronidase inhibition rate, the stronger the soothing effect.

[0090] The results of the test samples' effects on hyaluronidase activity are shown in Figure 2 The results showed that the polypeptide was able to inhibit hyaluronidase activity in the range of 25-400ppm. The inhibition rate was 6.03% at 25ppm, 18.95% at 50ppm, 39.56% at 100ppm, 37.32% at 200ppm, and as high as 52.13% at 400ppm.

[0091] It can be seen from this that the polypeptide of the present invention can inhibit the activity of hyaluronidase and maintain the content of hyaluronic acid in the body, thereby reducing the skin's neurological response to irritants, enhancing skin tolerance, improving skin sensitivity, and has a good soothing effect, and can be used in skin soothing products.

[0092] Example 3 Preparation of a polypeptide-containing serum

[0093]

[0094] Preparation method: Stir and heat purified water to 85°C and keep warm for 30 minutes; pre-dissolve sodium hyaluronate and xanthan gum in butylene glycol, add to water, and stir to dissolve completely; stir and cool to 35°C, add remaining ingredients, and stir evenly.

[0095] Example 4 Preparation of polypeptide-containing toner

[0096]

[0097] Preparation method: dissolve allantoin and glycerin in water, heat to 85°C, and keep warm for 30 minutes; dissolve PEG-7 glyceryl cocoate and polypeptide in water; mix and stir the above solutions after cooling to obtain a mixed solution; add propylene glycol, preservatives, and flavors to the above mixed solution in turn, add water and stir to obtain.

[0098] Although the preferred embodiments of the present invention have been described, those skilled in the art may make additional changes and modifications to these embodiments once they have learned the basic creative concept. Therefore, the appended claims are intended to be interpreted as including the preferred embodiments and all changes and modifications that fall within the scope of the embodiments of the present invention.

[0099] Finally, it should be noted that, in this article, relational terms such as first and second, etc. are only used to distinguish one entity or operation from another entity or operation, and do not necessarily require or imply any such actual relationship or order between these entities or operations. Moreover, the terms "include", "comprise" or any other variants thereof are intended to cover non-exclusive inclusion, so that a process, method, article or terminal device including a series of elements includes not only those elements, but also other elements not explicitly listed, or also includes elements inherent to such process, method, article or terminal device. In the absence of further restrictions, the elements defined by the sentence "comprise a ..." do not exclude the existence of other identical elements in the process, method, article or terminal device including the elements.

[0100] The novel use of the polypeptide provided by the present invention in preparing a composition for soothing the skin is introduced in detail above. Specific examples are used herein to illustrate the principle and implementation mode of the present invention. The description of the above embodiments is only used to help understand the method of the present invention and its core idea. At the same time, for those skilled in the art, according to the idea of ​​the present invention, there will be changes in the specific implementation mode and application scope. In summary, the content of this specification should not be understood as limiting the present invention.

Claims

1. Use of a polypeptide or a salt thereof in preparing a composition for soothing skin, wherein the soothing skin comprises one or more of inhibiting hyaluronidase activity, reducing the skin's neurological response to irritants, or enhancing skin tolerance; The sequence of the polypeptide is Ac-Phe-Phe-Trp-Phe-Lys-Val-NH2.

2. The use according to claim 1, characterized in that The composition comprises the polypeptide or its salt in a mass percentage concentration of 0.0001%-5%.

3. The use according to claim 1, characterized in that The composition comprises the polypeptide or its salt in a mass percentage concentration of 0.0005%-1%.

4. The use according to claim 1, characterized in that The composition comprises the polypeptide or its salt in a mass percentage concentration of 0.001%-0.1%.

5. The use according to claim 1, characterized in that: The composition comprises the polypeptide or its salt in a mass percentage concentration of 0.005%-0.01%.

6. The use according to claim 1, characterized in that: The salt of the polypeptide includes a metal salt of the polypeptide, and the metal includes: lithium, sodium, potassium, calcium, magnesium, manganese, copper, zinc or aluminum; The salt of the polypeptide includes a salt formed by the polypeptide and an organic base, and the organic base includes: ethylamine, diethylamine, ethylenediamine, ethanolamine, diethanolamine, arginine, lysine, histidine or piperazine; The salt of the polypeptide includes a salt formed by the polypeptide and an inorganic acid or an organic acid. The organic acid includes acetic acid, citric acid, lactic acid, malonic acid, maleic acid, tartaric acid, fumaric acid, benzoic acid, aspartic acid, glutamic acid, succinic acid, oleic acid, trifluoroacetic acid, oxalic acid, pamoic acid or gluconic acid; the inorganic acid includes hydrochloric acid, sulfuric acid, boric acid or carbonic acid.

7. The use according to claim 1, characterized in that The polypeptide or its salt is incorporated into a cosmetically or pharmaceutically acceptable delivery system or sustained-release system, or adsorbed onto a cosmetically or pharmaceutically acceptable solid organic polymer or solid inorganic support; The cosmetically or pharmaceutically acceptable delivery system or sustained release system is selected from the group consisting of liposomes, oleosomes, nonionic surfactant liposome vesicles, ethosomes, millicapsules, microcapsules, nanocapsules, nanostructured lipid carriers, sponges, lipid vesicles, micelles, millispheres, microspheres, nanospheres, lipid spheres, microemulsions, nanoemulsions, milliparticles, microparticles and nanoparticles; The cosmetically or pharmaceutically acceptable solid organic polymer or solid inorganic support is selected from the group consisting of talc, bentonite, silicon dioxide, starch or maltodextrin.

8. The use according to claim 7, characterized in that The cosmetically or pharmaceutically acceptable delivery system or sustained-release system is a liposome or a microemulsion.

9. The use according to claim 7, characterized in that: The cosmetically or pharmaceutically acceptable delivery system or sustained-release system is a water-in-oil microemulsion having an internal structure of reverse micelles.

10. The use according to claim 1, characterized in that The composition is a cosmetic composition or a pharmaceutical composition, and the formulation of the composition is selected from: cream, oil, balm, foam, lotion, gel, liniment, serum, ointment, mousse, powder, stick, pen, spray, aerosol, capsule, tablet, granule, suspension, emulsion, elixir, polysaccharide film or jelly.

11. The use according to claim 1, characterized in that The composition further comprises at least one other active agent for enhancing the soothing effect, wherein the other active agent is selected from peptides, natural plant ingredients, urea capsules or dipotassium glycyrrhizinate.

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