CN116019735A - New use of polypeptide in preparation of composition for relieving skin - Google Patents
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Abstract
The present invention provides a use of a polypeptide or a salt thereof in the manufacture of a composition for soothing skin comprising one or more of inhibiting hyaluronidase activity, reducing the neurological response of the skin to a stimulus or enhancing skin tolerance. The sequence of the polypeptide is Ac-Phe-Phe-Trp-Phe-Lys-Val-NH 2 The hyaluronic acid can inhibit the activity of hyaluronidase, maintain the content of hyaluronic acid in the organism, thereby reducing the nervous response of skin to irritants, enhancing the skin tolerance capability, improving the skin sensitive state, having good relieving effect and being applied to products for relieving skin.
Description
Technical Field
The invention belongs to the technical field of active polypeptides, and particularly relates to a novel application of a polypeptide in preparing a composition for relieving skin.
Background
Skin irritation occurs as a complex process involving the skin barrier, the cutaneous nervous system, the skin immune cells. Under the combined action of intrinsic and extrinsic factors such as excessive "exfoliating skin", "skin changing", the skin barrier function is impaired, leading to an increase in sensory nerve afferent signals, leading to an increase in the responsiveness of the skin to external stimuli, and thus to the initiation of the skin immune response. After the skin barrier function is compromised, some cytokines are often released at the site of the damage. These cytokines can further promote sensitization of the topically receptive cells and delay barrier repair, thereby forming a vicious circle, resulting in a disunion of sensitive skin. Investigation shows that the sensitive skin crowd accounts for 30% -40% of all people. The product with the relieving effect is an important research direction of daily chemicals because the product can effectively reduce the irritation degree of skin and improve the sensitive state of the skin.
Studies have shown that inhibiting hyaluronidase activity is beneficial to soothing the skin. Hyaluronidase is a specific lyase of hyaluronic acid, and hyaluronic acid is the component with the largest content and the largest proportion in extracellular matrix, which can maintain the volume of extracellular matrix, regulate and control the secretion of cell growth factors and cytokines, and influence the adhesion, growth, proliferation and differentiation of cells. Hyaluronic acid thus plays an important role in maintaining skin moisture and elasticity, wound healing, angiogenesis, and the like. Under the influence of adverse factors such as ultraviolet radiation, exogenous stimulus and the like, the mast cells activate and release histamine, so that the activity of the hyaluronidase is increased, and the increase of the hyaluronidase activity can promote the degradation of the hyaluronic acid, so that the skin generates allergic reaction.
Therefore, the skin tolerance can be enhanced by inhibiting the activity of hyaluronidase, reducing the nervous response of skin to stimulus, fundamentally improving the sensitive state of skin and solving the sensitive skin problem, thereby meeting the increasing demands of treating or caring skin.
Disclosure of Invention
As a result of experimental studies, the present inventors have found that a polypeptide can inhibit the activity of hyaluronidase and has an effect of soothing the skin, thereby completing the present invention.
Accordingly, the present invention aims to provide the use of a polypeptide or a salt thereof in the manufacture of a composition for soothing skin comprising one or more of inhibiting hyaluronidase activity, reducing the neurological response of the skin to a stimulus or enhancing skin tolerance.
The sequence of the polypeptide is Ac-Phe-Phe-Trp-Phe-Lys-Val-NH 2 。
These polypeptides of the invention may exist as stereoisomers or as mixtures of stereoisomers; for example, the amino acids comprising them may have the configuration L-, D-, or be racemic independently of each other. 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 these polypeptides of the invention are pure isomers, i.e., enantiomers or diastereomers.
For example, when-Lys-is described herein, it is understood that-Lys-is selected from-L-Lys-, -D-Lys-, or a mixture of both, is racemic or non-racemic. The preparation methods described in this document enable one of ordinary skill in the art to obtain each stereoisomer of the polypeptide of the invention by selecting amino acids with the correct configuration.
The invention also includes all suitable isotopic variants of the polypeptides. Isotopic variations of these polypeptides of the present invention are understood herein to mean compounds: wherein at least one atom is replaced by another atom of the same atomic number within the polypeptide of the invention, but of an atomic mass different from that which is usual or prevailing in nature. Examples of isotopes that can be incorporated into polypeptides of the 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. Specific isotopic variations of the polypeptides of the present invention (particularly those into which one or more radioisotopes have been incorporated) may be advantageous, for example, for examining the mechanism of action or the distribution of active compounds in vivo; due to relatively simple producibility and detectability, especially with 3 H or 14 C isotopically labeled compounds are suitable for this purpose. In addition, due to the greater metabolic stability of the compounds, the incorporation of isotopes (e.g., deuterium) may yield particular therapeutic benefits, such as increased in vivo half-life or reduced amounts of active agent required; thus, in certain instances, such modifications to the polypeptides of the invention may also constitute preferred embodiments of the invention. Isotopic variants of the polypeptides of the present invention can be prepared by methods known to those skilled in the art, for example by methods further described below and in the examples, by using the respective reagents and/or corresponding isotopic modifications of the starting materials.
In addition, the invention also includes prodrugs of the polypeptides of the invention. The term "prodrug" means herein such compounds: which may be biologically active or inactive in itself, but which react (e.g., metabolize or hydrolyze) to form the compounds of the invention during their residence time in the body.
Optionally, the composition comprises a polypeptide or salt thereof at a concentration of 0.0001% to 5% by mass;
optionally, the composition comprises a polypeptide or salt thereof at a mass percent concentration of 0.0005% to 1%;
optionally, the composition comprises a polypeptide or salt thereof at a mass percent concentration of 0.001% to 0.1%;
optionally, the composition comprises the polypeptide or salt thereof at a mass percent concentration of 0.005% to 0.01%.
The polypeptide can inhibit the activity of hyaluronidase and maintain the content of hyaluronic acid in the organism, thereby reducing the nervous response of skin to irritants, enhancing the skin tolerance capability, improving the skin sensitive state, having good skin soothing effect and being applied to soothing products.
Optionally, the salt of the polypeptide comprises a metal salt of the polypeptide, the metal comprising: lithium, sodium, potassium, calcium, magnesium, manganese, copper, zinc or aluminum;
alternatively, the salt of the polypeptide comprises a salt of the polypeptide with an organic base comprising: ethylamine, diethylamine, ethylenediamine, ethanolamine, diethanolamine, arginine, lysine, histidine or piperazine;
alternatively, the salt of the polypeptide comprises a salt of the polypeptide with an inorganic or organic acid comprising: 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;
optionally, the inorganic acid comprises: hydrochloric acid, sulfuric acid, boric acid or carbonic acid.
The above-mentioned polypeptide of the present invention or a salt thereof can be obtained according to a conventional method known in the art, for example, a solid phase synthesis method, a liquid phase synthesis method or a method of combining a solid phase with a liquid phase, and can also be prepared by a biotechnological method aimed at producing a desired sequence, or by controlled hydrolysis of a protein having animal, fungal, or plant origin.
For example, a method of obtaining a polypeptide comprises the steps of:
-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 protected or solid carrier-bound C-terminus;
-elimination of the group protecting the N-terminal end;
-repeating the coupling sequence and elimination of the N-terminal protecting group until the desired peptide sequence is obtained;
-elimination of the C-terminal protecting group or cleavage from the solid support.
Preferably, the C-terminus is bound to a solid support and the method is performed 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 polymeric support; eliminating the group protecting the N-terminus; and repeating this sequence as many times as necessary to thereby obtain a polypeptide having a desired length, followed by cleavage of the synthesized polypeptide from the original polymer carrier.
The functional groups of the side chains of these amino acids remain fully protected with temporary or permanent protecting groups throughout the synthesis and may be deprotected simultaneously or orthogonally to the process of cleaving the peptide from the polymeric carrier.
The method may comprise the further steps of: the functional groups of the ends may be subsequently modified using standard conditions and methods known in the art to deprotect the N-and C-termini and/or cleave the peptide from the polymeric support in a non-defined order. The optional modification of the N-and C-termini of the polypeptide bound to the polymeric support may be performed, or after the peptide has been cleaved from the polymeric support.
The polypeptide or salt thereof may be incorporated into a cosmetically or pharmaceutically acceptable delivery system or a slow release system in order to achieve better penetration of the active ingredient and/or to improve its pharmacokinetic and pharmacodynamic properties, the polypeptide or salt thereof or the composition may be applied to the skin and/or mucous membranes, or orally or parenterally as required for the treatment and/or care of a condition, disorder and/or disease.
The frequency of administration or dosing may vary widely depending on the needs of each subject, with recommended administration or dosing ranging from 1 per month to 10 times per day, preferably from 1 per week to 4 times per day, more preferably from 3 per week to 3 times per day, even more preferably 1 or 2 times per day.
The term "delivery system" refers to a diluent, adjuvant, excipient, or carrier with which a compound of the invention is administered, selected from the group consisting of: water, oils or surfactants, including those of petroleum origin, animal origin, vegetable origin, or synthetic origin, such as, and not limited to, peanut oil, soybean oil, mineral oil, sesame oil, castor oil, polysorbates, sorbitan esters, ether sulfates, betaines, glucosides, maltosides, fatty alcohols, nonoxynol, poloxamers, polyoxyethylene, polyethylene glycols, dextrose, glycerol, digitonin, and the like. Diluents which may be used in different delivery systems to which the compounds of the invention may be administered are known to those of ordinary skill in the art.
The term "sustained release" is used in a conventional sense to refer to a delivery system that provides a gradual release of a compound over a period of time, and preferably, but not necessarily, has a relatively constant level of release of the compound over the entire period of time.
Examples of delivery systems or slow release systems are liposomes, oleosomes, nonionic surfactant liposome vesicles, ethosomes, millimeter-capsules, microcapsules, nanocapsules, nanostructured lipid carriers, sponges, cyclodextrins, lipid vesicles, micelles, millimeter-spheres, microspheres, nanospheres, lipid spheres, microemulsions, nanoemulsions, millimeter-particles, microparticles or nanoparticles. Preferred delivery systems or slow release systems are liposomes and microemulsions, more preferably water-in-oil microemulsions having an internal structure of reverse micelles.
Sustained release systems can be prepared by methods known in the art and can be administered, for example, by: by topical or transdermal administration, including adhesive patches, non-adhesive patches, occlusive patches, and microelectronic patches; or by systemic administration, such as and without limitation, oral or parenteral routes, including nasal, rectal, subcutaneous implantation or injection, or direct implantation or injection into a particular body site, and preferably should release relatively constant amounts of these compounds of the invention. The amount of compound included in the sustained release system will depend, for example, on the site to which the composition is to be administered, the kinetics and duration of release of the compounds of the invention, and the nature of the condition, disorder and/or disease to be treated and/or treated.
The above polypeptide or a salt thereof may also be adsorbed on a solid organic polymer or a solid inorganic support, for example and without limitation, talc, bentonite, silica, starch, maltodextrin, or the like.
Alternatively, the composition is a cosmetic composition or a pharmaceutical composition.
The formulation of the composition is selected from: cream, oil, balm, foam, lotion, gel, wipe, slurry, ointment, mousse, powder, stick, pen, spray, aerosol, capsule, tablet, granule, chewing gum, solution, suspension, emulsion, elixir, polysaccharide film, jelly, or gelatin.
Optionally, the composition further comprises at least one additional active agent for enhancing the soothing effect, said additional active agent being selected from peptides, natural plant ingredients, urea vesicles or dipotassium glycyrrhizinate.
In order to facilitate understanding of the invention, the meaning of some terms and expressions used in the present invention is described as follows:
in the present invention, the term "skin" is understood to mean the layers that make up it, from the uppermost or stratum corneum to the lowermost or subcutaneous tissue, both endpoints being included. These layers are composed of different types of cells, such as keratinocytes, fibroblasts, melanocytes, and/or adipocytes, among others. In the present invention, the term "skin" includes the scalp.
The amino acid abbreviations used in the present invention follow the rules specified by the IUPAC-IUB Biochemical nomenclature Commission in European journal of biochemistry (Eur. J. Biochem. 1984, 138:9-37).
For example, lys represents NH 2 -CH(CH 2 CH 2 CH 2 CH 2 NH 2 ) -COOH, lys-represents NH 2 -CH(CH 2 CH 2 CH 2 CH 2 NH 2 ) -CO-, -Lys represents-NH-CH (CH) 2 CH 2 CH 2 CH 2 NH 2 ) -COOH, and-Lys-represents-NH-CH (CH) 2 CH 2 CH 2 CH 2 NH 2 ) -CO-. Thus, the hyphen representing the peptide bond eliminates the OH in the 1-carboxyl group of the amino acid (represented here in conventional non-ionized form) when located to the right of the symbol, and eliminates the H in the 2-amino group of the amino acid when located to the left of the symbol; two kinds of modification canTo apply to the same symbol (see table 1).
TABLE 1 Structure of amino acid residues and their single and three letter abbreviations
The beneficial effects obtained by the invention relative to the prior art include:
1. the polypeptide is obtained through artificial design, is convenient to synthesize, is safe and non-irritating to human bodies, and can be applied to the field of cosmetics.
2. The polypeptide or the salt thereof can inhibit the activity of hyaluronidase, maintain the content and the function of hyaluronic acid in a human body, thereby reducing the nervous response of skin to irritants, enhancing the skin tolerance capability, improving the skin sensitive state, having good relieving effect and being applied to products for relieving skin.
Drawings
FIG. 1 is Ac-Phe-Phe-Trp-Phe-Lys-Val-NH 2 (formula C) 51 H 63 N 9 O 7 ) Mass spectrum, [ M+H ]] + The mass to charge ratio (m/z) of the excimer ion peak was 914.5160 and the mass spectrum measured molecular weight was 913.52.
FIG. 2 is a graph showing the effect of a test sample on hyaluronidase activity.
Detailed Description
For a better understanding of the present invention, reference will now be made in detail to the present invention, examples of which are illustrated in the accompanying drawings, however, it being understood that the examples and the accompanying drawings are for illustrative purposes only and are not intended to limit the scope of the present invention.
Abbreviations (abbreviations)
The abbreviation for amino acids follows the biochemical nomenclature Committee of IUPAC-IUB at Eur J.biochem. (1984) 138:9-37 and J.chem (1989) 264: 633-673.
Amide Resin: a starting resin for polypeptide synthesis (crosslinking degree 1%, substitution degree 1.42 mmol/g); fmoc-Linker:4- [ (24-dimethoxyphenyl) (Fmoc-amino) methyl]Phenoxyacetic acid; ac (Ac) 2 O: 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: and tert-butoxycarbonyl group.
Example 1 Ac-Phe-Phe-Trp-Phe-Lys-Val-NH 2 Is prepared from
1.1 Treatment of resin
5g of Amide Resin was weighed into a solid phase synthesis reaction column, swollen with DMF, washed the Resin and the solvent was removed.
8.3g Fmoc-Linker, 2.517g HOBt were weighed into a drying flask. After being dissolved by DMF solvent, the mixture is placed in ice water bath for cooling for 2min, 3.187mL DIC is added for activation for 3min, and water vapor is avoided.
Adding the activated Fmoc-Linker into the swelled resin, reacting for 3.5 hours, pumping out the reaction liquid, washing the resin, and pumping out the solvent.
Continuing to add Ac 2 O and DIPEA were capped for 1.5h. The resin was washed and the solvent was pumped away.
1.2 Fmoc removal
Fmoc-Linker-Amide Resin was Fmoc-removed twice with 20% piperidine/DMF for 10min each time, sampled K for detection, and developed dark blue. The resin was washed 6 times with DMF and the solvent was removed.
1.3 Feeding reaction
6.3g Fmoc-Val-OH,3.011g HOBt were weighed into a dry flask, dissolved in DMF and sealed in a-18℃refrigerator for 30min. 3.8mL DIC was added to activate for 3min to avoid water vapor. And adding the activated amino acid into the deprotected resin for reaction for 2 hours, and pumping away the reaction solution. K detection resin is colorless and transparent, which indicates that the reaction is complete.
The N-terminal Fmoc group was deprotected and 8.7g of Fmoc-Lys (Boc) -OH after activation was coupled to the peptidyl resin using DMF as solvent in the presence of 3.011g HOBt and 3.8mL DIC, and the reaction was continued for 2h. These resins were then washed and the deprotection treatment of the Fmoc group was repeated to couple the next amino acid. In each coupling, 7.2g of Fmoc-Phe-OH were coupled sequentially using DMF as solvent in the presence of 3.011g of HOBt and 3.8mL of DIC; 9.8g Fmoc-Trp (Boc) -OH;7.2g Fmoc-Phe-OH followed by 7.2g Fmoc-Phe-OH; after the reaction was completed, the resin was washed and the solvent was removed.
The N-terminal Fmoc group of the peptidyl resin was deprotected and Fmoc was removed twice with 20% pipeidine/DMF for 10min each time, sampling K and developing dark blue. The resin was washed 6 times with DMF, the solvent was removed,
3.8g of Ac in the presence of DIPEA were treated with DMF as solvent 2 O is coupled to the peptide-based Resin, the reaction is continued for 1.5h, the Resin is washed, the solvent is pumped away, and 10g of Ac-Phe-Phe-Trp (Boc) -Phe-Lys (Boc) -Val-Linker-Amide Resin is obtained after shrinkage and drying.
1.4 Cleavage of
Measuring 38.5mL of TFA, 1.05mL of TIS, 1.05mL of water and 1.05mL of EDT, mixing and stirring uniformly to obtain a lysate, sealing and placing in a refrigerator at-18 ℃ for later use; the isopropyl ether is placed in a refrigerator at the temperature of minus 18 ℃ for refrigeration for standby.
10g of Ac-Phe-Phe-Trp (Boc) -Phe-Lys (Boc) -Val-Linker-Amide Resin was weighed, added to a round bottom flask, the frozen lysate was added, and the reaction was stirred for 2.5h. Suction filtering, collecting filtrate, concentrating, adding isopropyl ether, stirring, centrifugally washing for 6 times until the pH value is 3-4, and vacuum drying to obtain 5.5g of Ac-Phe-Phe-Trp-Phe-Lys-Val-NH 2 Crude peptide.
1.5 Purification
Weigh 5.5g of crude peptide in 200mL methanol: acetic acid: in water (V: v=8:1:1), a clear and transparent solution was obtained by filtration through a microporous membrane with a pore size of 0.22 μm, purified by reverse phase HPLC with the following purification gradient:
| time (min) | Flow rate (mL/min) | A% (acetonitrile) | B% (0.1% acetic acid + pure water) |
| 0 | 40 | 15 | 85 |
| 12 | 40 | 18 | 82 |
| 40 | 40 | 45 | 55 |
| 54 | 40 | 60 | 40 |
| 57 | 40 | 75 | 25 |
| 68 | 40 | 75 | 25 |
Purifying the filtered sample, collecting the fraction, concentratingLyophilizing to obtain polypeptide Ac-Phe-Phe-Trp-Phe-Lys-Val-NH with purity of 99.027% 2 。
The molecular weight of the polypeptide was determined by ESI-MS, and the test result is shown in FIG. 1, and the molecular weight mass spectrum analysis result is 913.52.
EXAMPLE 2 hyaluronidase inhibition assay
2.1 Reagents and materials
Hyaluronic acid, hyaluronidase, and water.
2.2 Instrument for measuring and controlling the intensity of light
An enzyme-labeled instrument and an electric heating constant temperature water bath kettle.
2.3 Sample to be measured
Polypeptide (Ac-Phe-Phe-Trp-Phe-Lys-Val-NH) 2 ) The test concentrations were 25ppm, 50ppm, 100ppm, 200ppm, 400ppm.
2.4 Experimental method
Inhibition of hyaluronidase by the polypeptide was determined by the Elson-Morgan improvement method. The experiments were divided into 3 groups: blank control group A 1 (Water+hyaluronan+hyaluronidase), no enzyme blank group A 2 (Water+hyaluronic acid), sample group B 1 (test samples at different concentrations+hyaluronic acid+hyaluronidase), enzyme-free sample group B 2 (different concentrations of test sample + hyaluronic acid), the total reaction volumes of each group are the same. The OD value of the sample is measured at 570nm by using an enzyme-labeled instrument, the sample at each concentration is measured for 4 times in parallel, the average value is taken, and the inhibition rate of the polypeptide to the hyaluronidase is calculated.
The hyaluronidase inhibition rate was calculated as follows:
hyaluronidase inhibition rate = [ (a) 1 －A 2 ）－（B 1 －B 2 ）]/（A 1 －A 2 ）×100%。
2.5 Experimental results
Hyaluronidase is a specific cleavage enzyme of hyaluronic acid, and hyaluronic acid is related to skin relief, and inhibiting the activity of the hyaluronidase is beneficial to maintaining the content and the normal function of the hyaluronic acid, so that the inhibition of the activity of the hyaluronidase can achieve the effect of relief, and the higher the inhibition rate of the hyaluronidase is, the stronger the effect of relief is.
The results of the influence of the test sample on the hyaluronidase activity are shown in fig. 2, and the results show that the polypeptide can inhibit the hyaluronidase activity in the range of 25-400ppm, the inhibition rate of the polypeptide is 6.03% at 25ppm, 18.95% at 50ppm, 39.56% at 100ppm, 37.32% at 200ppm and 52.13% at 400ppm.
Therefore, the polypeptide disclosed by the invention can inhibit the activity of hyaluronidase and maintain the content of hyaluronic acid in the organism, so that the nervous reaction of skin to a stimulator is reduced, the skin tolerance capacity is enhanced, the skin sensitive state is improved, and the polypeptide has a good relieving effect and can be applied to a product for relieving skin.
EXAMPLE 3 preparation of essence containing Polypeptides
| Composition of the components | Weight percent |
| Sodium hyaluronate | 0.05 |
| Butanediol (butanediol) | 3.00 |
| Xanthan gum | 0.10 |
| 1, 2-pentanediol | 2.00 |
| 1, 2-hexanediol | 0.50 |
| Trehalose | 2.00 |
| Polypeptides | 0.03 |
| Purified water | Moderate to 100 |
The preparation method comprises the following steps: stirring and heating the purified water to 85 ℃, and preserving heat for 30min; pre-dissolving sodium hyaluronate and xanthan gum in butanediol, adding into water, stirring and dissolving completely; stirring and cooling to 35 ℃, adding the rest ingredients, and stirring uniformly.
Example 4 preparation of toner containing polypeptide
| Composition of the components | Weight percent |
| Propylene glycol | 1.0 |
| Allantoin | 0.3 |
| Glycerol | 1.0 |
| PEG-7 glycerol cocoate | 1.0 |
| Polypeptides | 0.005 |
| Preservative agent | 0.5 |
| Essence | 0.5 |
| Water and its preparation method | Moderate to 100 |
The preparation method comprises the following steps: dissolving allantoin and glycerol with water, heating to 85deg.C, and maintaining for 30min; dissolving PEG-7 glycerol cocoate and polypeptide with water; the above solutions are cooled and then mixed, and the mixed solution is obtained after uniform stirring; and sequentially adding propylene glycol, preservative and essence into the mixed solution, adding water and stirring uniformly to obtain the product.
While preferred embodiments of the present invention have been described, additional variations and modifications in those embodiments may occur to those skilled in the art once they learn of the basic inventive concepts. It is therefore intended that the following claims be interpreted as including the preferred embodiment and all such alterations and modifications as fall within the scope of the embodiments of the invention.
Finally, it is further noted that relational terms such as first and second, and the like are used solely to distinguish one entity or action from another entity or action without necessarily requiring or implying any actual such relationship or order between such entities or actions. Moreover, the terms "comprises," "comprising," or any other variation thereof, are intended to cover a non-exclusive inclusion, such that a process, method, article, or terminal that comprises a list of elements does not include only those elements but may include other elements not expressly listed or inherent to such process, method, article, or terminal. Without further limitation, an element defined by the phrase "comprising one … …" does not exclude the presence of other like elements in a process, method, article or terminal device comprising the element.
The novel use of the polypeptides provided by the present invention in the preparation of compositions for soothing skin is described in detail, and specific examples are used herein to illustrate the principles and embodiments of the present invention, the above examples being provided only to assist in understanding the methods of the present invention and the core ideas thereof; meanwhile, as those skilled in the art will have variations in the specific embodiments and application scope in accordance with the ideas of the present invention, the present description should not be construed as limiting the present invention in view of the above.
Claims (7)
1. Use of a polypeptide or salt thereof in the manufacture of a composition for soothing skin comprising one or more of inhibiting hyaluronidase activity, reducing the neurological response of skin to a stimulus, or enhancing skin tolerance.
2. The use according to claim 1, wherein the sequence of the polypeptide is Ac-Phe-Phe-Trp-Phe-Lys-Val-NH 2 。
3. The use according to claim 1, wherein the composition comprises a polypeptide or a salt thereof in a concentration of 0.0001% to 5% by mass;
optionally, the composition comprises a polypeptide or salt thereof at a mass percent concentration of 0.0005% to 1%;
optionally, the composition comprises a polypeptide or salt thereof at a mass percent concentration of 0.001% to 0.1%;
optionally, the composition comprises the polypeptide or salt thereof at a mass percent concentration of 0.005% to 0.01%.
4. The use according to claim 1, wherein the salt of the polypeptide comprises a metal salt of the polypeptide, the metal comprising: lithium, sodium, potassium, calcium, magnesium, manganese, copper, zinc or aluminum;
salts of the polypeptides include salts of the polypeptides with organic bases including: ethylamine, diethylamine, ethylenediamine, ethanolamine, diethanolamine, arginine, lysine, histidine or piperazine;
salts of the polypeptides include salts of the polypeptides with inorganic or organic acids including: 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.
5. The use according to claim 1, wherein the polypeptide or salt thereof is incorporated into a cosmetically or pharmaceutically acceptable delivery system or a slow release system, or is adsorbed onto a cosmetically or pharmaceutically acceptable solid organic polymer or solid inorganic support;
the cosmetically or pharmaceutically acceptable delivery system or slow release system is selected from: liposomes, oleosomes, nonionic surfactant liposome vesicles, ethosomes, millimeter capsules, microcapsules, nanocapsules, nanostructured lipid carriers, sponges, cyclodextrins, lipid vesicles, micelles, millimeter spheres, microspheres, nanospheres, lipid spheres, microemulsions, nanoemulsions, millimeter particles, microparticles, and nanoparticles; the water-in-oil type microemulsion with the internal structure of reverse micelle is selected as liposome or microemulsion;
the cosmetically or pharmaceutically acceptable solid organic polymer or solid inorganic support is selected from: talc, bentonite, silica, starch or maltodextrin.
6. The use according to claim 1, characterized in that said composition is a cosmetic or pharmaceutical composition, the formulation of which is selected from: cream, oil, balm, foam, lotion, gel, wipe, slurry, ointment, mousse, powder, stick, pen, spray, aerosol, capsule, tablet, granule, chewing gum, solution, suspension, emulsion, elixir, polysaccharide film, jelly, or gelatin.
7. The use according to claim 1, wherein the composition further comprises at least one other active agent for enhancing the soothing effect, said other active agent being selected from peptides, natural plant ingredients, urea vesicles or dipotassium glycyrrhizinate.
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