A cyclic tetrapeptide compound, and a preparation method and application thereof

Abstract

This invention relates to the field of peptide technology, and more particularly to a cyclic tetrapeptide compound, its preparation method, and its applications. The peptide compound has the structure shown in Formula I, or its stereoisomer or salt thereof: c(AA1-AA2-AA3-AA4), Formula I. The cyclic tetrapeptide compound can simultaneously inhibit the release of the inflammatory factor IL-6 and effectively scavenge reactive oxygen species DPPH, ABTS, and PTIO. It can effectively inhibit the production of reactive oxygen species, alleviate skin inflammation, and improve skin condition, showing great promise in the fields of anti-inflammatory and antioxidant applications.

Description

Technical Field

[0001] This invention relates to the field of polypeptide technology, and in particular to a cyclic tetrapeptide compound, its preparation method, and its application. Background Technology

[0002] In recent years, increased life and work pressures, coupled with changes in the external environment, have led to a sharp increase in allergies, and skin inflammation has seriously affected people's normal lives. Skin inflammation refers to a state of the skin under physiological or pathological conditions, mainly related to impaired skin barrier function and epidermal inflammation. These factors often promote and accumulate each other, leading to a vicious cycle of sensitive skin problems.

[0003] Interleukin-6 (IL-6) is a multifunctional cytokine widely involved in inflammatory responses. In the case of sensitive skin, IL-6 is closely related to skin barrier dysfunction. When the skin barrier function is weakened, external irritants can more easily penetrate to the deeper layers of the skin, thereby triggering an inflammatory response. In this process, IL-6 is activated as an inflammatory factor and promotes the production of vascular endothelial growth factor (VEGF), which increases vascular reactivity and leads to vasodilation. Therefore, IL-6 plays a key role in the development of sensitive skin, and inhibiting or regulating IL-6 expression may help improve the condition of sensitive skin.

[0004] Reactive oxygen species (ROS) are strong oxidants that can trigger inflammatory responses and damage to the skin, thus exacerbating sensitive skin problems. Sensitive skin, due to its weakened barrier function, is more susceptible to external environmental factors such as UV radiation and chemicals, leading to the production of more ROS. These free radicals further intensify oxidative stress in the skin, causing inflammation. Inhibiting the production of IL-6 and free radicals can alleviate and improve skin inflammation; therefore, anti-inflammatory and antioxidant products are widely used in the cosmetics industry.

[0005] Currently, although there are many cosmetic products on the market that claim to be anti-inflammatory and soothing, very few can truly and effectively relieve inflammation. Moreover, many products are plant extracts, making it difficult to determine their effective ingredients. Often, many people do not experience significant improvement in their skin inflammation after using them. Summary of the Invention

[0006] In view of this, the technical problem to be solved by the present invention is to provide a cyclic tetrapeptide compound, its preparation method and application, which can effectively relieve skin inflammation.

[0007] This invention provides a cyclic tetrapeptide compound of general formula I, or its stereoisomer or its salt:

[0008] c(AA1-AA2-AA3-AA4), formula I;

[0009] In Formula I, AA1-AA2-AA3-AA4 is -Pro-Val-Pro-Tyr-, -Val-Pro-Tyr-Pro-, -Pro-Tyr-Pro-Val-, or -Tyr-Pro-Val-Pro-.

[0010] The -Pro-, -Val-, and -Tyr- groups mentioned above include their L-configuration, D-configuration, or racemic form. The configuration of the cyclic tetrapeptide compound can be adjusted by modifying the configurations of AA1, AA2, AA3, and AA4.

[0011] Preferably, AA1-AA2-AA3-AA4 is -Pro-Val-Pro-Tyr-.

[0012] In Equation I, c is an abbreviation for Cyclo, which means cycloid.

[0013] Preferably, the cyclic tetrapeptide compound has the following structure:

[0014]

[0015] This invention also provides salts of the aforementioned cyclic tetrapeptide compounds. These salts can be salts well-known to those skilled in the art and suitable for pharmaceutical compositions, health products, and cosmetic compositions, including but not limited to salt-free forms, organic base salts, and inorganic base salts. The organic base salts include, but are not limited to, ammonium salts, triethylamine salts, dicyclohexylamine salts, ethylenediamine salts, pyridinium salts, piperidine salts, choline salts, and betaine salts. The inorganic base salts include, but are not limited to, lithium salts, sodium salts, potassium salts, calcium salts, magnesium salts, iron salts, copper salts, and zinc salts.

[0016] Another aspect of the present invention provides a method for preparing the above-mentioned cyclic tetrapeptide compound, comprising the following steps:

[0017] S1) CTC resin is reacted with an amino acid reagent protected by an Fmoc group to obtain a peptide resin of H-AA4-AA3-AA2-AA1-CTC resin.

[0018] S2) Remove the resin from the peptide resin structure to obtain a fully protected polypeptide H-AA4-AA3-AA2-AA1-OH;

[0019] S3) Cyclize the fully protected polypeptide H-AA4-AA3-AA2-AA1-OH to obtain the fully protected Cyclo(AA1-AA2-AA3-AA4);

[0020] S4) After deprotection and purification of the fully protected Cyclo(AA1-AA2-AA3-AA4), the cyclic tetrapeptide Cyclo(AA1-AA2-AA3-AA4) is obtained;

[0021] The AA1-AA2-AA3-AA4 are -Pro-Val-Pro-Tyr-, -Val-Pro-Tyr-Pro-, -Pro-Tyr-Pro-Val-, or -Tyr-Pro-Val-Pro-.

[0022] The present invention does not specifically limit the reaction method between the CTC resin and the amino acid reagent protected by the Fmoc group in step S1) above, and can be a solid-phase reaction well known to those skilled in the art. The reaction is preferably carried out under the catalysis of DIEA. By adjusting the order of amino acid addition, peptides with specific sequences can be obtained.

[0023] Preferably, Fmoc-Pro-OH is first reacted with CTC resin, and then the Fmoc protecting group is removed; then it is reacted with Fmoc-Val-OH, and then the Fmoc protecting group is removed; then it is reacted with Fmoc-Pro-OH, and then the Fmoc protecting group is removed; then it is reacted with Fmoc-Tyr(OtBu)-OH to remove the Fmoc protecting group, thus obtaining the peptide resin of H-AA4-AA3-AA2-AA1-CTC resin.

[0024] The present invention does not specifically limit the method for removing resin in step S2) above, and can use methods well known to those skilled in the art. Preferably, the resin is removed in a TFA / DCM solution.

[0025] The present invention does not impose any particular limitation on the cyclization conditions in step S3) above, and can use any amino acid cyclization method well known to those skilled in the art. Preferably, the cyclization is carried out in the presence of DIC, HOBt, and DIEA. The preferred cyclization temperature is 20–40°C; the preferred cyclization time is 2–24 hours.

[0026] The present invention does not specifically limit the deprotection method in step S4) above, and can be any method for removing protecting groups known to those skilled in the art. Preferably, the deprotection is carried out in the presence of TFA and TIS; the deprotection time is preferably 1-5 hours.

[0027] After deprotection, the crude product was purified.

[0028] The purification process includes, but is not limited to, chromatographic purification and lyophilization.

[0029] The preferred method for chromatographic purification is reversed-phase C18 preparative chromatographic purification.

[0030] Another aspect of the present invention provides a composition comprising the above-described cyclic tetrapeptide compound, or its stereoisomer or its salt, and an excipient.

[0031] The present invention does not specifically limit the excipients, and can be any excipients known to those skilled in the art that are suitable for pharmaceutical compositions, health products, and cosmetic compositions.

[0032] The excipients include, but are not limited to, solvents, stabilizers, dispersants, surfactants, emulsifiers, thickeners, etc.

[0033] The cyclic tetrapeptide compound or composition provided by the present invention can also be used in combination with other pharmaceutical compositions, health products or cosmetic compositions with similar effects.

[0034] The present invention provides the use of the above-mentioned cyclic tetrapeptide compound, or its stereoisomer or its salt, or the above-mentioned composition in the preparation of products having anti-inflammatory, repairing, antioxidant, anti-allergic and / or anti-aging functions.

[0035] The products include, but are not limited to, pharmaceutical compositions, cosmetic compositions, health products, and other applicable categories.

[0036] Experimental results show that the cyclic tetrapeptide compound provided by the present invention can effectively inhibit the expression of IL-6 and the secretion of inflammatory factors, and has anti-inflammatory and soothing effects; at the same time, it can also effectively scavenge reactive oxygen free radicals DPPH, ABTS and PTIO, effectively inhibit the production of reactive oxygen species, relieve skin inflammation and improve skin condition.

[0037] Based on this, the present invention provides the use of the above-mentioned cyclic tetrapeptide compound, or its stereoisomer or its salt, or the above-mentioned composition in the preparation of cosmetic compositions, pharmaceutical compositions or health products for the prevention, treatment and / or relief of skin inflammation.

[0038] The aforementioned beauty compositions include, but are not limited to, skincare products such as creams, lotions, oils, ointments, gels, toners, serums, masks, facial cleansers, and makeup removers.

[0039] The above-mentioned drug compositions include, but are not limited to, dermal dosage forms, such as topical solutions, lotions, liniments, ointments, plasters, pastes, patches, etc.; and oral dosage forms, such as powders, tablets, granules, capsules, solutions, emulsions, suspensions, etc.

[0040] The aforementioned health products include, but are not limited to, common dosage forms such as tablets, capsules, granules, powders, oral liquids, tea bags, and water pills.

[0041] Compared with existing technologies, this invention provides a cyclic tetrapeptide compound of general formula I, or its stereoisomer or salt thereof: c(AA1-AA2-AA3-AA4), formula I. The cyclic tetrapeptide compound can simultaneously inhibit the release of the inflammatory factor IL-6 and effectively scavenge reactive oxygen species DPPH, ABTS, and PTIO, thus effectively inhibiting the production of reactive oxygen species, alleviating skin inflammation, and improving skin condition, showing excellent application prospects in the field of anti-inflammatory and antioxidant treatments. Attached Figure Description

[0042] Figure 1 The 1H NMR spectrum of the cyclic tetrapeptide compound 1 prepared in Example 1;

[0043] Figure 2 A bar graph showing the effect of cyclic tetrapeptide compound 1 on NIH / 3T3 cells;

[0044] Figure 3 A bar graph showing the expression levels of inflammatory factors in the experimental group containing cyclic tetrapeptide compound 1.

[0045] Figure 4 The graph shows the free radical scavenging rate of the experimental group containing cyclic tetrapeptide compound 1. Detailed Implementation

[0046] To further illustrate the present invention, a detailed description is provided below with reference to embodiments. However, it should be understood that these descriptions are merely for further illustrating the features and advantages of the present invention, and not for limiting the scope of the claims.

[0047] There are no particular restrictions on the source of any raw materials used in this invention; they can be purchased from the market or prepared using conventional methods known to those skilled in the art.

[0048] Example 1

[0049] Step S11: Place CTC resin (6.0 g, 6 mmol) in a 100 mL solid-phase synthesis reactor, add amino acid Fmoc-L-Pro-OH (8.1 g, 12 mmol), add 60 mL DMF, then add DIEA (8.4 mL), react at 25 °C for 3 h, add 6.0 mL methanol, react for 5 min, filter, wash the resin twice with 60 mL DMF, twice with 60 mL methanol, and twice with 60 mL DMF; then add 60 mL of 20% Pip / DMF solution to the solid-phase synthesis reactor, stir and react for 30 min, filter, remove the deprotection solution, then wash 6 times with 60 mL DMF solution, and dry for later use.

[0050] Step S12: Take Fmoc-L-Val-OH (8.1g, 15mmol) and HOBt (3.9g, 15mmol) in a 100mL beaker, cool to 2-8℃, add 25mL of DMF solution and DIC (4.5mL, 15mmol), let stand for 10-20min, and add the solution from the 100mL beaker to a 100mL solid-phase synthesis reactor. Stir and react for 1.5h. After the reaction is complete, wash the resin three times with 60mL of DMF solution each time. After washing, add 60mL of 20% Pip / DMF solution, stir and react for 30min, filter to remove the deprotection solution, and then wash 6 times with 60mL of DMF solution. Dry and set aside for later use.

[0051] Step S13: Take Fmoc-L-Pro-OH (8.1g, 15mmol) and HOBt (3.9g, 15mmol) in a 100mL beaker, cool to 2-8℃, add 25mL of DMF solution and DIC (4.5mL, 15mmol), let stand for 10-20min, and add the solution from the 100mL beaker to a 100mL solid-phase synthesis reactor. Stir and react for 1.5h. After the reaction is complete, wash the resin three times with 60mL of DMF solution each time. After washing, add 60mL of 20% Pip / DMF solution, stir and react for 30min, filter to remove the deprotection solution, and then wash 6 times with 60mL of DMF solution. Dry and set aside for later use.

[0052] Step S14: Take Fmoc-L-Tyr(OtBu)-OH (11.0 g, 15 mmol) and HOBt (3.9 g, 15 mmol) in a 100 mL beaker, cool to 2-8 °C, add 25 mL of DMF solution and 4.5 mL of DIC (15 mmol), and let stand for 10-20 min. Then add the solution from the 100 mL beaker to a 100 mL solid-phase synthesis reactor and stir for 1.5 h. After the reaction is complete, wash the resin three times with 60 mL of DMF solution each time. After washing, add 60 mL of 20% Pip / DMF solution and stir for 30 min. Filter to remove the deprotection solution, then wash six times with 60 mL of DMF solution, twice with 60 mL of methanol, twice with 60 mL of DCM solution, and twice with 60 mL of methanol. Dry under vacuum to obtain the peptide resin of H-Tyr(OtBu)-Pro-Val-Pro-CTC resin.

[0053] Step S2: Add the peptide resin of H-Tyr(OtBu)-Pro-Val-Pro-CTC resin to 200 mL of 1% TFA / DCM solution, stir and react at 30°C for 30 minutes, filter to remove the resin, and obtain the filtrate. Dry the filtrate to obtain the fully protected peptide H-Tyr(OtBu)-Pro-Val-Pro-OH.

[0054] Step S3: Dissolve the fully protected peptide H-Tyr(OtBu)-Pro-Val-Pro-OH in 1.0 L of DMF, add DIC (3.8 mL, 10 mmol), HOBt (3.2 g, 10 mmol), and DIEA (6.9 mL, 10 mmol), and stir at 30 °C for 12-16 hours to form Cyclo(Tyr(OtBu)-Pro-Val-Pro).

[0055] Step S4: Deprotect the Cyclo(Tyr(OtBu)-Pro-Val-Pro) solid with TFA / TIS / H2O = 90 / 5 / 5 (50 mL) for 2.5 hours. Add the resulting reaction solution to 500 mL of tert-butyl methyl ether (2-8 °C) solution, and a white solid will precipitate. Centrifuge to obtain a white solid crude peptide. Dry the white solid crude peptide under vacuum to obtain crude peptide powder Cyclo(Tyr-Pro-Val-Pro).

[0056] Step S5: The crude peptide powder Cyclo(Tyr-Pro-Val-Pro) was purified by reverse-phase C18 preparative chromatography and lyophilized to obtain the prepared cyclic tetrapeptide compound 1: Cyclo(Tyr-Pro-Val-Pro).

[0057] 1 H NMR(500MHz,MeOD)δ7.80(d,J=9.9Hz,1H),7.42(s,2H),7.02(dt,J=8.6,1.1H z,2H),6.82–6.71(m,2H),4.88-4.76(m,1H),4.35(dd,J=9.9,6.8Hz,1H),4.13 –3.98(m,2H),3.67-3.36(m,4H),2.86(ddt,J=13.9,6.8,1.0Hz,1H),2.80–2. 70(m,1H),2.34–2.16(m,1H),1.99-1.72(m,8H),0.91(dd,J=17.0,7.0Hz,6H).

[0058] Cytotoxicity assay:

[0059] NIH / 3T3 cells were used at a rate of 1×10 4Cells were cultured at a density of 96 wells in 96-well cell culture plates and incubated at 37°C in a 5% CO2 incubator. After 24 hours, the culture medium was discarded, and the cells were washed once with 1×PBS. Then, different concentrations of cyclic tetrapeptides were added for bioactive substance treatment. After 48 hours of treatment, the culture medium was removed, and 100 μL of medium containing 10% CCK-8 solution was added. The plates were incubated for 1 hour, and the absorbance at 450 nm was measured using a microplate reader. A control group without the sample was used. Cell viability was calculated using the following formula: Cell viability % = (Experimental group absorbance / Control group absorbance) × 100%.

[0060] The results of the effect of cyclic tetrapeptide on NIH / 3T3 cells are shown in Figure 2 ,from Figure 2 It can be seen that the experimental groups (10, 100 and 1000 μg / mL) of cyclic tetrapeptide had no significant cytotoxicity to NIH / 3T3 cells.

[0061] The soothing effects of cyclic tetrapeptide:

[0062] Detection reagent: Mouse interleukin-6 (IL-6) enzyme-linked immunosorbent assay kit (Catalog No.: E-EL-M0044, Elabscience, China);

[0063] Detection method: Mouse macrophages (RAW264.7) were processed at a concentration of 1×10⁻⁶. 6 Cells were cultured at a density of 6 wells in 12-well plates and incubated at 37°C in a 5% CO2 incubator. After 24 hours, the culture medium was discarded, and dexamethasone (DEX) and cyclic tetrapeptide (1000 μg / mL) were added for pre-incubation for 1.5 hours. Lipopolysaccharides (LPS) were then added for pre-incubation at a final concentration of 1 μg / mL. Normal control and experimental groups were established, with three biological replicates for each group. Cells were incubated for another 24 hours. The cell supernatant was then aspirated, centrifuged at 1000g, 4°C for 20 minutes, and the supernatant was collected and the precipitate discarded. Subsequent procedures were performed according to the IL-6 ELISA kit instructions.

[0064] The expression levels of inflammatory factors in the cyclic tetrapeptide experimental group are shown below. Figure 3 As can be seen, the expression level of IL-6 was significantly reduced after treatment with cyclic tetrapeptide, which indicates that cyclic tetrapeptide can inhibit the secretion of inflammatory factors and has anti-inflammatory and soothing effects.

[0065] Antioxidant effects of cyclic tetrapeptide:

[0066] Test reagents: 1,1-Diphenyl-2-trinitrophenylhydrazine (DPPH) (Catalog No.: D4313, TCI (Shanghai) Chemical Industry Development Co., Ltd.); 2,2-Aza-bis(3-ethyl-benzothiazole-6-sulfonic acid) diammonium salt (ABTS) (Catalog No.: A1888-1G Sigma-Aldrich); 3-O-2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxo (PTIO) (Catalog No.: P160514-1g, Shanghai Aladdin Biochemical Technology Co., Ltd.)

[0067] Detection method:

[0068] The ABTS method was used to determine the free radical scavenging activity of samples: ABTS reacts with potassium persulfate (K2S2O8) to generate green ABTS free radicals, which have a maximum absorption peak at 420 nm. The free radical scavenger reacts with the ABTS free radicals, causing the reaction system to decolorize and the absorbance to decrease. The intensity of the ABTS solution decolorization is positively correlated with the antioxidant capacity of the free radical scavenger. Therefore, the absorbance is measured using a microplate reader to indicate the ability of the analyte to scavenge ABTS free radicals.

[0069] Preparation of K2S2O8 stock solution: Take 1.3 mg of K2S2O8 and add 2 mL of distilled water;

[0070] Preparation of ABTS stock solution: 3.8 mg ABTS, add 0.989 mL distilled water;

[0071] Preparation of ABTS working solution: Take 0.2 mL each of K2S2O8 stock solution and ABTS stock solution and react at room temperature in the dark for 12-16 h. Before use, dilute with distilled water to prepare ABTS working solution by a 20-fold dilution.

[0072] Sample preparation and positive test: The positive test uses 10000 μg / mL of vitamin C, and the sample is prepared at 10000 μg / mL as needed;

[0073] Add 140 μL each of ABTS solution and sample solution to a 96-well plate and react in the dark for 5 min; measure the absorbance at 420 nm.

[0074] The free radical scavenging activity of samples was determined using the DPPH method. DPPH is a stable nitrogen-centered free radical; its ethanol solution is purple, with a maximum absorption wavelength of 517 nm. When a free radical scavenger is added to the DPPH solution, its lone pair electrons are paired, resulting in decreased absorption, a lighter solution color (pale yellow), and a decrease in absorbance at 517 nm. The degree of change is linearly related to the degree of free radical scavenging; a higher scavenging rate indicates a stronger scavenging ability.

[0075] Preparation of DPPH solution: Accurately weigh 3 mg of DPPH and dissolve it in 25 mL of 95% ethanol solution;

[0076] Sample preparation and positive test: The positive test uses 10000 μg / mL of vitamin C, and the sample is prepared at 10000 μg / mL as needed;

[0077] Sample loading reaction: 140 μL each of DPPH solution and sample solution were added to a 96-well plate and reacted in the dark for 30 min; absorbance was measured at 517 nm.

[0078] The PTIO method was used to determine the free radical scavenging activity of the samples. PTIO is a charged oxygen free radical; its aqueous solution is deep purple with a maximum absorption peak at 557 nm. Free radical scavengers react with PTIO free radicals, causing the reaction system to decolorize and the absorbance to decrease. The intensity of the PTIO solution decolorization is positively correlated with the antioxidant capacity of the free radical scavenger. Therefore, the absorbance was measured spectrophotometrically to represent the ability of the analyte to scavenge PTIO free radicals.

[0079] PTIO solution preparation: Dissolve 5.625 mg of PTIO in 25 mL of distilled water;

[0080] Sample preparation and positive test: The positive test uses 10000 μg / mL of vitamin C, and the sample is prepared at 10000 μg / mL as needed;

[0081] Sample loading reaction: 140 μL each of PTIO solution and sample solution were added to a 96-well plate and reacted in the dark for 4 h; absorbance was detected at 557 nm.

[0082] The free radical scavenging rate of the cyclic tetrapeptide experimental group is shown below. Figure 4 It can be seen that the DPPH, ABTS and PTIO free radicals were reduced after treatment with cyclic tetrapeptide, which indicates that cyclic tetrapeptide can scavenge free radicals and has antioxidant effects.

[0083] The above experimental results show that the cyclic tetrapeptide provided by the present invention can not only inhibit the release of the inflammatory factor IL-6, but also effectively scavenge reactive oxygen species DPPH, ABTS and PTIO, effectively inhibit the production of reactive oxygen species, relieve skin inflammation and improve skin condition.

[0084] The above description of the embodiments is only for the purpose of helping to understand the method and core ideas of the present invention. It should be noted that those skilled in the art can make several improvements and modifications to the present invention without departing from the principles of the present invention, and these improvements and modifications also fall within the protection scope of the claims of the present invention.

Claims

1. A cyclic tetrapeptide compound of general formula I, or its stereoisomer or salt thereof: c(AA1-AA2-AA3-AA4), formula I; In Formula I, AA1-AA2-AA3-AA4 is -Pro-Val-Pro-Tyr-, -Val-Pro-Tyr-Pro-, -Pro-Tyr-Pro-Val-, or -Tyr-Pro-Val-Pro-.

2. The cyclic tetrapeptide compound according to claim 1, characterized in that, It has the following structure:

3. A method for preparing the cyclic tetrapeptide compound according to any one of claims 1 to 2, comprising the following steps: S1) CTC resin is reacted with an amino acid reagent protected by an Fmoc group to obtain a peptide resin of H-AA4-AA3-AA2-AA1-CTC resin. S2) Remove the resin from the peptide resin structure to obtain a fully protected polypeptide H-AA4-AA3-AA2-AA1-OH; S3) Cyclize the fully protected polypeptide H-AA4-AA3-AA2-AA1-OH to obtain the fully protected Cyclo(AA1-AA2-AA3-AA4); S4) After deprotection and purification of the fully protected Cyclo(AA1-AA2-AA3-AA4), the cyclic tetrapeptide Cyclo(AA1-AA2-AA3-AA4) is obtained; The AA1-AA2-AA3-AA4 are -Pro-Val-Pro-Tyr-, -Val-Pro-Tyr-Pro-, -Pro-Tyr-Pro-Val-, or -Tyr-Pro-Val-Pro-.

4. The preparation method according to claim 3, characterized in that, The cyclization in step S3) is performed in the presence of DIC, HOBt, and DIEA.

5. The preparation method according to claim 3, characterized in that, The cyclization temperature in step S3) is 20–40°C; the cyclization time is 2–24 h.

6. The preparation method according to claim 3, characterized in that, The deprotection process in step S4) is performed in the presence of TFA and TIS; the deprotection time is 1-5 hours.

7. A composition comprising the cyclic tetrapeptide compound of any one of claims 1 to 2, or a stereoisomer thereof or a salt thereof, and an excipient.

8. The use of the cyclic tetrapeptide compound of any one of claims 1 to 2, or its stereoisomer or salt thereof, or the composition of claim 7, in the preparation of products having anti-inflammatory, repairing, antioxidant, anti-allergic and / or anti-aging functions.

9. The application according to claim 8, characterized in that, The products include pharmaceutical compositions, cosmetic compositions, and health products.

10. The use of the cyclic tetrapeptide compound of any one of claims 1 to 2, or its stereoisomer or salt thereof, or the composition of claim 7, in the preparation of a cosmetic composition, pharmaceutical composition or health product for the prevention, treatment and / or relief of skin inflammation.

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