Cyclopeptide compound with anti-inflammatory effect as well as preparation method and application thereof

Abstract

The invention relates to a cyclic peptide compound with an anti-inflammatory effect and a preparation method and application thereof.The preparation method comprises the following steps that dichloro resin is selected as load resin, an Fmoc solid-phase synthesis strategy is adopted, condensation, Fmoc protecting group removal, washing and drying treatment are repeated, and Met-Leu-Pro-Ile-Pro-Gln (Trt)-Thr (tBu)-Gly-resin with exposed alpha-amino is obtained; performing solid-phase cyclization on the polypeptide crude product to obtain a reacted mixture; adding hydrochloric acid, stirring, and drying under reduced pressure to obtain yellow oily matter; adding a cutting reagent, filtering, purifying and freeze-drying to obtain the cyclopeptide compound with the anti-inflammatory effect. The cyclopeptide compound contained in the annona squamosa fruit is prepared by adopting a method which is simple to operate, high in extraction yield and high in product purity, and is applied to cosmetics.

Description

Technical Field

[0001] The present invention belongs to the technical field of cosmetics, and more specifically, relates to a cyclic peptide compound with anti-inflammatory effect and a preparation method and application thereof. Background Art

[0002] Climate, environmental factors and other irritants have a significant impact on the occurrence of sensitive skin and skin inflammation. The above-mentioned other irritants include, for example, pollen, dust mites, pet dander or certain chemicals. In order to reduce the effects of the aforementioned factors on skin inflammation and allergic reactions, existing related research is mostly centered on adding anti-inflammatory raw materials to cosmetics. For example, Chinese patent publication CN112912063A provides an extract of Eucommia bark, which can inhibit the expression of PGE2 synthase protein increased by heat treatment and has anti-inflammatory effects; Chinese patent CN115089521B provides a soothing anti-inflammatory composition including sodium carboxymethyl β-glucan, purslane extract, Centella asiatica extract, sea fennel extract and panthenol, which can relieve skin sensitivity from multiple dimensions; Chinese patent publication CN117919143A provides a soothing anti-inflammatory composition, which includes rosemary leaf extract, Centella asiatica extract, Glycyrrhiza glabra extract and Sophora flavescens root extract, which has the effects of soothing and anti-inflammatory, repairing skin, soothing and removing redness. However, some plant extracts may affect the product's smell, color, skin feel, etc.

[0003] Annona cherimola is a plant belonging to the genus Annona in the family Annonaceae of the order Magnoliales. Its fruit, Annona cherimola Miller, contains cyclic peptide compounds that can downregulate histamine, TNF-α and substance P, reduce the expression of IL-31 receptors, and thus reduce skin sensitivity and alleviate inflammatory itching symptoms. However, due to the extremely low content of cyclic peptide compounds in Annona cherimola, extraction and separation are difficult. Therefore, it is very difficult and inefficient to extract cyclic peptide compounds from Annona cherimola by traditional separation processes.

[0004] Based on this, there is an urgent need to propose a cyclic peptide compound with anti-inflammatory effect and its preparation method and application, so as to solve the technical problems of extremely low content of cyclic peptide compounds contained in cherimoya fruit and high difficulty in extraction and separation through chemical synthesis. Summary of the invention

[0005] In view of the shortcomings of the prior art, the main purpose of the present invention is to propose a cyclic peptide compound with anti-inflammatory effect and its preparation method and application, and to solve the technical problem that the content of cyclic peptide compounds in cherimoya fruit is extremely low, the extraction and separation are difficult, and the extraction of cyclic peptide compounds in cherimoya fruit by traditional separation process is very difficult and the efficiency is extremely low through chemical synthesis.

[0006] To achieve this object, the present invention adopts the following technical solutions:

[0007] In a first aspect, the present invention provides a cyclic peptide compound having an anti-inflammatory effect, wherein the cyclic peptide compound has a structure shown in formula (I):

[0008]

[0009] In a second aspect, the present invention provides a method for preparing a cyclic peptide compound having an anti-inflammatory effect, the preparation method comprising the following steps:

[0010] Step S1: select dichloro resin as the loaded resin, provide an activated Fmoc-Gly-OH solution, adopt the Fmoc solid phase synthesis strategy, condense to prepare Fmoc-Gly-resin, remove the Fmoc protecting group, and obtain Gly-resin with the α-amino group exposed;

[0011] Step S2: the Gly-resin is sequentially subjected to condensation and Fmoc-protecting group removal operations with activated Fmoc-Thr(tBu)-OH solution, Fmoc-Gln(Trt)-OH solution, Fmoc-Pro-OH solution, Fmoc-Ile-OH solution, Fmoc-Pro-OH solution, Fmoc-Leu-OH solution, and Fmoc-Met-OH solution according to the Fmoc solid phase synthesis strategy, and after the condensation and Fmoc protecting group removal operations are all completed, the resin is washed with DMF and methanol in sequence, and dried after washing to obtain Met-Leu-Pro-Ile-Pro-Gln(Trt)-Thr(tBu)-Gly-resin with an exposed α-amino group;

[0012] Step S3: Stir and swell the Met-Leu-Pro-Ile-Pro-Gln(Trt)-Thr(tBu)-Gly-resin with the α-amino group exposed in a TFA-DCM solution, filter and collect the solvent to obtain a crude polypeptide;

[0013] Step S4: adding a coupling system formed by DIPEA, TBTU and HOBT to the crude polypeptide, stirring the reaction until the crude polypeptide completes solid phase cyclization to obtain a reaction mixture;

[0014] Step S5: adding hydrochloric acid to the reaction mixture to adjust the pH value to 6 to 7, stirring and collecting the organic phase, and drying under reduced pressure to obtain a yellow oil;

[0015] Step S6: slowly add the yellow oil into TFA / EDT / H2O / TIPS cutting reagent precooled to 0°C to form a mixed solution, and then slowly add the mixed solution into MTBE solution to precipitate a white solid, which is filtered, purified by reverse phase HPLC, and freeze-dried to obtain the cyclic peptide compound with anti-inflammatory effect.

[0016] Preferably, in step S1, the activated Fmoc-Gly-OH solution is obtained by activating Fmoc-Gly-OH with an activator, and the activator is DIPEA (N,N-diisopropylethylamine).

[0017] It should be noted that Fmoc-Gly-OH needs to be activated by DIPEA in order to react with the chloromethyl functional groups on the dichlororesin.

[0018] Preferably, in step S2, the sequential washing with DMF and methanol includes: washing the resin with DMF 5 times, and then washing the resin with methanol 3 times; the drying treatment includes vacuum drying. Among them, washing the resin with DMF (dimethylformamide) 5 times can remove the reactants, by-products and excess Fmoc reagents that may remain on the surface and pores of the resin; since methanol is a strong polar solvent, washing the resin with methanol 3 times can fully remove the residual DMF and other polar impurities on the loaded resin.

[0019] Preferably, in step S3, the stirring and swelling time is 10 min, the volume percentage concentration of TFA in the TFA-containing DCM solution is 1%, and the stirring and swelling, filtering and solvent collection operations are repeated 3 times.

[0020] Preferably, in step S4, the stirring reaction is carried out under ice bath conditions, and the stirring reaction time is 4 hours.

[0021] It should be noted that in the coupling system formed by DIPEA (N, N-diisopropylethylamine), TBTU (2,4,6-tribromophenyl carbonate) and HOBT (1-hydroxybenzotriazole) in step S4: DIPEA is an organic base used to deprotonate the carboxylic acid component to generate a carboxylate, thereby promoting the coupling reaction between the carboxylic acid and the isocyanate or activated carboxylic acid; TBTU is a peptide coupling reagent that can react with an amine to generate an active intermediate, which can react with another carboxylic acid to form a peptide bond; HOBT is an additive that can react with a carboxylic acid and an amine to generate an active ester to promote the coupling reaction. In addition, the reaction system is placed in an ice bath to control the reaction temperature, which helps to slow down the reaction rate, reduce side reactions, and improve the reaction selectivity.

[0022] It should be noted that, in step S4, the completion of the solid phase cyclization of the crude polypeptide can be monitored by LCMS (Liquid Chromatography-Mass Spectrometry) detection means.

[0023] Preferably, in step S5, the concentration of the hydrochloric acid is 1N HCl / H2O, and the stirring time is 0.5h. The 1N HCl / H2O means that the hydrochloric acid solution has a 1 equivalent concentration, which is mainly used to remove some alkaline substances, such as DIPEA; it can also quench the reaction and no longer proceed.

[0024] Preferably, in step S6, the yellow oil is slowly added to TFA / EDT / H2O / TIPS cutting reagent precooled to 0°C to form a mixed solution, and stirred for 2 hours.

[0025] It should be noted that the yellow oil is slowly added to a TFA / EDT / H2O / TIPS (triisopropylsilane) cutting reagent precooled to 0°C to form a mixed solution, and then the mixed solution is slowly added to a precooled MTBE (methyl tert-butyl ether) solution, which can control the reaction rate and reduce side reactions.

[0026] In a third aspect, the present invention provides an application of a cyclic peptide compound with anti-inflammatory effect in cosmetics.

[0027] Preferably, the mass percentage of the cyclic peptide compound in the cosmetics ranges from 0.008% to 0.016%.

[0028] Preferably, the type of the cosmetic is selected from any one of lotion, cream, gel, water solution and facial mask.

[0029] Compared with the prior art, the present invention has at least the following beneficial effects:

[0030] (1) The present invention provides a method for preparing a cyclic peptide compound with anti-inflammatory effect, which is simple to operate, has a high extraction yield and a high product purity, and realizes the industrial batch synthesis of cyclic peptide compounds that are the same as the cyclic peptide compounds contained in the custard apple fruit, thereby avoiding the problem that the cyclic peptide compounds contained in the traditional custard apple fruit are difficult to be utilized due to the extremely low content of the cyclic peptide compounds contained in the fruit and the high difficulty in direct extraction and separation.

[0031] (2) The cyclic peptide compound prepared by the method for preparing a cyclic peptide compound with anti-inflammatory effect provided by the present invention not only has good skin permeability, but also has anti-inflammatory activity, can be applied in the field of cosmetics, and has great application prospects and commercial value. BRIEF DESCRIPTION OF THE DRAWINGS

[0032] Figure 1 The synthetic route of the cyclic peptide compound with anti-inflammatory activity in one embodiment of the present application is shown;

[0033] Figure 2a-2b The figure shows the characterization of the two-dimensional nuclear magnetic resonance spectrum of the cyclic peptide compound with anti-inflammatory activity in one embodiment of the present application;

[0034] Figure 3a-3b The anti-inflammatory experiment results of cyclic peptide compounds in zebrafish are shown;

[0035] Figure 4 The results of the cell anti-inflammatory test of cyclic peptide compounds are shown. DETAILED DESCRIPTION

[0036] The technical solution of the present invention is further described below in conjunction with the accompanying drawings and through specific implementation methods. However, the following examples are only simplified examples of the present invention and do not represent or limit the scope of protection of the present invention. The scope of protection of the present invention shall be subject to the claims.

[0037] Example 1

[0038] See also Figure 1 , a method for preparing a cyclic peptide compound with anti-inflammatory effect in this embodiment, the preparation method comprises the following steps:

[0039] Step S1: Take 1 mol of dichlororesin (loading amount: 0.56 mol / kg) as the loaded resin, stir the dichlororesin in 6.5 L of DCM (dichloromethane) for 30 min, add 774 g, 6 mol of DIPEA (diisopropylethylamine) and 891.2 g, 3 mol of Fmoc-Gly-OH for condensation reaction, and stir at room temperature for 2.5 h; add 650 ml of MeOH (methanol) and stir for 0.5 h; wash the loaded resin with 6.5 L of DMF (N, N-dimethylformamide) 3 times; add 6.5 L of DMF containing 20% ​​piperidine to the loaded resin, react at room temperature for 20 min, wash 5 times with 6.5 L of DMF to remove the Fmoc protecting group, and obtain a Gly-resin with an exposed α-amino group;

[0040] Step S2: 658.8 g, 5.4 mol, of DIC (1,3-diisopropylcarbodiimide), 729.1 g, 5.4 mol, of HOBT (1-hydroxybenzotriazole), and 1.2 kg, 3 mol, of Fmoc-Thr(tBu)-OH were mixed in 6.5 L of DMF, and the mixture was added to a loaded resin for condensation reaction, and stirred at 0°C to room temperature for about 2 h, and then 20% piperidine was added, and stirred at room temperature for 20 min, and the loaded resin was washed 5 times with 6.5 L of DMF to remove the Fmoc protecting group, thereby obtaining a Thr(tBu)-Gly-resin with an exposed α-amino group;

[0041] The above condensation and removal of Fmoc protecting group steps were repeated in sequence with the following amino acids, the following amino acids included: Fmoc-Gln(Trt)-OH (1.83kg, 3mol), Fmoc-Pro-OH (1.01kg, 3mol), Fmoc-Ile-OH (1.06kg, 3mol), Fmoc-Pro-OH (1.01kg, 3mol), Fmoc-Leu-OH (1.06kg, 3mol) and Fmoc-Met-OH (1.11kg, 3mol); after the entire sequence coupling was completed, the loaded resin was washed 5 times with 6.5L of DMF and then washed 3 times with 10L of MeOH, and the resin was dried by vacuum drying to obtain 1.8kg of yellow solid loaded resin;

[0042] Step S3: 1.8 kg of yellow solid loaded resin was swelled in 10 L of 1% TFA / DCM, stirred for 10 min, the solvent was collected by filtration, and 10 L of 1% TFA / DCM was added and the above steps were repeated 3 times to obtain a crude polypeptide;

[0043] Step S4: DIPEA (387.2 g, 3 mol), TBTU (641.0 g, 2 mol) and HOBT (270.0 g, 2 mol) were added to the above 1000 L DCM solution under ice bath conditions, and stirred for 4 h until the solid phase cyclization of the crude product was completed to obtain a reaction mixture;

[0044] Step S5: adding 1N, 50L hydrochloric acid to the reaction mixture until the pH value is in the range of 6-7, stirring for 0.5h, collecting the organic phase, and drying under reduced pressure to obtain 0.98kg of yellow oil;

[0045] Step S6: Slowly add the 0.98 kg yellow oil to the TFA / EDT / H2O / TIPS cutting reagent at 0°C to form a mixed solution, and stir for 2 hours. The volume percentage concentration of TFA in the TFA / EDT / H2O / TIPS system is 92.5%. Then slowly add the mixed solution to the pre-cooled MTBE (methyl tert-butyl ether) solution (70L) until the white solid is completely precipitated, and filter to obtain 480 g of crude white solid, which is purified by reverse phase HPLC and freeze-dried to finally obtain the cyclic peptide compound with anti-inflammatory effect.

[0046] Table 1. Cyclic peptide A and cyclic peptide compounds from Annona chebula 13 C and 1 H NMR data

[0047]

[0048]

[0049]

[0050] Table 1 The cyclic peptide A of Annona chebula 13 C and 1 H NMR data from the literature: Tetrahedron 60 (2004) 405–414; 13 C and 1 The H NMR data is the result of the analysis of the two-dimensional NMR spectrum of the sample (cyclopeptide compound), the solvent is deuterated DMSO, and the NMR spectrum is as follows Figure 2a-2b As shown in Table 1, the structure of the cyclic peptide compound prepared by the preparation method of the cyclic peptide compound described in Example 1 is the same as the structure of the cyclic peptide A of the Annona chebula recorded in the existing literature, indicating that the present application has achieved the industrialized batch synthesis of the cyclic peptide compound identical to the cyclic peptide compound contained in the Annona chebula fruit, avoiding the problem that the cyclic peptide compound in the traditional Annona chebula fruit is difficult to be utilized due to the extremely low content of the cyclic peptide compound contained in the fruit and the high difficulty of direct extraction and separation.

[0051] Test Example 1

[0052] Zebrafish anti-inflammatory experiment

[0053] Neutrophil red fluorescence was used to label zebrafish Tg (mpx:dsRED). Zebrafish were reared according to "The zebrafish book". The water temperature was kept at about 28.5°C, with 14 hours of light and 10 hours of darkness per day, and feeding was done once in the morning and evening. The night before embryo collection, one female and two male fish were placed in an spawning bar, separated by a partition and placed in a dark environment. The next morning, the partition was removed after the lights were turned on, and the embryos were collected after spawning was completed. The embryos were placed in egg water and cultured in a light incubator at 28.5°C.

[0054] On the day of embryo collection, about 7-8 hpf, the embryos were thoroughly cleaned by changing the liquid, and the embryos in poor condition were removed. Fresh egg water was replaced and cultured in a 28.5℃ incubator until 3 dpf (poor embryos were picked out in time during the culture period, and fresh egg water was replaced every day). The 3 dpf zebrafish were randomly divided into groups, with 15 in each group: a. Normal control group: containing zebrafish and standard dilution water. b. Model control group: containing zebrafish and 1 μM copper sulfate solution. c. Positive control group: containing zebrafish, 1 μM copper sulfate solution and positive drug (5 μg / mL dexamethasone was used as the positive drug in this experiment). d. Test group: containing zebrafish, 1 μM copper sulfate solution and test substance (100 μg / mL cyclic peptide compound).

[0055] According to the experimental requirements, a sufficient number of 72hpf zebrafish with consistent developmental conditions were pre-screened, and the zebrafish were randomly assigned to six-well plates, with 15 per well. The standard dilution water in the 6-well plate was removed without harming the embryos, and 3mL of the test solution was quickly added to each well. After thorough mixing, the culture plate panel was covered and wrapped with aluminum foil, and incubated in a 28°C biochemical incubator in the dark for 2 hours. After the incubation, zebrafish were randomly selected from zebrafish with normal phenotypes and behaviors, fixed with 3% methylcellulose, observed and photographed under a stereofluorescence microscope, and all zebrafish photography results must be completed under the same instrument and environmental conditions, and the body position of the zebrafish should be consistent.

[0056] Table 2. Experimental results of zebrafish anti-inflammatory model

[0057] Group concentration Anti-inflammatory effect (%) Significant difference Dexamethasone 5 μg / mL 56.18 *** Cyclic peptide compounds 100 μg / mL 99.82 ***

[0058] Zebrafish is an emerging experimental animal model for high-throughput screening. The location of zebrafish neuromasts is relatively fixed, generally distributed along the lateral line corresponding to different myometriums. When copper sulfate induces inflammation, neutrophils normally located in the hematopoietic tissue and posterior blood island of the zebrafish tail will migrate, and a large number of neutrophils will accumulate at the location of the damaged lateral line neuromasts of zebrafish, such as Figure 3a-3b As shown, after treatment with the cyclic peptide compound, the migration of neutrophils to the neuromast cell area of ​​the line can be inhibited, indicating that the cyclic peptide compound is an anti-inflammatory active substance.

[0059] Test Example 2

[0060] Cell Anti-Inflammation Test

[0061] HaCaT cells were grown at 5×10 5 Each well was inoculated on a six-well plate and cultured at 37°C and 5% CO2. After the cells adhered to the wall, they were washed with PBS and 0, 4, 8, and 16 μg / mL of the cyclic peptide compound were added. 2 After irradiation (4min), add 200μL of lysis solution to each well, shake gently until the lysis solution covers the bottom of the well, and lyse on ice for 20 minutes, shaking several times during the period. Scrape the cells with a scraper, collect them in a 1.5mL EP tube, centrifuge at 4℃, 12000rpm for 30 minutes, take the supernatant and store it at -80℃ for testing. Elisa enzyme-linked immunosorbent assay kit was used to detect the content of IL-1β and IL-6.

[0062] The results are as follows Figure 4 As shown, UVB irradiation can induce an increase in the IL-1β and IL-6 levels in HaCaT cells. The cyclic peptide compounds at concentrations of 4, 8, and 16 μg / mL can significantly reduce the IL-1β content in the model group, and the cyclic peptide compounds at concentrations of 8 and 16 μg / mL can significantly reduce the IL-6 content in the model group, indicating that the cyclic peptide compounds have a certain anti-inflammatory effect.

[0063] Test Example 3

[0064] Skin penetration test

[0065] The tape tearing method was used to collect and test the content of cyclic peptide compounds in the superficial epidermis of the skin. A 3.8 cm piece of the inner forearm of a healthy subject was selected. 2 The undamaged and smooth skin of different sizes was used as the test area and marked. 20 μL of 50 mg / mL cyclopeptide compound solution was applied to this area and absorbed with a clean fingertip. After 2 hours of drug administration and absorption, the surface residue was rinsed with mild running water and gently wiped dry. The drug administration area was continuously taped with 10 layers, and the tape pressure was applied with an average of 225 g / cm 2, collect each layer of tape in a centrifuge tube, use methanol as the extract, and use LC-MS to test the retention of the cyclic peptide compound in each layer of the superficial epidermis of the human body, and calculate the retention per unit area of ​​the epidermis. As shown in Table 3, the experimental results show that at 2 hours, the cyclic peptide compound can penetrate into the epidermis of the skin and has a certain retention effect.

[0066] Table 3. Skin permeation results of cyclic peptide compounds

[0067] Subject number <![CDATA[Amount retained in the epidermis per unit area (ng / cm 2 )]]> 1 759.62 2 1507.89 3 681.71

[0068] Application Example 1

[0069] Application of cyclic peptide compounds in creams

[0070] Table 4. A cream formula containing a cyclic peptide compound

[0071]

[0072] Preparation method: Prepare according to the formula ratio shown in Table 4, and make up to 100% with deionized water. The preparation amount of formula 1 is 200g. Premix the phase B raw materials in the formula and add them to the water phase pot, stir at low speed for 5-10 minutes until completely uniform, and keep warm at 75-85℃ for 20 minutes; dissolve the phase A raw materials in the oil phase pot at 80-85℃ and keep warm for use. Transfer the phase B raw materials to the emulsification pot, heat to 75-85℃, stir and homogenize at medium speed for 10 minutes until completely dispersed and uniform, vacuum the emulsification pot while stirring, slowly draw in phase A, stir at medium and high speed for 5-10 minutes, homogenize for 3-8 minutes, continue stirring and cool to 75℃ to add phase C raw materials. Continue to cool to below 45℃ and add phase D raw materials in sequence. After the physical and chemical indicators are tested to be qualified, filter out the material.

[0073] Application Example 2

[0074] Application of cyclic peptide compounds in emulsions

[0075] Table 5. A formula of an emulsion containing a cyclic peptide compound

[0076]

[0077] Preparation method: Formula 2 is prepared according to the formula ratio shown in Table 5, and the specific preparation process is the same as that of Formula 1.

[0078] Application Example 3

[0079] Application of cyclic peptide compounds in facial masks

[0080] Table 6. A facial mask formula containing a cyclic peptide compound

[0081]

[0082]

[0083] Preparation method: Prepare according to the formula ratio shown in Table 6, and make up to 100% with deionized water. The preparation amount of formula 3 is 200g. The preparation process is: add the phase A raw material in the formula to the water phase pot and fully hydrate it. Premix the phase B raw material and add it to the water phase pot, heat it to 75-85℃ and stir to dissolve it completely; cool it down and stir, add phase C at 75℃ and stir it completely. Add phase D raw material at 55℃ and stir it completely. Add phase E raw material in sequence below 45℃ and stir evenly. After the physical and chemical indicators are tested and qualified, filter out the material.

[0084] Stability test

[0085] The formulations of Application Examples 1-3 were subjected to stability tests, and the stability of the cyclic peptide compounds of the present invention was tested at -15°C, 25°C, 40°C, 49°C and light conditions for 30 days, 60 days, and 90 days, respectively. The stability test results are shown in Table 7.

[0086] Table 7. Stability test results of several formulations containing cyclic peptide compounds

[0087]

[0088]

[0089] It can be seen that the product stability obtained by applying the formulas corresponding to Application Examples 1-3 to creams, lotions and masks meets the standards.

[0090] The applicant declares that the above is only a specific implementation mode of the present invention, but the protection scope of the present invention is not limited thereto. Those skilled in the art should understand that any changes or substitutions that can be easily thought of by those skilled in the art within the technical scope disclosed by the present invention shall fall within the protection scope and disclosure scope of the present invention.

Claims

1. A cyclic peptide compound with anti-inflammatory effect, characterized in that: The cyclic peptide compound has a structure shown in formula (I):

2. A method for preparing a cyclic peptide compound with anti-inflammatory effect as claimed in claim 1, characterized in that: The preparation method comprises the following steps: Step S1: select dichloro resin as the loaded resin, provide an activated Fmoc-Gly-OH solution, adopt the Fmoc solid phase synthesis strategy, condense to prepare Fmoc-Gly-resin, remove the Fmoc protecting group, and obtain Gly-resin with the α-amino group exposed; Step S2: the Gly-resin is sequentially subjected to condensation and Fmoc-protecting group removal operations with activated Fmoc-Thr(tBu)-OH solution, Fmoc-Gln(Trt)-OH solution, Fmoc-Pro-OH solution, Fmoc-Ile-OH solution, Fmoc-Pro-OH solution, Fmoc-Leu-OH solution, and Fmoc-Met-OH solution according to the Fmoc solid phase synthesis strategy, and after the condensation and Fmoc protecting group removal operations are all completed, the resin is washed with DMF and methanol in sequence, and dried after washing to obtain Met-Leu-Pro-Ile-Pro-Gln(Trt)-Thr(tBu)-Gly-resin with an exposed α-amino group; Step S3: Stir and swell the Met-Leu-Pro-Ile-Pro-Gln(Trt)-Thr(tBu)-Gly-resin with the α-amino group exposed in a TFA-DCM solution, filter and collect the solvent to obtain a crude polypeptide; Step S4: adding a coupling system formed by DIPEA, TBTU and HOBT to the crude polypeptide, stirring the reaction until the crude polypeptide completes solid phase cyclization to obtain a reaction mixture; Step S5: adding hydrochloric acid to the reaction mixture to adjust the pH value to 6 to 7, stirring and collecting the organic phase, and drying under reduced pressure to obtain a yellow oil; Step S6: slowly add the yellow oil into TFA / EDT / H2O / TIPS cutting reagent precooled to 0°C to form a mixed solution, and then slowly add the mixed solution into MTBE solution to precipitate a white solid, which is filtered, purified by reverse phase HPLC, and freeze-dried to obtain the cyclic peptide compound with anti-inflammatory effect.

3. The preparation method according to claim 2, characterized in that: In the step S1, the activated Fmoc-Gly-OH solution is obtained by activating Fmoc-Gly-OH with an activator, and the activator is DIPEA.

4. The preparation method according to claim 2, characterized in that: In the step S3, the stirring and swelling time is 10 minutes.

5. The preparation method according to claim 2, characterized in that: In the step S4, the stirring reaction is carried out under ice bath conditions.

6. The preparation method according to claim 2, characterized in that: In step S5, the concentration of the hydrochloric acid is 1N HCl / H2O.

7. The preparation method according to claim 2, characterized in that: In the step S6, the mixed solution is slowly added into the pre-cooled MTBE solution.

8. Use of the cyclic peptide compound with anti-inflammatory effect as claimed in claim 1 in cosmetics.

9. The use of the cyclic peptide compound with anti-inflammatory effect in cosmetics according to claim 8, characterized in that: The mass percentage content of the cyclic peptide compound in cosmetics ranges from 0.008% to 0.016%.

10. The use of the cyclic peptide compound with anti-inflammatory effect in cosmetics according to claim 8, characterized in that: The type of the cosmetic is selected from any one of lotion, cream, gel, water solution and facial mask.

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