Bicyclic peptide compositions and uses thereof

Abstract

Disclosed are a bicyclic peptide composition and application thereof, and relate to the technical field of polypeptides, the ring peptide composition comprising component X and component Y, the component X being a ring hexapeptide-8, and the component Y being selected from one or more of the following ring peptides: a ring octapeptide-69, Cyclo-(Pro-Lys-Glu-Lys), Cyclo-(Val-Leu-Gln-Trp-Val-Lys). Specifically, the ring peptide composition and the use thereof in the preparation of cosmetics are disclosed.

Description

Technical Field

[0001] This disclosure relates to the field of peptide technology, and in particular to a bicyclic peptide composition and its applications. Background Technology

[0002] As people's living standards continue to improve and their pursuit of beauty intensifies, consumers' demand for cosmetics has gradually shifted from simple beauty and makeup to functional skincare, especially in areas such as exfoliation, skin repair, and anti-glycation. Developing safe, effective, and multi-functional skincare active ingredients has become a crucial issue in cosmetic research and development.

[0003] The stratum corneum, as the outermost barrier structure of the skin, normally sheds and renews itself naturally according to its cycle. However, influenced by factors such as age, ultraviolet radiation, and environmental pollution, the stratum corneum metabolism cycle is prolonged, leading to excessive accumulation of old keratinocytes and problems such as rough, dull skin and clogged pores. Currently used exfoliating ingredients such as glycolic acid and salicylic acid, while effective to some extent, are prone to causing skin irritation and sensitive reactions. Skin barrier repair is also a core issue in functional skincare. Over-cleansing, chemical irritation, and climate change can all damage the barrier, leading to increased transepidermal water loss, dryness, flaking, erythema, and itching. Existing repairing ingredients such as ceramides, hyaluronic acid, and panthenol each have their own focus, but a single ingredient often cannot meet the multiple repair needs of damaged skin. In addition, the impact of glycation on skin aging has received widespread attention in recent years. Reducing sugars undergo non-enzymatic reactions with collagen and elastin in the skin, generating irreversible advanced glycation end products (AGEs), leading to cross-linking and denaturation of collagen fibers, manifested as decreased skin elasticity, deeper wrinkles, and a dull complexion. Currently, there are still relatively few anti-glycation active ingredients that combine high efficacy and safety.

[0004] As a class of bioactive molecules, peptides possess advantages such as good biocompatibility, strong targeting, and well-defined activity, demonstrating broad application prospects in the cosmetics field. Cyclic peptides such as cyclic hexapeptide-8 have already received some research attention in skincare. Cyclic peptides with different chain lengths and amino acid sequences exhibit differences in bioactivity, and the efficacy of cyclic octapeptides and other short-chain cyclic peptides is also gradually gaining interest.

[0005] However, in practical applications, the efficacy of a single peptide ingredient is limited by factors such as concentration, permeability, and stability, making it difficult to fully realize its potential bioactivity. How to achieve synergistic effects between different cyclic peptide ingredients through rational combination design to meet consumers' multi-functional skincare needs is a direction that this field continues to explore. Summary of the Invention

[0006] This disclosure relates to a bicyclic peptide composition and its application, wherein the cyclic peptide composition has effects such as skin care or mucous membrane care.

[0007] On the one hand, the present disclosure provides a cyclic peptide composition, which comprises component X and component Y. Component X is cyclohexapeptide-8, and component Y is selected from one or more of the following cyclic peptides: cyclooctapeptide-69, Cyclo-(Pro-Lys-Glu-Lys), Cyclo-(Val-Leu-Gln-Trp-Val-Lys).

[0008] Cyclohexapeptide-8 is an active peptide raw material registered and filed by Shenzhen Vicky Technology Co., Ltd. with the National Medical Products Administration, and its filing number is National Cosmetic Raw Material Preparation No. 20250151, which is denoted as cyclic peptide A in the present disclosure.

[0009] Cyclooctapeptide-69 is an active peptide raw material registered and filed by Shenzhen Vicky Technology Co., Ltd. with the National Medical Products Administration, and its filing number is National Cosmetic Raw Material Preparation No. 20250125, which is denoted as cyclic peptide B in the present disclosure.

[0010] Cyclo-(Pro-Lys-Glu-Lys) has been publicly recorded in a Chinese patent application for invention (Publication No. CN118240006A), and its chemical structural formula is shown in Formula (I), which is denoted as cyclic peptide C in the present disclosure. In the present disclosure, cyclic peptide C can be prepared without doubt according to the method in the publicly available literature (such as the Chinese patent application for invention with Publication No. CN118240006A).

[0011] (I).

[0012] Cyclo-(Val-Leu-Gln-Trp-Val-Lys) has been publicly recorded in a Chinese patent (Publication No. CN120058859A), and its chemical structural formula is shown in Formula (II), which is denoted as cyclic peptide D in the present disclosure. In the present disclosure, cyclic peptide D can be prepared without doubt according to the method in the publicly available literature (such as the Chinese patent with Publication No. CN120058859A).

[0013] (II).

[0014] The inventors of the present disclosure surprisingly found that when cyclic peptide A is respectively compounded with cyclic peptide B, cyclic peptide C or cyclic peptide D, a synergistic effect can be produced, which can significantly remove the keratinocytes that fail to normally exfoliate on the skin surface, promote the expression of syndecan-1, and also inhibit the generation of advanced glycation end products, thereby increasing skin smoothness, repairing the skin barrier, enhancing the cohesion within the epidermis or the dermal-epidermal junction, reducing the damage to the skin caused by glycation reaction, improving skin dullness and / or brightening the skin tone. Therefore, when cyclic peptide A is respectively compounded with cyclic peptide B, cyclic peptide C or cyclic peptide D in component Y, a cyclic peptide composition product with functions such as exfoliation, repair and anti-glycation can be obtained.

[0015] In some embodiments, the concentration ratio of component X to component Y is (1~9):3.

[0016] In some embodiments, the concentration ratio of component X to component Y is 1:1, 2:1, 3:1, 1:2, or 1:3, respectively.

[0017] In another aspect of this disclosure, a cosmetic product is provided, comprising an effective amount of the above-described cyclic peptide composition, and at least one additional ingredient.

[0018] "Effective amount" means an amount of the cyclic peptide composition of this disclosure that is non-toxic but sufficient to provide the desired effect. The cyclic peptide composition of this disclosure is used in the cosmetics of this disclosure at an effective concentration to obtain the desired effect. In some embodiments, the concentration of the cyclic peptide composition is between 0.00000001% (by weight) and 20% (by weight) relative to the total weight of the cosmetic; in some embodiments, the concentration of the cyclic peptide composition is between 0.000001% (by weight) and 15% (by weight) relative to the total weight of the cosmetic; in some embodiments, the concentration of the cyclic peptide composition is between 0.0001% (by weight) and 10% (by weight) relative to the total weight of the cosmetic; in some embodiments, the concentration of the cyclic peptide composition is between 0.0001% (by weight) and 5% (by weight) relative to the total weight of the cosmetic.

[0019] In some embodiments, the dosage form of the cosmetic includes ointment, cream, emulsion, aqueous solution, oil, gel, powder, tablet, mud, patch, film, aerosol, spray, lyophilized preparation or nano-preparation.

[0020] Another aspect of this disclosure provides the use of the above-described cyclic peptide composition in the preparation of a composition for caring for skin or mucous membranes.

[0021] Another aspect of this disclosure provides the use of the above-described cyclic peptide composition in the preparation of compositions for exfoliation, repair, or anti-glycation.

[0022] In another aspect of this disclosure, there is provided the use of the above-described cyclic peptide composition in the preparation of a composition for removing keratinocytes that have failed to shed normally from the skin surface; or in the preparation of a composition for increasing skin smoothness; or in the preparation of a composition for repairing the skin barrier; or in the preparation of a composition for promoting the expression of multiligand proteoglycan-1; or in the preparation of a composition for enhancing epidermal cohesion or dermal-epidermal junction; or in the preparation of a composition for inhibiting the formation of advanced glycation end products; or in the preparation of a composition for improving dull skin and / or brightening skin tone.

[0023] Another aspect of this disclosure provides the use of the above-described cyclic peptide composition in the preparation of cosmetics.

[0024] Another aspect of this disclosure provides a cosmetic method for non-therapeutic purposes, comprising using the above-described cyclic peptide composition or the above-described cosmetic on the skin.

[0025] In this disclosure, the term "skin" should be understood as comprising its multiple layers, from the uppermost layer or stratum corneum to the lowermost layer or subcutaneous tissue, including both ends. These layers are composed of different types of cells, such as keratinocytes, fibroblasts, melanocytes, and / or adipocytes.

[0026] The term "skin care" refers to the maintenance and care of the skin to improve its condition, making it delicate, smooth, soft, and healthy.

[0027] The term "keratinocytes that fail to shed normally" refers to terminally differentiated keratinocytes in the stratum corneum of human epidermis that fail to shed in an orderly and physiological manner within the normal epidermal renewal cycle of healthy skin due to abnormal skin metabolism rate, impaired desmosome degradation, damaged barrier function, or the influence of internal and external factors. As a result, these keratinocytes become abnormally retained and accumulated on the skin surface and in the hair follicle infundibulum, leading to objectively verifiable changes in skin condition such as rough skin, blocked hair follicle openings, and thickened stratum corneum.

[0028] This disclosure has the following advantages and effects: 1. The cyclic peptide composition disclosed herein can effectively remove keratinocytes that have not shed normally from the skin surface, thereby achieving the effect of exfoliation and increasing skin smoothness.

[0029] 2. The cyclic peptide composition disclosed herein can effectively promote the expression of multiligand proteoglycan-1, thereby enhancing epidermal cohesion or dermal-epidermal junction, improving skin barrier function, and promoting skin regeneration and repair, thus having a repairing effect.

[0030] 3. The cyclic peptide composition disclosed herein can effectively inhibit the formation of advanced glycation end products, reduce the damage of glycation reaction to the skin, and help improve dull and sallow skin, brighten skin tone, delay skin aging, and has anti-aging and anti-glycation effects. Detailed Implementation

[0031] To make the objects, features, and advantages of this disclosure more apparent and understandable, the disclosure will be further described in detail below with reference to embodiments. Obviously, the described embodiments are only some, not all, of the embodiments of this disclosure. All other embodiments obtained by those skilled in the art based on the embodiments of this disclosure without inventive effort are within the scope of protection of the appended claims.

[0032] Unless otherwise specified, all experimental reagents and materials used in this disclosure are commercially available.

[0033] Cyclic peptide A and cyclic peptide B were purchased from Shenzhen Vikitech Co., Ltd.

[0034] The structure of Arenariphilin H is Cyclo-(Pro-Gly-Phe-Ser-Leu). In this paper, Arenariphilin H can be prepared without question according to methods known in the literature. Arenariphilin H can be prepared from plants using methods known in the literature of Jia AQ et al. (New cyclopeptides in Arenaria oreophila (Caryophyllaceae)[J]. Journal of Asian Natural Products Research. 9:6, 569-574). Arenaria oreophila It is obtained by extraction and separation. Alternatively, those skilled in the art can also obtain Ganoderma lucidum cyclic peptide H through conventional solid-phase synthesis methods. Ganoderma lucidum cyclic peptide H is referred to as cyclic peptide H in this disclosure.

[0035] The concentrations of each component in the composition of the embodiments of this disclosure are as follows: Note: " / " indicates that the substance is not present. When the concentration of the composition is 50 ppm, such as cyclic peptide A:cyclic peptide B = 1:1, it means that cyclic peptide A is 25 ppm and cyclic peptide B is 25 ppm.

[0036] Example 1: In vitro exfoliation test

[0037] 1.1 Reagents and Materials Bama fragrant pig skin, PBS, NaOH solution, HCl solution, and BCA protein quantification kit.

[0038] 1.2 Instruments Franz diffusion cell, magnetic stirrer, transdermal moisture loss analyzer, clean bench, and ELISA reader.

[0039] 1.3 Sample to be tested Experimental group: Cyclic peptide A, cyclic peptide B, cyclic peptide C, cyclic peptide D, cyclic peptide H, composition 1, composition 3, composition 6, and composition 9 were dissolved in PBS and tested at concentrations of 50 ppm and 100 ppm.

[0040] Control group: PBS.

[0041] 1.4 Experimental Methods a) External exfoliation using Bama miniature pig skin, approximately 25mm in diameter and 4.9cm in area. 2 .

[0042] b) Pigskin Integrity Check: Preheat the water bath to 32±1℃ and stabilize the temperature. Install and fix the pigskin between the supply and receiving chambers of the Franz diffusion cell, with the stratum corneum facing the supply chamber and the dermis facing the receiving chamber. Add receiving solution to the receiving chamber through the Franz diffusion cell's replenishment tube, removing air bubbles between the receiving solution and the skin to ensure complete contact between the pigskin and the receiving solution. Turn on the magnetic stirrer at 300 rpm and allow the Franz diffusion cell system to equilibrate under these conditions for 30 minutes. Measure the transepidermal water loss (TEWL) value on the stratum corneum of the pigskin using a transepidermal water loss (TEWL) meter. A TEWL value <15 g / m² is acceptable. 2 Only skin with an integrity level of 6 h can be used for testing. The Bama miniature pig skin used in this test met the integrity requirements.

[0043] c) Fix the Bama fragrant pig skin between the receiving chamber and the supply chamber, take 200 μL of the sample solution to be tested into the supply chamber, use 0.01 M PBS buffer as the receiving chamber system, stir at 300 rpm at 32 °C, and incubate for 24 h.

[0044] d) Place the finger cot over the glass rod, secure it with a rubber band, and place it in the supply chamber to rub the pigskin. After rubbing for 2 minutes, add 300 μL of PBS to wash the supply chamber and collect the keratinocytes shed from the skin surface.

[0045] e) Centrifuge to collect the cell pellet, resuspend the above keratinocytes in 50 μL of deionized water, add 25 μL of 12 mol / L NaOH solution to the liquid, boil in a water bath for 30 min to lyse the keratinocytes, and finally add 25 μL of 12 mol / L HCl solution to neutralize the above lysate.

[0046] f) The total protein concentration of the lysate was determined using the BCA protein quantification kit.

[0047] 1.5 Experimental Results The stratum corneum consists of approximately 10-15 layers of nucleated dead skin cells (keratinocytes), whose main components are proteins and lipids. Under certain environmental conditions, such as dry, cold winters or spring with frequent sandstorms, these keratinocytes can easily accumulate excessively. Timely and moderate exfoliation not only helps improve skin smoothness but also promotes the penetration and absorption of skincare products. In this experiment, test samples were used to treat the skin surface, and the shed keratinocytes were collected for analysis. Since the exfoliation process involves the shedding of keratinocytes, and the number of keratinocytes is positively correlated with the total protein content within them, the number of shed keratinocytes can be indirectly quantitatively characterized by measuring changes in the content of shed protein, thereby analyzing the exfoliating effect of the disclosed cyclic peptide composition. The results of the test samples' influence on the shed keratinocytes on the skin surface are shown in Table 1.

[0048] Table 1. Results of the effect of the test samples on exfoliated keratinocytes on the skin surface (Mean±SD)

[0049] Note: Compared with the control group, ** P <0.01, *** P <0.001.

[0050] The experimental results showed that, compared with the control group, the relative protein shedding amount of the following groups were significantly increased: 100 ppm cyclic peptide A group, 50 ppm cyclic peptide B group, 100 ppm cyclic peptide C group, 50 ppm and 100 ppm cyclic peptide D group, 100 ppm cyclic peptide H group, 50 ppm and 100 ppm combination 1 group, 50 ppm and 100 ppm combination 3 group, 50 ppm and 100 ppm combination 6 group, and 50 ppm and 100 ppm combination 9 group. This demonstrates that each cyclic peptide monomer and combination sample in the experimental groups can effectively remove keratinocytes that have not shed normally from the skin surface, thus exhibiting exfoliating efficacy. Among them, the relative protein shedding amount of the 50 ppm and 100 ppm combination 1 groups were 138.42% and 140.70%, respectively, both significantly better than those of the cyclic peptide A group and the cyclic peptide B group, indicating that the combination of cyclic peptide A and cyclic peptide B produced a synergistic effect, enhancing the exfoliating efficacy. The relative protein shedding rates of the 50ppm and 100ppm compositions in Group 3 were 127.27% and 140.58%, respectively, both significantly better than those of the cyclic peptide A and cyclic peptide C groups. This indicates that the combination of cyclic peptide A and cyclic peptide C produced a synergistic effect, enhancing the exfoliating efficacy. Similarly, the relative protein shedding rates of the 50ppm and 100ppm compositions in Group 6 were 141.15% and 138.65%, respectively, both significantly better than those of the cyclic peptide A and cyclic peptide D groups. This also indicates that the combination of cyclic peptide A and cyclic peptide D produced a synergistic effect, enhancing the exfoliating efficacy. In contrast, while the relative protein shedding amount in group 9 with 50 ppm composition was significantly different from the control group, it did not show a statistically significant difference compared to groups A and H with the same concentration. Similarly, while the relative protein shedding amount in group 9 with 100 ppm composition was significantly different from the control group, it did not show a statistically significant difference compared to group A with the same concentration, and was lower than group H with the same concentration, failing to meet the criteria for synergistic effect. This indicates that the combination of cyclic peptide A and cyclic peptide H did not produce a synergistic effect, proving that not all cyclic peptides capable of removing keratinocytes that fail to shed normally from the skin surface can produce a synergistic effect when combined.

[0051] Further analysis of the relative protein shedding amount of different concentrations of the composition groups showed that, with the increase of concentration, the relative protein shedding amount of composition group 3 increased, and the exfoliation effect was enhanced, indicating a concentration-dependent relationship. The concentration change affected the final exfoliation effect.

[0052] In summary, the cyclic peptide composition disclosed herein can be used to remove keratinocytes that have not shed properly from the skin surface, thereby achieving the effect of exfoliation and increasing skin smoothness.

[0053] Example 2: Multiligand proteoglycan-1 content test

[0054] 2.1 Reagents and Materials Syndecan-1 ELISA kit, RIPA extract, BCA protein quantification kit, trypsin, fetal bovine serum, DMEM medium, phosphate buffer.

[0055] 2.2 Instruments CO2 incubator, ELISA reader, and clean bench.

[0056] 2.3 Cell lines Human keratinocytes (HaCaT).

[0057] 2.4 Sample to be tested Experimental group: Cyclic peptides A, B, C, D, H, Composition 2, Composition 4, Composition 6, and Composition 9 were dissolved in PBS and tested at a concentration of 100 ppm.

[0058] Blank control group: PBS.

[0059] UV group: PBS, plus UV radiation.

[0060] 2.5 Experimental Methods Take one flask of cells in the exponential growth phase, add 0.25% trypsin digestion solution, digest to detach the adherent cells, and count (1~4) × 10⁻⁶ cells. 5 Cells were prepared at a density of 10 cells / mL to form a cell suspension. The cells were then seeded into 12-well plates and incubated in a CO2 incubator for 24 hours.

[0061] Complete culture medium was aspirated from the wells. For the blank control group, 200 μL of PBS was added, and the culture medium was replenished to 800 μL without UVB irradiation. For the UV group and experimental group, 200 μL of PBS was added, and the mixture was irradiated under a UVB lamp for 15 min (irradiation intensity: 80-90 μW / cm²). 2 Irradiation dose: 80 mJ / cm 2 After irradiation for 15 min, the PBS solution was aspirated. 200 μL of PBS was added to the UV group, and the culture medium was replenished to 800 μL. 200 μL of samples of different concentrations were added to the experimental groups, and the culture medium was replenished to 800 μL. The blank control group, UV group, and experimental groups were incubated at 37℃ in a 5% CO2 incubator for 48 h.

[0062] After culture, cells were collected, centrifuged to obtain the cell pellet, and RIPA lysis buffer was added. The pellet was vortexed three times (30 s / time, 3 min interval) and centrifuged at 12000 rpm for 10 min. The supernatant was collected and analyzed according to the multiligand proteoglycan-1 ELISA instruction manual.

[0063] 2.6 Experimental Results In keratinocytes, multiligand proteoglycan-1 (SDC-1), a major transmembrane heparan sulfate proteoglycan, plays a crucial role in maintaining the structural and functional integrity of the epidermis. SDC-1 not only participates in cell-extracellular matrix adhesion but also regulates keratinocyte proliferation, differentiation, and migration, and is involved in the interaction between cells and the microenvironment, as well as the regulation of physiological processes related to skin repair and regeneration. In this experiment, keratinocytes treated with test samples after ultraviolet irradiation were treated, and the SDC-1 content in the keratinocytes was measured to determine whether the cyclic peptide composition disclosed herein could promote SDC-1 expression in keratinocytes. The results of the effect of the test samples on SDC-1 expression in HaCaT cells are shown in Table 2.

[0064] Table 2. Effects of the test samples on the relative expression level of SDC-1 in HaCaT cells (Mean±SD) Test group SDC-1 relative expression level (%) Blank control group 141.79±12.61 UV group <![CDATA[100.00±6.25 ## ]]> Cyclic peptide A group 132.26±5.53*** Cyclic peptide B group 153.00±7.54*** Cyclic peptide C group 139.01±14.09** Cyclic peptide D group 128.93±6.41** Cyclic peptide H group 143.32±8.57*** Composition 2 groups 184.35±14.30*** Composition 4 groups 178.60±8.57*** Composition 6 groups 182.04±13.21*** 9 groups of compositions 142.49±12.46** Note: Compared with the blank control group ## P <0.01; compared with the UV group, ** P <0.01, *** P <0.001.

[0065] The results showed that, compared with the blank control group, the relative expression level of SDC-1 in the UV group was significantly reduced, indicating successful modeling. Compared with the UV group, the relative expression level of SDC-1 in the experimental groups was significantly increased, proving that the experimental samples could effectively promote the expression of SDC-1 in HaCaT cells and have a repairing effect. Further analysis of the combined group results showed that the SDC-1 expression level in HaCaT cells of combination group 2 was 184.35%, significantly better than that of cyclic peptide A and cyclic peptide B groups, indicating that the combination of cyclic peptide A and cyclic peptide B produced a synergistic effect. The SDC-1 expression level in HaCaT cells of combination group 4 was 178.60%, significantly better than that of cyclic peptide A and cyclic peptide C groups, indicating that the combination of cyclic peptide A and cyclic peptide C produced a synergistic effect. The SDC-1 expression level in combination group 6 was 182.04%, significantly better than that of cyclic peptide A and cyclic peptide D groups, indicating that the combination of cyclic peptide A and cyclic peptide D produced a synergistic effect. This demonstrates that combining cyclic peptide A with cyclic peptides B, C, and D produces a synergistic effect, significantly promoting SDC-1 expression and further enhancing its repair efficacy. In contrast, while the relative SDC-1 expression level in group 9 was higher than that in the UV group, it did not show a statistically significant difference compared to groups A and H. This indicates that the combination of cyclic peptide A and H did not produce a synergistic effect, proving that even combinations of cyclic peptides that promote SDC-1 expression do not necessarily produce a synergistic effect and enhance the effect of promoting SDC-1 expression.

[0066] In summary, the cyclic peptide composition disclosed herein can promote the expression of multiligand proteoglycan-1, thereby enhancing epidermal cohesion or dermal-epidermal junction, improving skin barrier function, and promoting skin regeneration and repair, thus having a repairing effect.

[0067] Example 3 Anti-glycation test

[0068] 3.1 Reagents and Materials Phosphate-buffered saline (PBS), pyrrolizaldehyde (MGO), and bovine serum albumin (BSA).

[0069] 3.2 Instruments Clean bench, enzyme-linked immunosorbent assay (ELISA) reader.

[0070] 3.3 Sample to be tested Experimental group: Cyclic peptide A, cyclic peptide B, cyclic peptide C, cyclic peptide D, cyclic peptide H, compositions 1-3, composition 5, and compositions 7-9 were dissolved in PBS and tested at a concentration of 200 ppm.

[0071] Control group: PBS.

[0072] 3.4 Experimental Methods Weigh 100 mg of bovine serum albumin and add it to 10 mL of PBS solution. Dissolve completely to prepare a 10 mg / mL BSA solution. Weigh 14.41 mg of acetone and add it to 40 mL of PBS solution. Dissolve completely to prepare a 5 mM MGO solution. Mix the 10 mg / mL BSA solution and the 5 mM MGO solution in 0.2 M phosphate buffer (pH 7.4) to prepare AGEs.

[0073] The experimental group samples were added to the BSA-MGO model at a volume ratio of 1:1 and shaken thoroughly. All reaction mixtures were incubated at 37°C under sterile conditions for 21 days. The control group was prepared by replacing the test samples with the same volume of PBS, with all other procedures performed identically. Before determining the anti-glycation effect, each reaction mixture was diluted 5-fold with 160 μL of PBS buffer to pH 7.4, then transferred to a 96-well plate, and the fluorescence intensity was measured at an excitation wavelength of 340 nm and an emission wavelength of 435 nm. The AGEs inhibition rate of the test samples was calculated using the following formula: AGEs inhibition rate % = (1 - F1 / F0) × 100% Wherein, F1 is the fluorescence value of the sample to be tested, and F0 is the fluorescence value of the control group.

[0074] 3.5 Experimental Results Advanced glycation end products (AGEs) are stable end products formed by the non-enzymatic glycation reaction of proteins with reducing sugars. The amount of AGEs generated, exhibiting fluorescence properties, is positively correlated with their fluorescence intensity. In this experiment, an in vitro AGEs generation model was constructed using BSA and MGO. By detecting changes in fluorescence intensity of different samples, the anti-glycation activity of the disclosed cyclic peptide composition was determined. The results of the influence of the test samples on AGEs generation are shown in Table 3.

[0075] Table 3. Results of the effect of test samples on AGEs formation (Mean ± SD) Test group AGEs inhibition rate (%) control group 0.00±1.19 Cyclic peptide A group 9.83±1.10** Cyclic peptide B group 12.85±1.08*** Cyclic peptide C group 5.09±1.99* Cyclic peptide D group 7.07±1.20** Cyclic peptide H group -1.84±2.31 Group 1 of the composition 31.17±0.50*** Composition 2 groups 33.00±0.98*** Composition 3 groups 34.07±1.52*** 5 groups of compositions 33.54±0.67*** 7 groups of compositions 40.59±1.84*** 8 groups of compositions 38.75±1.11*** 9 groups of compositions 7.05±1.03** Note: Compared with the control group, * P <0.05,** P <0.01, *** P <0.001.

[0076] The results showed that, compared with the control group, cyclic peptide A, cyclic peptide B, cyclic peptide C, cyclic peptide D, combinations 1-3, combination 5, and combinations 7-9 all significantly inhibited AGEs formation, while cyclic peptide H did not show a significant inhibitory effect on AGEs formation. Specifically, the AGEs inhibition rates of combination 1 and combination 2 were 31.17% and 33.00%, respectively, both significantly better than cyclic peptide A and cyclic peptide B, and their effects were similar, indicating that cyclic peptide A and cyclic peptide B exhibited a synergistic effect when combined within the investigated concentration range. The AGEs inhibition rates of combination 3 and combination 5 were 34.07% and 33.54%, respectively, both significantly better than cyclic peptide A and cyclic peptide C, and their effects were also similar, indicating that cyclic peptide A and cyclic peptide C exhibited a synergistic effect when combined within the investigated concentration range. The AGEs inhibition rates of composition groups 7 and 8 were 40.59% and 38.75%, respectively, both significantly better than cyclic peptide A and cyclic peptide D, and their effects were similar, indicating that cyclic peptide A and cyclic peptide D exhibited a synergistic effect when combined within the investigated concentration range. In summary, cyclic peptide A, when combined with cyclic peptide B, cyclic peptide C, and cyclic peptide D, all produced a synergistic effect, significantly inhibiting AGEs formation and further enhancing its anti-glycation efficacy. In contrast, the AGEs inhibition rate of composition group 9 was only 7.05%, which was significantly improved compared to cyclic peptide H, but did not show a statistically significant difference compared to cyclic peptide A, and did not meet the criteria for synergistic effect, suggesting that the combination of cyclic peptide A and cyclic peptide H failed to produce a synergistic effect.

[0077] In summary, the cyclic peptide composition disclosed herein can effectively inhibit the formation of AGEs, thereby reducing the damage of glycation reactions to the skin, improving dull and sallow skin, delaying skin aging, brightening skin tone, and having anti-aging and anti-glycation effects.

[0078] Example 4

[0079] An essence is prepared through the following steps, and the specific formula is shown in Table 4 below: Table 4

[0080] According to the formula dosage, add all materials of phase A to the mixing pot, stir and heat to 80-85℃, keep warm for 30-35 minutes, start stirring and cooling down to 60-65℃, add all materials of phase B, continue stirring and cooling down to 35-40℃, add materials of phases C and D, stir for 10-15 minutes, and the product is ready.

[0081] In this disclosure, relational terms such as "first" and "second" are used merely to distinguish one entity or operation from another, and do not necessarily require or imply any such actual relationship or order between these entities or operations. Furthermore, the terms "comprising," "including," or any other variations thereof are intended to cover non-exclusive inclusion, such that a process, method, article, or terminal device that comprises a list of elements includes not only those elements but also other elements not expressly listed, or elements inherent to such a process, method, article, or terminal device. Without further limitation, an element defined by the phrase "comprising one..." does not exclude the presence of other identical elements in the process, method, article, or terminal device that includes said element.

[0082] While specific embodiments of this disclosure have been described for illustrative purposes, various modifications or alterations can be made by those skilled in the art without departing from the spirit and scope of this disclosure. All such modifications or alterations should fall within the scope of the appended claims.

Claims

1. A cyclic peptide composition, characterized in that, The cyclic peptide composition comprises component X and component Y, wherein component X is cyclic hexapeptide-8, and component Y is selected from one or more of the following cyclic peptides: cyclic octapeptide-69, Cyclo-(Pro-Lys-Glu-Lys), Cyclo-(Val-Leu-Gln-Trp-Val-Lys).

2. The cyclic peptide composition according to claim 1, characterized in that, The concentration ratio of component X to component Y is (1~9):

3.

3. The cyclic peptide composition according to claim 1, characterized in that, The concentration ratio of component X to component Y is 1:1, 2:1, 3:1, 1:2 or 1:

3.

4. A cosmetic product, characterized in that, The composition comprises an effective amount of the cyclic peptide composition according to any one of claims 1-3, and at least one additional ingredient.

5. The cosmetic product according to claim 4, characterized in that, The dosage forms of the cosmetics include ointments, creams, emulsions, liquids, oils, gels, powders, tablets, muds, patches, films, aerosols, sprays, freeze-dried preparations, or nano-preparations.

6. Use of the cyclic peptide composition according to any one of claims 1-3 in the preparation of compositions for the care of skin or mucous membranes.

7. Use of the cyclic peptide composition according to any one of claims 1-3 in the preparation of compositions for exfoliation, repair or anti-glycation.

8. Use of the cyclic peptide composition according to any one of claims 1-3 in the preparation of a composition for removing keratinocytes that fail to shed normally from the skin surface; or in the preparation of a composition for increasing skin smoothness; or in the preparation of a composition for repairing the skin barrier; or in the preparation of a composition for promoting the expression of multiligand proteoglycan-1; or in the preparation of a composition for enhancing epidermal cohesion or dermal-epidermal junction; or in the preparation of a composition for inhibiting the formation of advanced glycation end products; or in the preparation of a composition for improving dull skin and / or brightening skin tone.

9. Use of the cyclic peptide composition according to any one of claims 1-3 in the preparation of cosmetics.

10. A cosmetic method for non-therapeutic purposes, characterized in that, The method includes using the cyclic peptide composition of any one of claims 1-3, or the cosmetic of claim 4 or 5, on the skin.

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