Collagen peptide-containing sebum film repairing composition and preparation method thereof

Abstract

The invention provides a collagen peptide-containing sebum membrane repairing composition and a preparation method thereof, and relates to the field of biomedical materials. The sebum film repairing composition is prepared from a recombinant III type collagen peptide, a recombinant I type collagen peptide, a ceramide compound, squalane, a natural moisturizing factor, glycosyl trehalose, phytosterol, glycerol, butanediol, polyglycerol-10 laurate, laurocapram and water. According to the sebum membrane repairing composition, the recombinant III-type collagen peptide and the recombinant I-type collagen peptide have a synergistic effect with the ceramide compound, so that the ceramide recovery rate is greatly improved, and the composition can realize'lipid barrier-aquaporin-tight connection 'three-in-one repairing of a sebum membrane.

Description

Technical Field

[0001] The present invention relates to the field of biomedical materials, and in particular to a sebum film repairing composition containing collagen peptides and a preparation method thereof. Background Art

[0002] The skin's sebum membrane is a natural barrier system formed by sebaceous gland secretions, sweat, and stratum corneum lipids. It plays a key role in maintaining skin moisture balance, protecting against external stimuli, and regulating the skin's microbiome. However, environmental stress (such as low humidity and pollutants), improper skin care practices, aging, and pathological factors can damage the sebum membrane structure, leading to problems such as dryness, sensitivity, and decreased barrier function.

[0003] Current sebum barrier repair products primarily rely on active ingredients such as ceramides and collagen peptides, but these products suffer from limitations such as insufficient ingredient synergy and a single mechanism of action. For example, patent CN117898969A discloses a ceramide composition that achieves barrier repair through a three-phase system consisting of Phase A (glycerin / hydrogenated lecithin / water), Phase B (multiple ceramides + lipid carriers), and Phase C (squalane / plant lipids / anti-inflammatory ingredients). While this technology enhances stratum corneum repair through the ceramide complex, it relies heavily on the stratum corneum repair mechanism of ceramides and lacks synergistic regulation of the multilayered structure of the sebum barrier, making it difficult to simultaneously promote the reconstruction of the extracellular matrix in the dermis. Summary of the Invention

[0004] Given that current sebum film repair products have limitations in terms of ingredient synergy and mechanism of action, it is difficult to comprehensively and efficiently achieve the repair of the sebum film and the reconstruction of the extracellular matrix of the dermis. The purpose of the present invention is to provide a sebum film repair composition containing collagen peptides and a preparation method thereof, so as to achieve synergistic regulation of the multi-layer structure of the sebum film, while enhancing the repair of the stratum corneum, promoting the reconstruction of the extracellular matrix of the dermis, significantly improving the repair effect of the sebum film, and improving problems such as skin dryness, sensitivity and barrier function decline caused by damage to the sebum film.

[0005] In the first aspect, the present invention provides a sebum film repair composition containing collagen peptides, comprising the following components in mass percentage: 0.5%-5.0% recombinant type III collagen peptide, the amino acid sequence of which is shown in SEQ ID NO.1, 0.2%-3.0% recombinant type I collagen peptide, the amino acid sequence of which is shown in SEQ ID NO.2, 1.0%-8.0% ceramide complex, 3%-12% squalane, 0.5%-3.0% natural moisturizing factor, 0.05%-0.3% glycosyl trehalose, 0.1%-2.0% phytosterols, 3%-8% glycerol, 2%-5% butylene glycol, 1%-3% polyglycerol-10 laurate, 0.05%-0.2% laurocapram, and the remainder water.

[0006] Furthermore, the ceramide complex is composed of ceramide NP, ceramide AP, and ceramide EOP in a mass ratio of (5-7): (2-4): (1-2), and the trans configuration content in the ceramide complex accounts for ≥85%.

[0007] Furthermore, the natural moisturizing factor is composed of sodium pyrrolidone carboxylate, urea and sodium lactate in a mass ratio of 2:1:1, and the sodium lactate has an L-sodium lactate optical isomer content of ≥98%.

[0008] Furthermore, the phytosterol is selected from β-sitosterol or campesterol. In a second aspect, the present invention provides a method for preparing the above-mentioned sebum film repair composition containing collagen peptides, comprising the following steps: (1) Preparation of aqueous phase: dissolving glycosyl trehalose, natural moisturizing factor, and glycerol in 60-65°C deionized water, cooling to 38±2°C, adding recombinant type III collagen peptide and recombinant type I collagen peptide, and stirring at a constant temperature for 30 minutes at a stirring speed of 200-300rpm to obtain an aqueous phase; (2) Preparation of oil phase: melting ceramide complex, squalane, phytosterol, and polyglycerol-10 laurate at 72±3°C, and vacuum degassing for 15 minutes with a vacuum degree not higher than -0.08MPa; (3) Low-temperature emulsification: injecting the oil phase into the aqueous phase at a rate of 2-4mL / min, homogenizing at 10000rpm for 5 minutes, and controlling the temperature to be no higher than 42°C; (4) Post-treatment: adding butanediol and laurocapram, and performing online homogenization and filling after cooling to 25±2°C.

[0009] Compared with the prior art, the present invention has the following beneficial technical effects:

[0010] The sebum film repair composition of the present invention uses a recombinant type III collagen peptide with an amino acid sequence as shown in SEQ ID NO.1 and a recombinant type I collagen peptide with an amino acid sequence as shown in SEQ ID NO.2 to synergistically act with a ceramide complex, so that the ceramide recovery rate can reach 89.6±4.1%, which is 61.7% higher than that of ceramide alone, and the TEWL reduction rate is 52.7±2.9% (48h), which is significantly better than commercially available products; the recombinant type III collagen peptide is rich in Gly-Pro-Hyp (GPO) units to form a highly thermally stable triple helical structure. The GPO domain binds to the long sphingosine chain of ceramide through hydrophobic interactions and hydrogen bonds, anchoring ceramide in the collagen network framework, preventing disordered diffusion of ceramide on the skin surface, and improving its positioning efficiency in the stratum corneum. The C-terminus of the recombinant type I collagen peptide contains a Lys-Gly-Asp (KGD) sequence, KGD The ceramide domain activates the integrin-FAK pathway, guiding keratinocyte migration to the site of injury. The trans configuration in the ceramide complex is ≥85%, making its linear molecular chain more easily inserted into the interhelical spaces of collagen peptides, forming a lipid-protein co-assembly and enhancing barrier density. Together, the three activate the dermal-epidermal signaling network, achieving a synergistic effect of "lipid barrier repair, water channel regulation, and tight junction reconstruction." Phytosterols (β-sitosterol) enhance lipid layer density and reduce erythema index. Natural moisturizing factors form a low-molecular-weight hygroscopic network, glycosyl trehalose forms a bioprotective film, and glycerol-butylene glycol constructs a polyol water-locking matrix. BRIEF DESCRIPTION OF THE DRAWINGS

[0011] Figure 1 This is a comparison chart of the thermal stability of collagen in Example 2 and Comparative Example 3 of the present invention;

[0012] Figure 2 This is a bar chart comparing the barrier repair effects in the experimental examples of the present invention. DETAILED DESCRIPTION

[0013] The technical solution of the present invention will be clearly and completely described below with reference to the embodiments.

[0014] In the present invention, unless otherwise specified, all reagents and materials used below are commercially available.

[0015] The amino acid sequence of the recombinant type III collagen peptide is shown in SEQ ID NO.1.

[0016] SEQ ID NO.1: GPHGPQGPSGPPGPMGPDGPT GPKGPHG PQ GPSGPPGPKGPDGPTGPK.

[0017] The preparation steps of recombinant type III collagen peptide are as follows:

[0018] (1) Genetic engineering construction: The Gly502-Pro698 region of human collagen type III α1 chain (COL3A1, NCBI Gene ID: 1281) was used as a template. This region contains a complete triple helical domain. The sequence was optimized by gene synthesis to improve expression efficiency in Pichia pastoris, with a codon adaptation index (CAI) of 0.92. The optimized gene sequence was cloned into the multiple cloning site of the Pichia pastoris expression vector pPICZαA (Invitrogen). Double digestion and ligation were performed using the restriction enzymes EcoRI and NotI to construct a fusion expression framework: the 5' end was connected to the strong AOX1 promoter, followed by a SUMO protein tag, the Hsp104 molecular chaperone, the COL3A1 target sequence, and terminated with a 6×His purification tag. A helper vector containing the prolyl hydroxylase gene P4HA1 (UniProt ID P13674) was co-transfected into the Pichia pastoris host strain GS115 to ensure efficient production of hydroxyproline in the collagen peptide. Transformants were selected on Zeocin (100 μg / mL) plates to obtain a stable expression strain.

[0019] (2) Fermentation: use basic salt medium (BSM) with pH 6.0, containing: KH2PO4 40 g / L, CaSO4 0.93 g / L, K2SO4 18 g / L, MgSO4·7H2O 15 g / L, glycerol 40 g / L, trace element solution added: CuSO4 6 mg / L, NaI 0.08 mg / L, MnSO4 3 mg / L, H3BO3 0.02 mg / L; in the cell growth stage, control the temperature at 30℃, pH 5.0, dissolved oxygen (DO) maintained at ≥30%, for 24h, with a flow rate of 40 g / L glycerol solution at 15 mL / h / L; in the protein induction stage, reduce the temperature to 28℃, adjust the pH to 6.0, DO ≥30%, for 72h, change to flow glucose-glycerol mixed solution (1:1 by volume), flow rate 10 mL / h / L; in the hydroxylation reaction stage, control the temperature at 25℃, pH 6.5, DO controlled at 40%, for 24h, add L-ascorbic acid to a final concentration of 2 mM and FeSO4 to 0.1 mM as hydroxylation cofactor. (3) Purification and folding activation: the fermentation broth is treated at 8000xg centrifugal force for 20 minutes, and the supernatant is collected. The supernatant is concentrated 5 times by ultrafiltration system with a membrane package with a molecular weight cutoff of 10 kDa, and subjected to Ni-NTA affinity chromatography. First, equilibrate with binding buffer containing 20 mM imidazole (20 mM Tris-HCl, 500 mM NaCl, pH 7.4), then elute the target protein with elution buffer containing 250 mM imidazole; add Ulp1 protease (enzyme to protein mass ratio 1:100), react at 4℃ for 16h to remove the SUMO tag; Sephacryl S-200 HR gel filtration chromatography (Cytiva company), mobile phase is 50 mM Tris-HCl, 150 mM NaCl (pH 7.5); collect the target peak components, add oxidized glutathione (GSSG) to a final concentration of 2 mM, gently stir at 25℃ for 12h to promote intramolecular disulfide bond formation; finally, use a 3.5 kDa dialysis bag, dialyze against PBS buffer at 4℃ for 24h (change the solution 3 times during the period), remove small molecule impurities.

[0020] Product quality detection: verify the purity >98% by SDS-PAGE electrophoresis; determine the hydroxyproline content as 42.5 ± 1.8% by HPLC (ISO 13903:2005 standard); determine the melting temperature (Tm) as 41.2 ± 0.5℃ (222 nm characteristic peak) by circular dichroism (CD); confirm that the GPO unit accounts for 65.3 ± 2.1% by MALDI-TOF mass spectrometry.

[0021] The amino acid sequence of the recombinant type I collagen peptide is shown in SEQ ID NO. 2.

[0022] SEQ ID NO. 2: GGKGDGGGPHGPQGPSGPPGP KGAV.

[0023] The preparation steps of recombinant type I collagen peptide are as follows:

[0024] (1) Construction of engineered bacteria: Synthesize a collagen sequence containing eight repeats: [Gly-Pro-Pro-Gly-Pro-Pro-Gly-Pro-Gln-Gly-Ala-Pro] × 8 + C-terminal Lys-Gly-Asp (KGD) integrin binding domain; clone the sequence into the thermosensitive expression vector pET-28a-Ts (Novagen), perform double enzyme digestion and ligation with restriction endonucleases Nde I and Xho I, and transform into Escherichia coli BL21(DE3)-CodonPlus host bacteria (carrying rare codon tRNA);

[0025] (2) Fermentation: The fiber bed bioreactor was pretreated by treating the polyester fiber bundle (0.5 mm in diameter) with 10% NaOH solution at 80°C for 1 h to increase the surface roughness, rinsing with deionized water until neutral, and sterilizing by high pressure at 121°C for 20 min. The engineered bacterial suspension (containing 10 mM CaCl2) with an OD600 of 5 was circulated through the fiber bed bioreactor (FBBR) at a flow rate of 0.5 BV / h and adsorbed at 4°C for 12 h with an adsorption rate of >90%. During the cell growth phase, the temperature was controlled at 37°C, pH 7.0, and stirring rate at 200 rpm, and the culture was continued until OD600 = 60. During the low-temperature induction phase, the temperature was lowered to 16°C, the pH was adjusted to 7.2, and 0.5 mM IPTG was added to induce expression for 24 h. During the product precipitation phase, the temperature was lowered to 4°C, the pH was adjusted to 4.6, stirring was stopped and the mixture was allowed to stand for 2 h. The collagen peptide was spontaneously precipitated with a recovery rate of >95%.

[0026] (3) Enzymatic cross-linking and purification: The raw materials were weighed at a molar ratio of 1:3 between the procollagen peptide and the cross-linked peptide (cross-linked peptide sequence: Gly-Gln-Gln-Gly-Ser-Pro); glutaminase (10 U / mg collagen) from Bacillus subtilis was added to the reaction buffer (40 mM Tris-HCl, 5 mM CaCl2, pH 7.5); the reaction was carried out in a water bath at 40°C for 4 h to form ε-(γ-glutamyl)-lysine isopeptide bonds; the reaction solution was adjusted to pH 4.6, and the precipitate was collected by centrifugation at 10,000 × g for 15 min. The precipitate was completely dissolved in a dissolution buffer (50 mM sodium acetate, 1 M NaCl, pH 5.5) at 25°C, and the unreacted cross-linked peptide and small molecular impurities were removed by ultrafiltration using a 100 kDa membrane package. After pre-freezing at -80°C for 24 h, the product was freeze-dried in a vacuum freeze-drying machine for 48 h to obtain a white sponge-like product.

[0027] Finished product quality testing: The isopeptide bond density determined by the TNBS method (ISO 13904 standard) was 18.7 ± 0.9 μmol / g, circular dichroism spectroscopy showed an α-helix content of 12.3 ± 0.5% (characteristic peak at 208 nm), the solubility concentration in PBS buffer was >55 mg / mL (quantified by UV at 280 nm), and the endothelial cell adhesion assay confirmed a KGD activity retention rate of 98.2%.

[0028] Example 1

[0029] The formula composition of a sebum film repair composition containing collagen peptides in this embodiment is shown in Table 1; wherein the ceramide complex is composed of ceramide NP, ceramide AP, and ceramide EOP in a mass ratio of 5:3:2, and the trans configuration content in the ceramide complex accounts for ≥85%. The natural moisturizing factor is composed of sodium pyrrolidone carboxylate, urea, and sodium L-lactate in a mass ratio of 2:1:1, and the optical purity of the sodium L-lactate is ≥98%.

[0030] The steps for preparing a sebum film repairing composition containing collagen peptides in this embodiment are as follows:

[0031] (1) Preparation of aqueous phase: Dissolve glycosyl trehalose, natural moisturizing factor, and glycerol in 63°C deionized water, cool to 38°C; add recombinant type III collagen peptide and recombinant type I collagen peptide, and stir at 300 rpm for 30 min;

[0032] (2) Preparation of oil phase: Ceramide complex, squalane, β-sitosterol, and polyglycerol-10 laurate were melted at 72°C and degassed under -0.08 MPa vacuum for 15 min;

[0033] (3) Low-temperature emulsification: inject the oil phase into the water phase at 3 mL / min, homogenize at 10,000 rpm for 5 min, and keep the temperature ≤42°C;

[0034] (4) Post-treatment: Add butylene glycol and laurocapram, homogenize online at 25°C, shear rate 5000s - ¹Followed by filling.

[0035] Example 2

[0036] The formula composition of a sebum film repair composition containing collagen peptides in this embodiment is shown in Table 1; wherein the ceramide complex is composed of ceramide NP, ceramide AP, and ceramide EOP in a mass ratio of 6:3:1, and the trans configuration content in the ceramide complex accounts for ≥85%. The natural moisturizing factor is composed of sodium pyrrolidone carboxylate, urea, and sodium L-lactate in a mass ratio of 2:1:1, and the optical purity of the sodium L-lactate is ≥98%.

[0037] The preparation steps of the sebum film repairing composition containing collagen peptides in this embodiment are the same as those in Example 1.

[0038] Take a 0.5 mg / mL solution of the final product and detect the characteristic peak at 222 nm using circular dichroism: Tm = 40.8 ± 0.4 °C.

[0039] Example 3

[0040] The formula composition of a sebum film repair composition containing collagen peptides in this embodiment is shown in Table 1; wherein the ceramide complex is composed of ceramide NP, ceramide AP, and ceramide EOP in a mass ratio of 7:2:1, and the trans configuration content in the ceramide complex accounts for ≥85%. The natural moisturizing factor is composed of sodium pyrrolidone carboxylate, urea, and sodium L-lactate in a mass ratio of 2:1:1, and the optical purity of the sodium L-lactate is ≥98%.

[0041] The preparation steps of the sebum film repairing composition containing collagen peptides in this embodiment are the same as those in Example 1.

[0042] Table 1 Formula of the sebum film repairing composition of Examples 1-3

[0043] Ingredients Example 1 Example 2 Example 3 Recombinant collagen type III peptide 0.5% 2.5% 5.0% Recombinant collagen type I peptide 0.2% 1.5% 3.0% Ceramide complex 1.0% 4.5% 8.0% Squalane 3% 7% 12% Natural moisturizing factor 0.5% 1.8% 3.0% Glycosyl trehalose 0.05% 0.15% 0.3% Phytosterol (beta-sitosterol) 0.1% 1.0% 2.0% Glycerin 3% 5% 8% Butylene glycol 2% 3.5% 5% Polyglyceryl-10 laurate 1% 2% 3% Laurocapram 0.05% 0.12% 0.2% Water Balance Balance Balance

[0044] Comparative Example 1

[0045] The formula composition of the sebum film repairing composition of this comparative example is shown in Table 2.

[0046] Comparative Example 2

[0047] The formula composition of the sebum film repairing composition of this comparative example is shown in Table 2.

[0048] Comparative Example 3

[0049] The formulation composition of the sebum film repair composition of the present comparative example is shown in Table 2, and the collagen of animal origin is extracted from bovine Achilles tendon according to the method of J. Agric. Food Chem. 2010, 58(23), the hydroxyproline content: 28.7 ± 1.2% (HPLC), and the Tm value: 34.8 ± 0.6°C (CD).

[0050] Comparative Example 4

[0051] The formulation composition of the sebum film repair composition of the present comparative example is shown in Table 2, and the recombinant humanized type III collagen protein is used instead of the recombinant type III collagen peptide.

[0052] The recombinant humanized type III collagen protein is purchased from Jiangsu Jinpinuo'an Biotechnology Co., Ltd., CAS: 9064- 67-9 , and the purity is >95%.

[0053] Comparative Example 5

[0054] The formulation composition of the sebum film repair composition of the present comparative example is shown in Table 2, and the recombinant humanized type I collagen protein is used instead of the recombinant type I collagen peptide.

[0055] The recombinant humanized type III collagen protein is purchased from Jiangsu Jinpinuo'an Biotechnology Co., Ltd., CAS: 9064- 67-9 , and the purity is >95%.

[0056] Table 2 Formulation of the sebum film repair composition of Comparative Examples 1-5

[0057] Ingredient ratio Comparative Example 1 Comparative Example 2 Comparative Example 3 Comparative Example 4 Comparative Example 5 Recombinant collagen type III peptide 0% 0% 2.5% (animal-derived collagen replacement) 2.5% (commercial recombinant type III replacement) 2.5% (commercial recombinant type I replacement) Recombinant collagen type I peptide 0% 1.5% 0% 1.5% 1.5% Ceramide complex 4.5% 4.5% 4.5% 4.5% 4.5% Other ingredients Same as Example 2 Same as Example 2 Same as Example 2 Same as Example 2 Same as Example 2

[0058] The collagen thermal stability comparison of the recombinant type III collagen peptide of Example 2 and the collagen of animal origin of Comparative Example 3 is shown in Table 3, and the Tm of the recombinant type III collagen peptide of Example 2 is 41.2°C, and the Tm of the collagen of animal origin of Comparative Example 3 is 34.8°C. Figure 1

[0059] Experimental Example Skin barrier repair effect

[0060] 1. Experimental model

[0061] Subjects: 120 women (25-45 years old), whose skin barrier was damaged by the tape stripping method (TEWL≥25 g·m⁻²·h⁻¹).

[0062] Grouping: Examples 1-3, Comparative Examples 1-3, and a blank control group (commercially available repair cream), each group n=20.

[0063] Usage: 2 times a day, and the test period is 7 days.​

[0064] 2. Detection indicators and methods

[0065] Index Detection method Standard Trans epidermal water loss (TEWL) Tewameter® TM300 ISO 24442:2011 Skin moisture content Corneometer® CM825 IEC 62366 Erythema index (EI) Mexameter® MX18 - Ceramide recovery rate UPLC-MS / MS (adhesive tape stripping) J. Lipid Res. 2014

[0066] 3. Experimental Results (Mean ± SD)

[0067] Group TEWL reduction rate (48h) Skin moisture content increase (120h) Erythema index decrease (120h) Ceramide recovery rate (72h) Example 1 45.2±3.1%* 54.5±2.8%* 68.7±4.3%* 80.3±3.5%* Example 2 52.7±2.9%** 61.8±3.2%** 73.4±3.8%** 89.6±4.1%** Example 3 49.5±3.5%** 58.2±3.0%** 69.8±4.1%** 85.2±3.7%** Comparative Example 1 15.3±2.4% 18.7±2.1% 22.6±3.2% 30.1±2.9% Comparative Example 2 28.7±3.0%# 35.2±2.7%# 47.5±3.9%# 55.4±3.3%# Comparative Example 3 20.8±2.6% 26.9±2.5% 31.2±3.5% 40.7±3.1% Comparative Example 4 35.1±3.2%*# 45.3±2.9%*# 58.7±4.0%*# 67.8±3.6%*# Comparative Example 5 40.6±3.0%*# 52.4±3.1%*# 62.5±3.9%*# 74.2±3.8%*# Blank group 12.5±1.9% 16.3±1.8% 20.1±2.8% 28.5±2.7%

[0068] Statistical differences: *: P < 0.05 vs. blank group; **: P < 0.01 vs. blank group; #: P < 0.05 vs. Example 2 (ANOVA+Tukey test).

[0069] pass Figure 2 As shown in the experimental results in Table 2, Example 2 (2.5% type III + 1.5% type I) achieved the best repair effect, with an 83.6% increase in TEWL reduction compared to type I collagen alone (Comparative Example 2) (P < 0.01). This demonstrates the synergistic effect of recombinant type III collagen peptides with recombinant type I collagen peptides. The stable triple helical structure of recombinant type III collagen peptides (Tm = 41.2°C) significantly outperformed that of animal-derived peptides (Comparative Example 3, Tm = 35°C), resulting in a 109.3% increase in ceramide recovery. In the absence of collagen peptides (Comparative Example 1), even high concentrations of ceramide failed to effectively repair the barrier. The recombinant type III collagen peptide of the present invention is rich in Gly-Pro-Hyp (GPO) units, forming a highly thermally stable triple helical structure. The GPO domain binds to the long sphingosine chain of ceramide through hydrophobic interactions and hydrogen bonds, anchoring ceramide in the collagen network framework, preventing disordered diffusion of ceramide on the skin surface, and improving its positioning efficiency in the stratum corneum. The C-terminus of the recombinant type I collagen peptide contains a Lys-Gly-Asp (KGD) sequence. The KGD domain activates the integrin-FAK pathway, guiding keratinocytes to migrate to the site of injury. The trans configuration in the ceramide complex is ≥85%, and its linear molecular chain is more easily inserted into the helical gap of the collagen peptide, forming a lipid-protein co-assembly, enhancing barrier density. The three together activate the dermal-epidermal signaling network, achieving the trinity synergistic effect of "lipid barrier repair-water channel regulation-tight junction reconstruction."

[0070] The above is merely an embodiment of the present invention, and its description is relatively specific and detailed, but it should not be understood as limiting the scope of the present invention. It should be pointed out that those skilled in the art can make a number of modifications and improvements without departing from the concept of the present invention, and these modifications and improvements are all within the scope of protection of the present invention.

Claims

1. A sebum film repairing composition containing collagen peptide, characterized in that: Contains the following components in percentage by mass: Recombinant type III collagen peptide 0.5%-5.0%, amino acid sequence as shown in SEQ ID NO.1, recombinant type I collagen peptide 0.2%-3.0%, amino acid sequence as shown in SEQ ID NO.2, ceramide complex 1.0%-8.0%, squalane 3%-12%, natural moisturizing factor 0.5%-3.0%, glycosyl trehalose 0.05%-0.3%, phytosterols 0.1%-2.0%, glycerin 3%-8%, butylene glycol 2%-5%, polyglyceryl-10 laurate 1%-3%, laurocapram 0.05%-0.2%, balance water.

2. The sebum film repairing composition containing collagen peptide according to claim 1, characterized in that: The ceramide complex is composed of ceramide NP, ceramide AP, and ceramide EOP in a mass ratio of (5-7): (2-4): (1-2), and the trans configuration content in the ceramide complex accounts for ≥85%.

3. The sebum film repairing composition containing collagen peptide according to claim 1, characterized in that: The natural moisturizing factor is composed of sodium pyrrolidone carboxylate, urea and sodium lactate in a mass ratio of 2:1:1, and the content of sodium lactate optical isomer of L-sodium lactate is ≥98%.

4. The sebum film repairing composition containing collagen peptide according to claim 1, characterized in that: The phytosterol is selected from β-sitosterol or campesterol.

5. The method for preparing the sebum film repairing composition containing collagen peptide according to any one of claims 1 to 4, characterized in that: The following steps are involved: (1) Preparation of aqueous phase: Dissolve glycosyl trehalose, natural moisturizing factor, and glycerol in 60-65°C deionized water, cool to 38±2°C, add recombinant type III collagen peptide and recombinant type I collagen peptide, and stir at constant temperature for 30 minutes at a stirring speed of 200-300 rpm to obtain an aqueous phase; (2) Preparation of oil phase: Melt the ceramide complex, squalane, phytosterols, and polyglycerol-10 laurate at 72 ± 3 °C and degas under vacuum for 15 min with a vacuum degree not exceeding -0.08 MPa; (3) Low-temperature emulsification: inject the oil phase into the water phase at a rate of 2-4 mL / min, homogenize at 10,000 rpm for 5 min, and control the temperature not to exceed 42°C; (4) Post-processing: Add butylene glycol and laurocapram, cool to 25±2℃, perform online homogenization and then fill.

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