Composition containing polypeptide and collagen and application thereof

Abstract

The invention discloses a composition containing polypeptide and collagen and application of the composition. The composition comprises the polypeptide and the collagen. The polypeptide is prepared from palmitoyl pentapeptide-4, decarboxylated carnosine, acetyl octapeptide-3 and hexapeptide-11; the collagen is a recombinant XVII type collagen; the mass ratio of the polypeptide to the collagen is (12: 5)-(12: 25). The recombinant XVII type collagen is added into the polypeptide composition, on one hand, the permeability of the polypeptide composition can be remarkably improved, on the other hand, the generation of the collagen can be improved, and compounding of the polypeptide composition and the recombinant XVII type collagen can achieve synergistic interaction and improve relative expression of COL7A1 and COL17A1 genes, so that the overall anti-aging effect is enhanced.

Description

Technical Field

[0001] The present invention relates to the technical field of cosmetics, and particularly to a composition containing polypeptides and collagen and its application. Background Art

[0002] In recent years, with the continuous growth of the appearance economy and self-pleasing consumption, the public's anti-aging awareness has shown a trend of becoming younger. Anti-aging has become a rigid demand for beauty-seeking across multiple age groups and is also the most concerned skin care need of consumers. Anti-aging skin care products have led to a boom in functional skin care consumption, and the market demand for related technologies has increased significantly.

[0003] Patent document CN119454551A records that by compounding plant extracts (Leontopodium alpinum, peach resin, gentian root, nasturtium) with composite polypeptides (palmitoyl tripeptide-1, tetrapeptide-7, etc.) and recombinant collagen (types I / IV / VII), the skin elasticity and anti-wrinkle effect are improved. Patent document CN119280095A records the compounding of okra hydrolyzed glycoprotein, Bidens pilosa extract, recombinant type XVII / III collagen and Cordyceps sinensis extract, emphasizing anti-wrinkle by supplementing collagen and activating endogenous generation. Although these compositions introduce recombinant collagen, the correlation with the expression of collagen-related genes (such as COL1A1, COL4A1, COL17A1, etc.) has hardly been verified, and there is a lack of targeted repair of collagen. Secondly, the stability of some natural ingredients in the composition is poor and is easily affected by factors such as heat and light, resulting in a decrease in their activity.

[0004] Patent document CN114010526A discloses an anti-aging polypeptide composition containing a complex of hexapeptide-11 and trifluoroacetyl tripeptide-2. It slows down the aging process by reducing the level of oxidative stress (ROS). However, the action target of this patented composition is relatively single and is only limited to the reduction of oxidative stress, and cannot comprehensively solve multiple aspects of skin aging problems, such as collagen synthesis and improvement of skin elasticity.

[0005] In addition, most of the anti-aging ingredients in the prior art, although having certain activity, are difficult to penetrate deep into the skin due to their large molecular structure or physical and chemical property limitations, resulting in a significant reduction in the effect. Summary of the Invention

[0006] Aiming at the deficiencies of the prior art, the present invention provides a composition containing polypeptides and collagen and its application.

[0007] The object of the present invention is achieved by the following technical solutions:

[0008] In the first aspect, the present invention provides a composition containing polypeptides and collagen, and the composition includes polypeptides and collagen;

[0009] The polypeptide includes palmitoyl pentapeptide-4, carnosine, acetyl octapeptide-3 and hexapeptide-11;

[0010] The collagen is recombinant type XVII collagen;

[0011] The mass ratio of the polypeptide to the collagen is 12:5 to 12:25.

[0012] As a preferred embodiment, the mass ratio of the polypeptide to the collagen is 12:10 to 12:20.

[0013] As a preferred embodiment, the mass ratio of the polypeptide to the collagen is 12:18 to 22, and most preferably the mass ratio is 12:20.

[0014] As a preferred embodiment, the polypeptide includes palmitoyl pentapeptide-4, carnosine, acetyl octapeptide-3 and hexapeptide-11 with a mass ratio of 0.0001-5:0.0001-5:0.0001-5:0.0001-5.

[0015] As a preferred embodiment, the polypeptide includes palmitoyl pentapeptide-4, carnosine, acetyl octapeptide-3 and hexapeptide-11 with a mass ratio of 1:1:1:1.

[0016] In a second aspect, the present invention provides an application of the composition containing polypeptide and collagen as described above in the preparation of anti-aging products.

[0017] As a preferred embodiment, the mass percentage content of the composition in the anti-aging product is 0.0001-5%.

[0018] As a preferred embodiment, the anti-aging product is anti-aging skin care products, and the dosage forms of the skin care products include any one of aqueous solutions, emulsions, creams, gels, oils, powders, tablets, muds, aerosols, patches, films or nano-formulations.

[0019] In a third aspect, the present invention provides an anti-aging skin care product, including the composition containing polypeptide and collagen as described above; the mass percentage content of the composition in the anti-aging skin care product is 0.0001-5%.

[0020] As a preferred embodiment, the skin care product further includes at least one of a solvent, an oil, a chelating agent, an emulsifier, a humectant, a thickening agent, a solubilizer, an emollient, a rheology modifier, an antioxidant, a whitening agent, a conditioner, a soother, an aromatic agent, a pigment.

[0021] Compared with the prior art, the present invention has the following beneficial effects:

[0022] 1) By adding recombinant type XVII collagen to the polypeptide composition, the present invention can significantly improve the permeability of the polypeptide composition. The results of percutaneous penetration tests show that after adding recombinant type XVII collagen, the relative permeabilities of the polypeptide composition at 0.5 h, 2 h, 4 h, and 6 h are increased by 815.6%, 70.6%, 70.4%, and 47.7% respectively.

[0023] 2) By adding recombinant type XVII collagen to the polypeptide composition, the present invention can promote the production of collagen. Moreover, through the compounding of the polypeptide composition and recombinant type XVII collagen, synergistic effects can be achieved, the relative expressions of COL7A1 and COL17A1 genes can be increased, thereby enhancing the overall anti-aging effect. Description of the Drawings

[0024] By reading the following detailed description of the non-limiting embodiments with reference to the accompanying drawings, other features, objectives, and advantages of the present invention will become more apparent:

[0025] Figure 1 Results of testing the cell viability using the polypeptide composition, recombinant type XVII collagen, or a combination of both;

[0026] Figure 2 Distribution diagram of the test samples of the polypeptide composition at different depths of human in vivo skin;

[0027] Figure 3 Distribution diagram of the test samples of the polypeptide composition compounded with recombinant type XVII collagen at different depths of human in vivo skin;

[0028] Figure 4 Relative permeability change curve of the polypeptide composition when using the test samples of the polypeptide composition and the test samples of the polypeptide composition compounded with recombinant type XVII collagen. Detailed Embodiments

[0029] The present invention will be described in detail below in conjunction with specific embodiments. The following embodiments will help those skilled in the art to further understand the present invention, but do not limit the present invention in any form. It should be noted that for those of ordinary skill in the art, without departing from the concept of the present invention, several modifications and improvements can still be made. These all fall within the protection scope of the present invention.

[0030] In the previous research results of the applicant's R & D team, a polypeptide composition with synergistic effect (CN118141702A) was developed. Through the reasonable combination of different polypeptides, it can play roles such as antioxidant, promoting collagen production, and inhibiting elastase, thereby delaying skin aging. However, the skin permeability of this polypeptide composition is still insufficient, and the effect of promoting collagen production remains to be improved. Based on this, on the basis of this polypeptide composition scheme, the present invention attempts to add type XVII collagen to achieve promoting the skin permeability of other polypeptides, further improving the production of collagen, and enhancing the overall anti-aging effect.

[0031] The technical solution of the present invention will be elaborated in detail through examples below.

[0032] Example 1

[0033] (1) In vitro cell safety evaluation

[0034] 1.1 Experimental materials

[0035] Samples to be tested: recombinant type XVII collagen and polypeptide composition

[0036] Blank control group (BC): serum-free DMEM medium

[0037] Treatment of the test sample group: 1) Recombinant type XVII collagen group: Take 1 mL of recombinant type XVII collagen solution (the mass concentration of recombinant type XVII collagen is 100 ppm), add 4 mL of DEME medium containing 10% serum (FBS) to prepare a 20% recombinant type XVII collagen solution, and then dilute it to 10%, 5%, 2.5%, 1.25%, 0.625%, 0.3125% recombinant type XVII collagen solutions for standby; 1) Polypeptide composition group: Weigh palmitoyl pentapeptide-4, decarboxy carnosine, acetyl octapeptide-3 and hexapeptide-11 and add them to a solvent (pure water) to prepare a polypeptide composition solution (where the mass concentration of palmitoyl pentapeptide-4, decarboxy carnosine, acetyl octapeptide-3 and hexapeptide-11 is 5 ppm each); Weigh 1 mL of the polypeptide composition solution, add 4 mL of DEME medium containing 10% serum (FBS) to prepare a 20% polypeptide composition solution, and then dilute it to 10%, 5%, 2.5%, 1.25%, 0.625%, 0.3125% polypeptide composition solutions for standby; 3) Polypeptide composition: Recombinant type XVII collagen = 6:1 group (the mass ratio of palmitoyl pentapeptide-4, decarboxy carnosine, acetyl octapeptide-3, hexapeptide-11, recombinant type XVII collagen is 3:3:3:3:10): Take 1200 μL of the previously prepared polypeptide composition solution, add 200 μL of recombinant type XVII collagen solution to prepare a 100% 6:1 finished product solution, take 1 mL of the 100% 6:1 finished product solution, add 4 mL of DEME medium containing 10% serum (FBS) to prepare a 20% 6:1 finished product solution, and then dilute it to 10%, 5%, 2.5%, 1.25%, 0.625%, 0.3125% 6:1 finished product solutions for standby; 4) Polypeptide composition: Recombinant type XVII collagen = 3:1 group (the mass ratio of palmitoyl pentapeptide-4, decarboxy carnosine, acetyl octapeptide-3, hexapeptide-11, recombinant type XVII collagen is 3:3:3:3:20): Take 1200 μL of the previously prepared polypeptide composition solution, add 400 μL of recombinant type XVII collagen solution to prepare a 100% 3:1 finished product solution, take 1 mL of the 100% 3:1 finished product solution, add 4 mL of DEME medium containing 10% serum (FBS) to prepare a 20% 3:1 finished product solution, and then dilute it to 10%, 5%, 2.5%, 1.25%, 0.625%, 0.3125% 3:1 finished product solutions for standby. Incubate samples with different concentrations for 24 h.

[0038] Cell source: Human immortalized keratinocytes HaCaT, from the Cell Bank of the Chinese Academy of Sciences.

[0039] 1.2 Main reagents and instruments (as shown in Tables 1 and 2 below)

[0040] Table 1 Raw materials and reagents

[0041]

[0042]

[0043] Table 2 Instruments and Equipment

[0044]

[0045] 1.3 Experimental Methods

[0046] Separate sample groups and blank control groups were set up for comparative experiments, and 6 replicates (n = 6) were set up for the cell experiments. Cells in the logarithmic growth phase were taken and inoculated into 96-well plates at 1×10 4 cells / well, and incubated in an incubator at 37°C and 5% CO 2 for 24 h. After incubation, the supernatant was discarded and the cells were washed twice with PBS. Solutions of each concentration gradient prepared for each test sample group were added to the wells, 100 μL per well, and incubated for 24 h. Then, 10 μL of CCK-8 reagent was added and incubated for 1 h, and the OD value at 450 nm was measured. The calculation formula for cell viability (i.e., cell survival rate) is as follows:

[0047]

[0048] In the formula: V(%) — cell viability, %; ODsample — absorbance of the reaction system containing the test sample; ODblank control — absorbance of the blank well without any substance; ODcell control — absorbance of the reaction system without the test sample.

[0049] 1.4 Data Processing

[0050] Using GraphPad Prism 8 software, the data are expressed as mean ± standard error.

[0051] 1.5 Experimental Results and Analysis

[0052] Cell survival rate is usually used as an index to evaluate the cytotoxicity of components, and the CCK-8 method can measure the number of viable cells in cells, and its advantages are high sensitivity and no radioactivity. As Figure 1 shown, compared with the blank control group, the cell survival rate was greater than 90% at concentrations of recombinant type XVII collagen from 0.3125% to 5%; the cell survival rate was greater than 90% within the concentration threshold of 0.3125% to 10% for the polypeptide composition; the cell survival rate was greater than 90% within the concentration threshold of 0.3125% to 2.5% for the polypeptide composition: recombinant type XVII collagen = 6:1 or 3:1. Based on the above results, 2.5% of the polypeptide composition, recombinant type XVII collagen, and polypeptide composition: recombinant type XVII collagen = 6:1 or 3:1 were selected for subsequent experiments.

[0053] (2) In vitro efficacy test

[0054] 2.1 Experimental materials

[0055] Samples to be tested: 2.5% sample solutions prepared in each sample group in Step 1.1

[0056] Blank control group (BC): Starved with serum-free DMEM medium for 2 h and then cultured with 10% serum (FBS) DMEM medium for 24 h

[0057] Model (UVB) group: Starved with serum-free medium for 2 h, irradiated with 60 mJ / cm 2 and then cultured with 10% serum (FBS) DMEM medium for 24 h after UVB irradiation

[0058] Treatment of the sample group to be tested: Starved with serum-free medium for 2 h, irradiated with 60 mJ / cm 2 and then cultured with the corresponding concentration of sample solution for 24 h after UVB irradiation

[0059] Positive control (PC) group: Starved with serum-free medium for 2 h, irradiated with 60 mJ / cm 2 and then cultured with 10% serum (FBS) DMEM medium containing VC + VE for 24 h after UVB irradiation

[0060] Cell source: Human immortalized keratinocyte HaCaT, P14

[0061] 2.2 Main reagents and instruments (as shown in Tables 3 and 4 below)

[0062] Table 3 Reagents

[0063]

[0064] Table 4 Instruments and equipment

[0065]

[0066]

[0067] 2.3 Experimental grouping (as shown in Table 5)

[0068] Table 5 Experimental grouping

[0069]

[0070] 2.4 Experimental methods

[0071] 1) Seed HaCaT cells in the logarithmic growth phase at 1*10 6 cells per well in a 6-well plate and culture at 37°C in 5% CO 2Cultivate in an incubator for 24 h;

[0072] 2) Discard the culture medium, add 2 mL of serum-free DMEM medium to each well, and starve for 2 h;

[0073] 3) After discarding the serum-free medium, treat the cells with UVB (60 mJ / cm 2 ), (the blank control group does not need to be treated with UVB);

[0074] 4) After washing twice with PBS, add the sample solution to the sample group, and add 10% serum DMEM medium to the blank control group and the model group. Incubate in an incubator at 37 °C with 5% CO 2 for 24 h;

[0075] 5) Discard the supernatant, wash twice with PBS, and collect the cells;

[0076] 6) Extract RNA, reverse transcribe it into cDNA, and then perform RT-qPCR.

[0077] 7) The relative expression level of the target gene uses GAPDH as an internal reference and is calculated by the 2 -△△Ct method.

[0078] 8) Import the calculated values into Graphpad Prism 8 for statistical analysis and graphing.

[0079] 2.5 Data processing

[0080] Using Graphpad Prism 8 software, the data is expressed as mean ± standard error. The inter-group difference between the blank control group and the model group is analyzed by T-test; the inter-group difference between the experimental group and the model group is analyzed by one-way ANOVA. P < 0.05 is considered to have a significant difference, P < 0.01 is considered to have a highly significant difference, and P < 0.001 is considered to have an extremely significant difference.

[0081] 2.6 Experimental results and analysis

[0082] Table 6 Summary of the analysis of COL4A1 gene expression results

[0083]

[0084] Table 7 Summary of the analysis of COL7A1 gene expression results

[0085]

[0086] Table 8 Summary of the analysis of COL17A1 gene expression results

[0087]

[0088] Summary of the analysis of COL1A1 gene expression results

[0089]

[0090] COL1A1 is a gene encoding the α1 chain of type I collagen and is involved in maintaining the integrity and elasticity of the skin. COL17A1 plays an important role in keeping the skin young. It promotes stem cell competition, maintains tissue health, and at the same time promotes the proliferation of stronger cells; ECM is mainly composed of collagen IV (COL4) and is crucial for maintaining tissue structure and function. Collagen VII (COL7) encoded by the COL7A1 gene forms anchoring fibers that connect the epidermis to the dermis.

[0091] HaCaT cells were used, and RT-qPCR was performed to analyze the relative expression levels of COL4A1, COL1A1, COL17A1, and COL1A1 genes. The results are shown in Tables 6, 7, 8, and 9. Compared with the model group, the use of 2.5% polypeptide composition, recombinant type XVII collagen, and the compound of polypeptide composition: recombinant type XVII collagen = 6:1 and 3:1 could significantly increase the relative expression of COL4A1, COL7A1, COL17A1, and COL1A1 genes.

[0092] Furthermore, from the results of Tables 6 and 10, it can be seen that when using the compound of 2.5% polypeptide composition: recombinant type XVII collagen = 6:1 or 3:1, the promotion rates of the relative expression of COL4A1 and COL1A1 genes are both between the promotion rate of using 2.5% polypeptide composition alone and the promotion rate of using 2.5% recombinant type XVII collagen alone. From the results of Table 7, it can be seen that when using the compound of 2.5% polypeptide composition: recombinant type XVII collagen = 6:1, the promotion rates of the relative expression of COL4A1 and COL1A1 genes are between the promotion rate of using 2.5% polypeptide composition alone and the promotion rate of using 2.5% recombinant type XVII collagen alone; while when using the compound of 2.5% polypeptide composition: recombinant type XVII collagen = 3:1, the promotion rate of the relative expression of COL7A1 gene is higher than the promotion rate of using 2.5% polypeptide composition or recombinant type XVII collagen alone, indicating that the combination of 3:1 compound can play a synergistic effect and increase the relative expression of COL7A1 gene. From the results of Table 8, it can be seen that when using the compound of 2.5% polypeptide composition: recombinant type XVII collagen = 6:1 or 3:1, the promotion rates of the relative expression of COL17A1 gene are higher than the promotion rate of using 2.5% polypeptide composition or recombinant type XVII collagen alone, indicating that the combination of polypeptide composition and recombinant type XVII collagen can play a synergistic effect and increase the relative expression of COL17A1 gene.

[0093] The combination based on the polypeptide composition and the recombinant type XVII collagen can significantly increase the relative expression of the COL7A1 and COL17A1 genes. Therefore, the combination of the polypeptide composition and the recombinant type XVII collagen can promote the expression of these two genes and thus significantly enhance the anti-aging effect.

[0094] (3) Percutaneous penetration test

[0095] 3.1 Experimental purpose and method

[0096] Select the front area of the human forearm for human Raman testing: The samples used for testing are the polypeptide composition (sample group 1 in Table 5) and the polypeptide composition: recombinant type XVII collagen = 3:1 (sample group 4 in Table 5). Select a test skin area of 1×1 cm 2 and conduct tests at time points of 0.5 h, 2 h, 4 h, and 6 h; The total number of test subjects is 1 person, and the test area is 3 pieces of 1×1 cm 2 test skin area. Select 5 points in each test area and conduct parallel tests 3 times.

[0097] Specific method: T / SHRH 064-2024 "In-vivo Raman Spectroscopy Method for Percutaneous Penetration Test of Cosmetic Ingredients on Human Body".

[0098] 3.2 Test samples

[0099] Test samples: Polypeptide composition, polypeptide composition: recombinant type XVII collagen = 3:1

[0100] Usage method: Apply topically, and the usage amount is 2 mg / cm 2

[0101] 3.3 Test instruments

[0102] LabRAM Soleil ultra-high resolution confocal Raman spectrometer

[0103] 3.4 Test environment

[0104] Temperature: 22°C ± 2°C; Humidity: 50% ± 10%

[0105] 3.5 Test process

[0106] Explain the test to the subject. After the subject arrives, clean the skin of the test area with clean water. After cleaning, enter the constant temperature and humidity room and sit quietly for 30 min. Then take the product and apply it to the test area for Raman testing of the light peptide sample.

[0107] 3.6 Result statistical method

[0108] Raman spectroscopic imaging data processing includes spectral preprocessing and data analysis. The spectral preprocessing process includes several processes such as cosmic ray removal, spectral smoothing, background noise removal, baseline calibration, and spectral normalization. Univariate data analysis mainly focuses on the biochemical substances corresponding to a specific peak position, performs Raman spectroscopic data analysis, and shows the distribution of the substance in human skin.

[0109] For data analysis, Labspec software is used to perform baseline calibration and confirm the positions of characteristic peaks on the Raman spectrogram, and calculations are carried out on the obtained Raman spectra, including peak intensity, peak shift, peak area, full width at half maximum, etc.; at the same time, Labspec software is used for numerical analysis of the peak intensities corresponding to different depths and the drawing of their spatial distributions.

[0110] The penetration behavior of the sample is confirmed by the characteristic Raman signal that distinguishes the product from the skin intrinsic signal, and its distribution in different skin depth spaces is determined.

[0111] 3.7 Test Results

[0112] Through in-depth analysis of the Raman images, the distribution of the polypeptide composition in the test sample of the polypeptide composition at different depths in human in-vivo skin is obtained, and its distribution map is as follows Figure 2 As shown, through analysis, it is obtained that within 0.5 h, 2 h, 4 h, and 6 h after using the polypeptide composition sample on human in-vivo skin, the relative permeabilities of the polypeptide composition are 0.45%, 7.08%, 12.52%, and 19.73% respectively.

[0113] Through in-depth analysis of the Raman images, the distribution of the polypeptide complex in the test sample of the polypeptide complex complexed with recombinant type XVII collagen at different depths in human in-vivo skin is obtained, and its distribution map is as follows Figure 3 As shown, through analysis, it is obtained that within 0.5 h, 2 h, 4 h, and 6 h after using the test sample of the light peptide complexed with recombinant type XVII collagen on human in-vivo skin, the relative permeabilities of the polypeptide composition are 4.12%, 12.08%, 21.33%, and 29.15% respectively.

[0114] Through the analysis of Figure 4 the permeability change curve, it can be known that recombinant type XVII collagen promotes the penetration of the polypeptide composition in the skin, and after the polypeptide composition is complexed with recombinant type XVII collagen, compared with the use of the polypeptide composition alone, the relative permeabilities of the polypeptide composition at 0.5 h, 2 h, 4 h, and 6 h are increased by 815.6%, 70.6%, 70.4%, and 47.7% respectively.

[0115] The specific application scenarios of the present invention are numerous. The above description is only the preferred embodiment of the present invention. It should be noted that the above embodiments are only used to illustrate the present invention and do not limit the protection scope of the present invention. For those of ordinary skill in the art of this technology, several improvements can be made without departing from the principle of the present invention, and these improvements should also be regarded as within the protection scope of the present invention.

Claims

1. A composition containing polypeptide and collagen, characterized in that: The composition includes a polypeptide and collagen; The polypeptides include palmitoyl pentapeptide-4, decarboxylated carnosine, acetyl octapeptide-3 and hexapeptide-11; The collagen is recombinant type XVII collagen; The mass ratio of the polypeptide to collagen is 12:5 to 12:

25.

2. The composition containing polypeptide and collagen according to claim 1, characterized in that: The mass ratio of the polypeptide to collagen is 12:10 to 12:

22.

3. The composition containing polypeptide and collagen according to claim 1, characterized in that: The mass ratio of the polypeptide to collagen is 12:18-22.

4. The composition containing polypeptide and collagen according to claim 1, 2 or 3, characterized in that: The polypeptides include palmitoyl pentapeptide-4, decarboxylated carnosine, acetyl octapeptide-3 and hexapeptide-11 in a mass ratio of 0.0001-5:0.0001-5:0.0001-5:0.0001-5.

5. The composition containing polypeptide and collagen according to claim 3, characterized in that: The polypeptides include palmitoyl pentapeptide-4, decarboxylated carnosine, acetyl octapeptide-3 and hexapeptide-11 in a mass ratio of 1:1:1:

1.

6. Use of the composition containing polypeptide and collagen according to any one of claims 1 to 5 in the preparation of anti-aging products.

7. The use according to claim 6, characterized in that: The mass percentage of the composition in the anti-aging product is 0.0001-5%.

8. The use according to claim 6 or 7, characterized in that: The anti-aging product is an anti-aging skin care product, and the dosage form of the skin care product includes any one of an aqueous solution, an emulsion, a cream, a gel, an oil, a powder, a tablet, a mud, an aerosol, a patch, a film or a nano preparation.

9. An anti-aging skin care product, characterized in that: A composition comprising a polypeptide and collagen as claimed in any one of claims 1 to 5; the mass percentage of the composition in anti-aging skin care products is 0.0001 to 5%.

10. The anti-aging skin care product according to claim 9, characterized in that: The skin care product also includes at least one of solvents, oils, chelating agents, emulsifiers, moisturizers, thickeners, solubilizers, emollients, rheology regulators, antioxidants, whitening agents, conditioners, soothing agents, fragrances, and pigments.

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