A peptide capable of regulating sebum secretion and its synthesis method and application

CN118791560BActive Publication Date: 2025-02-25GUANGZHOU MUCO BIOTECHNOLOGY CO LTD
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Patent Information

Application Number
CN202410775766.0
Authority / Receiving Office
CN · China
Patent Type
Patents(China)
Current Assignee / Owner
Filing Date
2024-06-17
Publication Date
2025-02-25
Estimated Expiration
2044-06-17

AI Technical Summary

Technical Problem

[0005]现有技术虽然开发了具有皮脂调节的多肽,但因为氨基酸序列长,产率低成本高,而且产品的耐水解性能差,不利于在化妆品产品中的应用

Benefits of technology

[0051] 1) The present invention designs and develops a group of oil control peptides with excellent performance, including: oil control polypeptide-1: Pal-Tyr-Gly-Gly-Phe-Leu-OH; oil control polypeptide-2: Pal-Tyr-(D) Ala-Gly-Phe-Leu-OH; Oil-controlled polypeptide-3: Pal-Leu-Lys-Thr-Arg-Asn-OH;

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Abstract

The present invention provides a group of oil-controlling polypeptide structures, preparation methods and application methods. The sequences of the oil-controlling polypeptides are Pal-Tyr-Gly-Gly-Phe-Leu-OH, Pal-Tyr-(D)Ala-Gly-Phe-Leu-OH and Pal-Leu-Lys-Thr-Arg-Asn-OH, respectively. The 5α-reductase inhibition rates of the three polypeptides at a concentration of 0.1% are 39.00%, 30.94% and 40.31%, respectively. The application forms include but are not limited to applications in daily chemicals, and the daily chemicals are selected from oil-control essences, oil-control creams, oil-control masks, oil-control scalp essences, oil-control shampoos, and acne-removing essences; the application method in daily chemical products is to disperse the oil-controlling polypeptides in solvents such as glycerol, propylene glycol, and butylene glycol and then add them to daily chemical products. The prepared oil-controlling polypeptides have excellent oil-control effects when used in oil-controlling essences or oil-controlling shampoo products.
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Description

Technical Field

[0001] The invention relates to the synthesis and application of a group of peptides, belonging to the technical field of cosmetics, and in particular to a peptide capable of regulating sebum secretion, a synthesis method and application thereof. Background Art

[0002] Sebaceous glands are a type of multi-acinar holocereal tissue distributed throughout the skin of the entire body except the palms and soles of the feet, with the highest density on the scalp and face. Normal lipids on the skin surface can act as a barrier, moisturizing the skin, resisting infection and maintaining the balance of bacteria on the human skin surface. Excessive secretion of sebum by sebaceous glands can cause excessive oil production in the skin, affecting the beauty of the face and hair, and may also promote the development of acne or other diseases.

[0003] Chinese Patent 2020110294878 published "A plant extract composition with multi-target scalp oil control and anti-dandruff effects, its preparation method and scalp care composition". The composition is composed of 20-40% camellia seed extract, 15-25% tea bran polysaccharide, 10-30% citrus peel extract, 10-30% eucalyptus extract, and 1-20% Sophora flavescens extract. It achieves multi-target oil control and dandruff removal through four different pathways (inhibiting microbial lipase, inhibiting Malassezia B-carbonic anhydrase, inhibiting 5a-reductase in scalp cells, and inhibiting Propionibacterium acnes).

[0004] Peptides are the core ingredients that have won the Nobel Prize many times. Due to their definite structure, clear mechanism of efficacy, strong efficacy, and low effective dosage (generally only a few to several hundred ppm are needed to achieve significant effects), beauty peptides with different functions such as anti-wrinkle, whitening, moisturizing, anti-oxidation, and repair have been widely developed and applied. Chinese patent CN 107325157B discloses decapeptides and nonapeptides that can regulate sebum secretion. The amino acid sequences of the two peptides are distributed as Ser-Val-Ala-Lys-Arg-Glu-Cys-Arg-Asp-Gln and Glu-His-Gly-Pro-Phe-Asp-Ala-Gln-Pro.

[0005] Although the prior art has developed polypeptides with sebum regulating properties, they are not suitable for application in cosmetic products due to their long amino acid sequences, high production costs and low yields, and poor hydrolysis resistance.

[0006] Therefore, it is necessary to develop polypeptide raw materials with cost advantages, efficacy advantages and stable application advantages in cosmetic formulas to provide solutions to solve oily face and head. Summary of the invention

[0007] In order to overcome the deficiencies of the prior art, the purpose of the present invention is to provide a peptide that can regulate sebum secretion. The prepared oil-controlling polypeptide has excellent oil-controlling effect when used in oil-controlling essence or oil-controlling shampoo products.

[0008] The technical solution of the present invention is:

[0009] In the first aspect, the present invention provides three oil-controlling polypeptides with excellent performance, and the oil-controlling polypeptides include:

[0010] Oil Control Peptide-1:

[0011] The sequence of oil-controlling polypeptide-1 is: Pal-Tyr-Gly-Gly-Phe-Leu-OH;

[0012] The structural formula of oil-controlling polypeptide-1 is as follows:

[0013]

[0014] Oil Control Peptide-2:

[0015] The sequence of oil-controlling polypeptide-2 is: Pal-Tyr-(D)Ala-Gly-Phe-Leu-OH;

[0016] The structural formula of oil-controlling polypeptide-2 is as shown in Formula II:

[0017]

[0018] Oil-control peptide-3:

[0019] The sequence of oil-controlling polypeptide-3 is: Pal-Leu-Lys-Thr-Arg-Asn-OH;

[0020] The structural formula of oil-controlling polypeptide-3 is as follows:

[0021]

[0022] In a second aspect, the present invention provides a method for preparing an oil-controlling polypeptide, the preparation steps of which include:

[0023] Step 1: Compound synthesis:

[0024] 2-Chlorotriphenylmethyl chloride (2-CTC resin, 1.58mmol / g loading, 4g) was weighed in a reaction tube and dichloromethane (DCM) was added to swell at room temperature for 1 hour. After the solvent was drained, the first amino acid monomer (1.5equiv) at the C-terminus and N,N-diisopropylethylamine (DIEA, 5equiv) in dichloromethane solution were added. After shaking at room temperature for 1 hour, the resin was washed with N,N-dimethylformamide (DMF) and DCM three times in sequence and drained. Subsequently, Fmoc protection was removed by adding 20% ​​piperidine / DMF solution for deprotection twice, each time for 10 minutes, and then the resin was washed with DCM and DMF three times in sequence. After drying, the second amino acid was coupled, and the activated second amino acid monomer DMF solution (including 5equiv of amino acid monomer, 4.75equiv of condensing agent HBTU and 5equiv of DIEA) was added. After shaking at room temperature for 1 hour, the resin was washed with DMF and DCM three times in sequence and drained. Repeat the above steps of Fmoc deprotection, washing, coupling, and washing until the last amino acid monomer. After all couplings are completed, perform Fmoc deprotection, wash, and drain. Then perform palmitoylation, add palmitoyl chloride (2 equiv) and DIEA (2.5 equiv) in DCM to the resin, shake at room temperature for 2 h, wash the resin 3 times with DMF and DCM in turn, and drain.

[0025] Step 2: Compound cleavage:

[0026] Add the cleavage reagent to the palmitoyl-pentapeptide resin: trifluoroacetic acid (TFA) / triisopropylsilane (TIPS) / water = 95 / 2.5 / 2.5, and shake at room temperature for 2 hours. Collect the filtrate in a centrifuge tube, wash twice with DCM and acetonitrile, and combine the filtrate. After drying most of the solvent with an air pump, add anhydrous ether to precipitate, mix thoroughly and centrifuge, and pour the supernatant.

[0027] This washing was performed three times to obtain a crude product.

[0028] Step 3: Compound purification:

[0029] The polypeptide is dissolved in a solvent such as acetonitrile, ethyl acetate, ethanol, etc., and the crude product is further purified by washing, beating or recrystallization.

[0030] The specific steps of purification are: dissolving the polypeptide in a mixed solvent of ethyl acetate and ethanol in a ratio of 2:1, heating under reflux until it is clear, leaving it at room temperature for crystallization, and filtering to obtain the final purified polypeptide.

[0031] The purity of the oil-controlling polypeptide prepared by the preparation method of the oil-controlling polypeptide provided by the present invention is greater than 98%.

[0032] In a third aspect, the present invention provides a method for applying the oil-controlling peptide in daily chemical products.

[0033] The application forms of the oil-controlling peptide provided by the present invention in daily chemical products include but are not limited to: oil-controlling essence, oil-controlling cream, oil-controlling mask, oil-controlling scalp essence, oil-controlling shampoo, acne-removing essence and other products. The application method of the oil-controlling peptide in daily chemical products is to disperse the oil-controlling peptide in a solvent such as glycerin, propylene glycol, butylene glycol, etc. and then add it to the daily chemical product.

[0034] The cosmetic is an oil-control essence;

[0035] The oil control essence contains the following percentage components:

[0036] Phase A: water balance; EDTA-2Na 0.1%; sodium hyaluronate 0.04%; sodium acrylate copolymer 0.3%; xanthan gum 0.1%; arginine 0.08%;

[0037] Phase B: Phenoxyethanol 0.4%; Hexylene glycol 0.8%; Ethylhexylglycerin 0.1%;

[0038] Phase C: Propylene glycol 2%; Oil-controlling polypeptide-1 or Oil-controlling polypeptide-2 or Oil-controlling polypeptide-3;

[0039] The percentage content of the oil-controlling polypeptide is: oil-controlling polypeptide-1 0.2%, or oil-controlling polypeptide-2 0.15%, or oil-controlling polypeptide-3 0.1%;

[0040] The steps for preparing the oil control essence are as follows:

[0041] Add phase A to the reaction container in sequence, stir and disperse, heat to 75°C and keep stirring for 15 to 30 minutes; after phase A is completely dispersed, add phase B, stir and cool to below 40°C; add phase C and mix evenly, stir and disperse evenly to obtain the final oil-control essence.

[0042] The daily chemical product is an oil-control shampoo;

[0043] The oil control shampoo contains the following percentage components:

[0044] Phase A: Water 63.23%; Guar Hydroxypropyltrimonium Chloride 0.2%; Polyquaternium-11 0.2%; Citric Acid 0.07%;

[0045] Phase B: Lauryl Hydroxysultaine 15%; Sodium Laureth Sulfate 14%;

[0046] Phase C: Polysilicone Quaternium-16 1.5%; Phenoxyethanol 0.5%; Sodium Benzoate 0.5%; Fragrance 0.6%; Salt 1%;

[0047] Phase D: Propylene glycol 3%; Oil-controlling polypeptide-1 or oil-controlling polypeptide-2 or oil-controlling polypeptide-3 0.3%;

[0048] The preparation steps of the oil-control shampoo are as follows:

[0049] Add phase A to the reaction container in sequence, stir and disperse, heat to 75°C and keep stirring for 15 to 20 minutes; after phase A is completely dispersed, add phase B in sequence, keep stirring for 20 minutes; after phase A and phase B are evenly mixed, cool to 40°C, add phase C, stir and disperse; add pre-mixed phase D, stir and disperse evenly to obtain the final oil-control shampoo.

[0050] The technical effects and beneficial effects of the present invention are as follows:

[0051] 1) The present invention designs and develops a group of oil-controlling peptides with excellent performance, including: oil-controlling peptide-1: Pal-Tyr-Gly-Gly-Phe-Leu-OH; oil-controlling peptide-2: Pal-Tyr-(D)Ala-Gly-Phe-Leu-OH; oil-controlling peptide-3: Pal-Leu-Lys-Thr-Arg-Asn-OH;

[0052] 2) The present invention provides a method for preparing an oil-controlling peptide, wherein the purity of the prepared oil-controlling peptide is greater than 98%;

[0053] 3) The oil-control peptide designed and developed by the present invention has an excellent 5α-reductase inhibition effect. The 5α-reductase inhibition rate of 0.1% oil-control peptide 1 is as high as 39.00%, the 5α-reductase inhibition rate of 0.1% oil-control peptide 2 is as high as 30.94%, and the 5α-reductase inhibition rate of 0.1% oil-control peptide 3 is as high as 40.31%;

[0054] 4) The sebum secretion inhibition rate of the oil-control essence containing the oil-control peptide of the present invention is greater than 30%. BRIEF DESCRIPTION OF THE DRAWINGS

[0055] Figure 1 This is the LCMS spectrum of oil-controlling polypeptide-1;

[0056] Figure 2 This is the LCMS spectrum of oil-controlling polypeptide-2;

[0057] Figure 3 This is the LCMS spectrum of oil-controlling polypeptide-3;

[0058] Figure 4 This is a comparison chart of 5α-reductase inhibition rate. DETAILED DESCRIPTION

[0059] In order to make the above-mentioned objects, features and advantages of the present invention more obvious and easy to understand, the specific embodiments of the present invention are described in detail below.

[0060] As used herein, the term "prepared from" is synonymous with "comprising." As used herein, the terms "comprising," "including," "having," "containing," or any other variation thereof, are intended to cover a non-exclusive inclusion. For example, a composition, process, method, article, or apparatus that comprises the listed elements is not necessarily limited to only those elements but may include other elements not expressly listed or inherent to such composition, process, method, article, or apparatus.

[0061] When amount, concentration or other value or parameter is expressed as range, preferred range or a series of upper preferred value and lower preferred value limit range, this should be understood as specifically disclosing all ranges formed by any pairing of any range upper limit or preferred value and any range lower limit or preferred value, regardless of whether the range is disclosed separately. For example, when disclosing range "1 to 5", described range should be interpreted as including range "1 to 4", "1 to 3", "1 to 2", "1 to 2 and 4 to 5", "1 to 3 and 5" etc. When numerical range is described in this article, unless otherwise stated, the range is intended to include its end value and all integers and fractions within the range.

[0062] Many specific details are set forth in the following description to facilitate a full understanding of the present invention. However, the present invention can be implemented in many other ways than those described herein, and those skilled in the art can make similar improvements without violating the connotation of the present invention, so the present invention is not limited to the specific embodiments disclosed below.

[0063] Examples 1 to 3

[0064] The present invention provides three oil-controlling polypeptides, and the sequences and structures of the three oil-controlling polypeptides are:

[0065] Oil Control Peptide-1:

[0066] The sequence of oil-controlling polypeptide-1 is: Pal-Tyr-Gly-Gly-Phe-Leu-OH;

[0067] The structural formula of oil-controlling polypeptide-1 is as follows:

[0068]

[0069] The LCMS spectrum of oil-controlling peptide-1 is as follows Figure 1 shown.

[0070] Oil Control Peptide-2:

[0071] The sequence of oil-controlling polypeptide-2 is: Pal-Tyr-(D)Ala-Gly-Phe-Leu-OH;

[0072] The structural formula of oil-controlling polypeptide-2 is as shown in Formula II:

[0073]

[0074] The LCMS spectrum of oil-controlling peptide-2 is as follows Figure 2 shown.

[0075] Oil-control peptide-3:

[0076] The sequence of oil-controlling polypeptide-3 is: Pal-Leu-Lys-Thr-Arg-Asn-OH;

[0077] The structural formula of oil-controlling polypeptide-3 is as follows:

[0078]

[0079] The LCMS spectrum of oil-control peptide-3 is as follows Figure 3 shown.

[0080] The oil-controlling polypeptide is prepared by the following steps:

[0081] Step 1: Synthesis of compounds

[0082] 2-Chlorotriphenylmethyl chloride (2-CTC resin, 1.58mmol / g loading, 4g) was weighed in a reaction tube and dichloromethane (DCM) was added to swell at room temperature for 1 hour. After the solvent was drained, the first amino acid monomer (1.5equiv) at the C-terminus and N,N-diisopropylethylamine (DIEA, 5equiv) in dichloromethane solution were added. After shaking at room temperature for 1 hour, the resin was washed with N,N-dimethylformamide (DMF) and DCM three times in sequence and drained. Subsequently, Fmoc protection was removed by adding 20% ​​piperidine / DMF solution for deprotection twice, each time for 10 minutes, and then the resin was washed with DCM and DMF three times in sequence. After drying, the second amino acid was coupled, and the activated second amino acid monomer DMF solution (including 5equiv of amino acid monomer, 4.75equiv of condensing agent HBTU and 5equiv of DIEA) was added. After shaking at room temperature for 1 hour, the resin was washed with DMF and DCM three times in sequence and drained. Repeat the above steps of Fmoc deprotection, washing, coupling, and washing until the last amino acid monomer. After all couplings are completed, perform Fmoc deprotection, wash, and drain. Then perform palmitoylation, add palmitoyl chloride (2 equiv) and DIEA (2.5 equiv) in DCM to the resin, shake at room temperature for 2 h, wash the resin 3 times with DMF and DCM in turn, and drain.

[0083] Step 2: Compound cleavage:

[0084] Add the cleavage reagent to the palmitoyl-pentapeptide resin: trifluoroacetic acid (TFA) / triisopropylsilane (TIPS) / water = 95 / 2.5 / 2.5, and shake at room temperature for 2 hours. Collect the filtrate in a centrifuge tube, wash twice with DCM and acetonitrile, and combine the filtrate. After drying most of the solvent with an air pump, add anhydrous ether to precipitate, mix thoroughly and centrifuge, pour the supernatant, and wash 3 times to obtain a crude product.

[0085] Step 3: Compound purification:

[0086] The polypeptide was dissolved in a mixed solvent of ethyl acetate and ethanol in a ratio of 2:1, heated under reflux until clarified, left at room temperature for crystallization, and filtered to obtain the final purified polypeptide.

[0087] Application Examples 1 to 3 and Comparative Examples 1 to 3

[0088] The preparation method of the product containing the oil-controlling polypeptide of the present invention is as follows:

[0089] Preparation of oil-control essence containing oil-control peptides:

[0090] The application examples 1 to 3 and comparative examples 1 to 3 of the oil control essence were prepared according to the addition ratios in Table 1, and the preparation steps were as follows:

[0091] 1) Add phase A into the reaction vessel in sequence, stir and disperse, raise the temperature to 75°C and keep stirring for 15 to 30 minutes;

[0092] 2) After phase A is completely dispersed, add phase B and stir to cool down to below 40°C;

[0093] 3) Add the mixed phase C and stir to disperse evenly to obtain the final oil-control essence.

[0094] Table 1 Oil Control Essence Application Examples 1-3 and Comparative Examples 1-3

[0095]

[0096]

[0097] Application Examples 4 to 6 and Comparative Examples 4 to 6

[0098] Preparation of shampoo containing oil-control peptides:

[0099] Application Examples 4 to 6 and Comparative Examples 4 to 6 of the oil control shampoo were prepared according to the addition ratios in Table 2, and the preparation steps were as follows:

[0100] 1) Add phase A into the reaction vessel in sequence, stir and disperse, heat to 75°C and keep stirring for 15 to 20 minutes;

[0101] 2) After phase A is completely dispersed, add phase B in sequence and stir for 20 minutes;

[0102] 3) After phase A and phase B are evenly mixed, cool to 40°C and add phase C, stirring and dispersing;

[0103] 4) Add the pre-mixed phase D and stir to disperse evenly to obtain the final oil-control shampoo.

[0104] Table 2 Oil Control Shampoo Examples and Comparative Examples

[0105]

[0106] Effect Test Example 1

[0107] Test method for 5α-reductase inhibition rate:

[0108] 5a-reductase catalyzes the conversion of testosterone into dihydrotestosterone with the participation of reduced coenzyme II. If there is a 5α-reductase inhibitor, this reaction process can be inhibited to a certain extent. Since reduced coenzyme II has characteristic absorption at a wavelength of 340nm, the characteristic absorption of oxidized coenzyme II generated after participating in the reaction disappears at a wavelength of 340nm. Using an ultraviolet spectrophotometer to measure can reflect whether a certain substance has an inhibitory effect on 5a-reductase and the extent of the inhibitory effect.

[0109] Determination of blank control: add 4 μL testosterone T (20.747 mmol / L), 6 μL 5α-reductase (176 mg / mL), 60 μL phosphate buffer (pH = 7.4), and 30 μL reduced coenzyme II into the reaction tube, measure the absorbance after mixing, incubate at 37°C for 60 min, measure the absorbance after deducting the blank decrease background value of reduced coenzyme II, and measure the blank decrease value (ΔA 0 )

[0110] Determination of inhibitors: 4 μL testosterone T (20.747 mmol / L), 6 μL 5α-reductase (176 mg / mL), 5 μL sample to be tested (see Table 3), 55 μL phosphate buffer (pH = 7.4), and 30 μL reduced coenzyme II were added to the reaction tube, and the absorbance was measured after mixing. After incubation at 37°C for 60 min, the absorbance was measured, and the blank reduction background value of reduced coenzyme II was deducted to measure the reduction value of the sample (ΔA n The experiment was repeated 3 times, with 3 parallel samples each time. The inhibition rate was calculated according to the inhibition rate formula: I (%) = (ΔA 0 -ΔA n ) / ΔA 0 ×100%.

[0111] The test structure and results of 5α-reductase inhibition rate are shown in Table 3 and Figure 4 Shown

[0112] Table 3. Table of samples to be tested and 5α-reductase inhibition rate

[0113]

[0114] From Table 3 and Figure 4 It can be seen that the effect of the oil-controlling polypeptide of the present invention is far better than that of the negative control group. Under the condition of an added concentration of 0.1%, the 5α-reductase inhibition rate of the oil-controlling polypeptide of the present invention is very close to that of the positive control, which indicates that the oil-controlling polypeptide of the present invention has an excellent 5α-reductase inhibition effect.

[0115] Effect Test Example 2

[0116] Essence oil control effect test method:

[0117] 1) Volunteers with oily or mixed skin (aged 18 to 40) were divided into 9 groups, with 10 participants in each group (5 males and 5 females);

[0118] 2) Clean the subject's face with the same facial cleanser in a constant temperature and humidity environment;

[0119] 3) In groups 1 to 6, a blank control sample was applied on the left side of the forehead, and samples of application examples 1 to 3 and comparative examples 1 to 3 were applied on the right side of the forehead, respectively, with a sample amount of 2±0.2 g;

[0120] 4) The samples of Comparative Examples 1 to 3 were applied to the left side of the foreheads of Groups 7 to 9, and the samples of Application Examples 1 to 3 were applied to the right side of the foreheads, respectively, with a sample amount of 2±0.2 g;

[0121] 5) Utilize MB560 Grease Tester (CK, Germany) was used to measure the amount of grease on the left and right sides of the forehead at 1 hour, 6 hours, and 12 hours. Three sets of data were measured at each symmetrical part and the average value was calculated.

[0122] 6) Calculate the oil reduction rate according to the oil reduction rate calculation formula: Oil reduction rate = (oil amount on the left side of the forehead - oil amount on the right side of the forehead) / oil amount on the left side of the forehead × 100%.

[0123] The test results of oil control essence are shown in Table 4:

[0124] Table 4 Test results of oil control essence (people)

[0125]

[0126] In Table 4, the oil reduction rate of most people in Group 1, Group 2, and Group 3 was greater than 10%, and more than half of the people had an oil reduction rate greater than 30% at the 12th hour. This shows that Application Example 1, Application Example 2, and Application Example 3 have excellent oil control effects. In Table 4, the oil reduction rate of most people in Group 4, Group 5, and Group 6 was less than 10%, which shows that the comparative example also has a certain oil control effect, but the oil control effect is relatively weak.

[0127] The population of Group 7, Group 8 and Group 9 mainly concentrated in the range of oil reduction rate of 10-30%, which shows that the oil control effect of the application example is much better than that of the comparative example.

[0128] Effect Test Example 3

[0129] Testing method for oil control effect of shampoo:

[0130] 1) Volunteers with oily scalp (aged 18 to 40) were divided into 9 groups, with 10 people in each group (5 males and 5 females);

[0131] 2) A dedicated hair washing staff will conduct a half-head washing test on the volunteers in a constant temperature and humidity environment;

[0132] 3) A blank control was used on the left side of the head of Groups 1 to 6, and the samples of Application Examples 4 to 6 and Comparative Examples 4 to 6 were used on the right side of the head, with a sample amount of 8±0.5 g. The left and right heads were cleaned and massaged for 3 minutes, then rinsed and dried;

[0133] 4) The samples of Comparative Examples 4 to 6 were used on the left side of the head of Groups 7 to 9, and the samples of Application Examples 4 to 6 were used on the right side of the head, with a sample amount of 8±0.5 g. The left and right heads were cleaned and massaged for 3 minutes respectively, then rinsed and dried;

[0134] 5) Utilize MB560 Grease Tester (CK Company, Germany) measures the grease content 24 hours after the first, second and third shampooing. Three sets of data are measured at each symmetrical part and the average value is calculated. The time interval between the first, second and third shampooing is required to be one day. For example, if you wash your hair at 8 o'clock this morning, the data will be tested at 8 o'clock the next day, and you can wash your hair for the second time after the data is measured.

[0135] 6) Calculate the grease reduction rate according to the grease reduction rate calculation formula: grease reduction rate = (grease amount on the left side of the head - grease amount on the right side of the head) / grease amount on the left side of the head × 100%.

[0136] The test results of the oil control shampoo are shown in Table 5.

[0137] Table 5 Test results of oil control shampoo (people)

[0138]

[0139]

[0140] In Table 5, the 1st, 2nd and 3rd groups of people are mainly concentrated in the range of 0-10% and 10-30% of oil reduction rate. After the third shampooing, the oil reduction rate of a small number of people will be in the range of 30-50%, while the 4th, 5th and 6th groups of people are all concentrated in the range of 0-10% of oil reduction rate. Combined with the comparative usage data of the application examples and the comparative examples of the 7th, 8th and 9th groups, it can be seen that the oil reduction rate of the application examples is better than that of the comparative example, and after the third use, more than half of the people have an oil suppression rate greater than 10%.

[0141] The above description is only a preferred embodiment of the present invention and does not limit the present invention in any form. Therefore, any simple modification, equivalent change and modification made to the above embodiment according to the technical essence of the present invention without departing from the technical solution of the present invention still fall within the scope of the technical solution of the present invention.

Claims

1. Use of a polypeptide capable of regulating sebum secretion in the preparation of an oil-control shampoo product, characterized in that: The oil-control shampoo product is an oil-control shampoo; its application method is to disperse the oil-control polypeptide into glycerin, propylene glycol, and butylene glycol solvents, and then add the resulting mixture into the oil-control shampoo product; The polypeptide that regulates sebum secretion is oil-control polypeptide-3; Among them, the sequence of oil-controlling polypeptide-3 is: Pal-Leu-Lys-Thr-Arg-Asn-OH; The structural formula of oil-controlling polypeptide-3 is as follows:

2. The use according to claim 1, characterized in that: The oil control shampoo contains the following percentage components: Phase A: Water 63.23%; Guar Hydroxypropyltrimonium Chloride 0.2%; Polyquaternium-11 0.2%; Citric Acid 0.07%; Phase B: Lauryl Hydroxysultaine 15%; Sodium Laureth Sulfate 14%; Phase C: Polysilicone Quaternium-16 1.5%; Phenoxyethanol 0.5%; Sodium Benzoate 0.5%; Fragrance 0.6%; Salt 1%; Phase D: Propylene glycol 3%; Oil-controlling polypeptide-3 0.3%; The preparation steps of the oil-control shampoo are as follows: Add phase A to the reaction container in sequence, stir and disperse, heat to 75°C and keep stirring for 15 to 20 minutes; after phase A is completely dispersed, add phase B in sequence, keep stirring for 20 minutes; after phase A and phase B are evenly mixed, cool to 40°C, add phase C, stir and disperse; add pre-mixed phase D, stir and disperse evenly to obtain the final oil-control shampoo.

Citation Information

Patent Citations

  • Peptides that regulate sebum secretion and cosmetics containing them.

    CN107325157B

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    CN106999401A

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    CN110105432A

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