CN116919839A - Even-brightness stable synergistic component and collagen multiple peptide combined component prepared from same - Google Patents
Even-brightness stable synergistic component and collagen multiple peptide combined component prepared from same Download PDFInfo
- Publication number
- CN116919839A CN116919839A CN202311127291.6A CN202311127291A CN116919839A CN 116919839 A CN116919839 A CN 116919839A CN 202311127291 A CN202311127291 A CN 202311127291A CN 116919839 A CN116919839 A CN 116919839A
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- Prior art keywords
- collagen
- polypeptide
- synergistic
- component
- palmitoyl
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
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- 230000002195 synergetic effect Effects 0.000 title claims abstract description 51
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- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 77
- 239000000203 mixture Substances 0.000 claims abstract description 57
- 239000000284 extract Substances 0.000 claims abstract description 21
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- BYUQATUKPXLFLZ-UIOOFZCWSA-N CCCCCCCCCCCCCCCC(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(O)=O)CC1=CN=CN1 Chemical compound CCCCCCCCCCCCCCCC(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(O)=O)CC1=CN=CN1 BYUQATUKPXLFLZ-UIOOFZCWSA-N 0.000 claims abstract description 12
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Classifications
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- A—HUMAN NECESSITIES
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- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/58—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds containing atoms other than carbon, hydrogen, halogen, oxygen, nitrogen, sulfur or phosphorus
- A61K8/585—Organosilicon compounds
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
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Abstract
The invention belongs to the technical field of daily chemical raw materials and cosmetics, and discloses a uniform-brightness stable synergistic component and a collagen multiple peptide combination component prepared by the same. The collagen multiple peptide composition comprises palmitoyl tripeptide-1, palmitoyl pentapeptide-4, acetyl hexapeptide-8, palmitoyl tetrapeptide-7, acetyl tetrapeptide-5, a crocus sativus extract, a chondrus crispus extract, cyclopentamethyl siloxane, polypeptide modified cyclosiloxane, a uniform brightness stabilizing synergistic component and an effective component of hydrolyzed collagen. The polypeptide modified cyclosiloxane brightening and stabilizing synergistic component synergistic polypeptide and specific plant extract component can obviously enhance the anti-aging and repairing effects of the composition. Through the multi-component synergistic effect, the obtained collagen multiple peptide composition has remarkably improved soft skin feel, good stability and formula compatibility.
Description
Technical Field
The invention belongs to the technical field of daily chemical raw materials and cosmetics, and particularly relates to a brightening stable synergistic component and a collagen multiple peptide combined component prepared by the same.
Background
The polypeptide has the effects of whitening, resisting oxidation, diminishing inflammation and refreshing skin, contains a large amount of collagen, has very strong penetrability to the skin, can activate epidermal cells, and has the effects of skin care and beauty; the polypeptide also has the effects of removing wrinkles and resisting aging, and can directly permeate into the dermis layer of the skin, promote the metabolism of cells, smooth wrinkles and delay skin aging. Therefore, the polypeptide is widely used for skin care products or cosmetic raw materials, and the efficacy of the polypeptide is synergistically promoted to be exerted through a specific formula.
As disclosed in patent CN 113893184A, a polypeptide whitening and freckle removing composition, a skin care product and a preparation method thereof are disclosed, and whitening effects are achieved by adding whitening polypeptides (a mixture of nonapeptide-1, glutathione, carnosine and hexapeptide-2) which are easy to be absorbed by skin, and whitening components such as acetyl tyrosine, VC ethyl ether, arbutin, tocopheryl acetate and the like, and inhibiting melanin production by melanocytes and transfer of the generated melanin in the deep layer of the skin to the surface layer of the skin through multiple mechanisms.
Also, as disclosed in patent CN 111686048A, an anti-aging essence and a preparation method thereof are disclosed, and by adding a plurality of plant extract components to cooperate with polypeptide components of tripeptide, hall palmitoyl tripeptide-1, palmitoyl tetrapeptide-7, eyeliss dipeptide-2 and palmitoyl tetrapeptide-7, a good anti-aging effect is obtained, skin elasticity is improved, wrinkles are reduced, and the anti-aging essence is safe, efficient, almost free from adverse reactions and has a certain freckle removing effect.
However, the pure polypeptide component and plant extract component have poor moisturizing effect, and direct use can lead to skin tightness and poor skin feel, and the corresponding skin care and beauty cannot be effectively exerted. The corresponding effects are usually improved by the addition of different emollient components. In addition, the solubility of the various polypeptide components and plant extract components varies, and it is often necessary to add a certain amount of surfactant component to promote system stability, but this results in a complex composition of the components of the composition with increased potential for irritation.
Disclosure of Invention
Aiming at the defects and shortcomings of the prior art, the primary purpose of the invention is to provide a preparation method of polypeptide modified cyclosiloxane uniform brightness stable synergistic components.
The invention also aims to provide the polypeptide modified cyclosiloxane uniform brightness stable synergistic component prepared by the method.
It is still another object of the present invention to provide a collagen multipeptide composition prepared from the above-mentioned brightness-stabilizing synergistic composition.
It is still another object of the present invention to provide a method for producing the above collagen multipeptide composition.
The invention aims at realizing the following technical scheme:
a preparation method of polypeptide modified cyclosiloxane uniform brightness stable synergistic components comprises the following preparation steps:
adding cyclic hydrogen-containing polysiloxane and allyl glycidyl ether into an alcohol solvent, heating to 60-90 ℃, adding chloroplatinic acid catalyst for reaction, and obtaining epoxy modified cyclosiloxane; then adding polypeptide compound to continue stirring reaction, and removing alcohol solvent and low-boiling-point substances in vacuum after the reaction is completed to obtain polypeptide modified cyclosiloxane uniform brightness stable synergistic component.
Further, the cyclic hydrogen-containing polysiloxane refers to at least one of 2,4,6, 8-tetramethyl cyclotetrasiloxane (hydrogen-containing D4) or 2,4,6,8, 10-pentamethyl cyclopentasiloxane (hydrogen-containing D5). Preferably, the cyclic hydrogen-containing polysiloxane is hydrogen-containing D5, and the polypeptide modified cyclosiloxane brightening, stabilizing and synergistic component is polypeptide modified cyclopenta-dimethyl siloxane.
Further, the molar ratio of the cyclic hydrogen-containing polysiloxane to the allyl glycidyl ether is 1:3-5.
Further, the alcohol solvent is one or a mixed solvent of more than two of ethanol, propanol and isopropanol.
Further, the polypeptide compound is at least one selected from collagen tripeptide, palmitoyl tetrapeptide, palmitoyl pentapeptide and acetyl hexapeptide.
Further, the addition amount of the polypeptide compound is 1 to 1.2 times of the molar amount of the allyl glycidyl ether.
The polypeptide modified cyclosiloxane brightening stable synergistic component is prepared by the method.
The collagen multiple peptide composition prepared from the uniform brightness stable synergistic component comprises the following raw materials:
water, palmitoyl tripeptide-1, palmitoyl pentapeptide-4, acetyl hexapeptide-8, palmitoyl tetrapeptide-7, acetyl tetrapeptide-5, crocus sativus (HYPNEA MUSCIFORMIS) extract, CHONDRUS CRISPUS (CHONDRUS CRISPUS) extract, cyclopentadimethicone, polypeptide modified cyclosiloxane, a lightening stabilizing synergistic ingredient, and hydrolyzed collagen (HYDROLYZED COLLAGEN).
Further, the mass percentages of the raw materials are as follows:
the preparation method of the collagen multiple peptide composition comprises the following preparation steps:
sequentially adding palmitoyl tripeptide-1, palmitoyl pentapeptide-4, acetyl hexapeptide-8, palmitoyl tetrapeptide-7, acetyl tetrapeptide-5 and hydrolyzed collagen into water to dissolve uniformly, then adding polypeptide modified cyclosiloxane to uniformly lighten, stabilize and synergistic components, and adding the crocus sativus extract and the chondrus crispus extract to stir and dissolve uniformly, and finally adding the cyclopentamethylsiloxane to stir and mix uniformly to obtain the collagen multiple peptide composition.
Compared with the prior art, the invention has the beneficial effects that:
(1) The polypeptide modified cyclosiloxane light-homogenizing stable synergistic component synergistic polypeptide and the specific plant extract component are adopted, so that the anti-aging and repairing effects of the composition can be remarkably enhanced.
(2) The invention adopts the cyclopenta-dimethicone to promote the skin feel of the composition, and simultaneously utilizes the surface activity of polypeptide modified cyclosiloxane to lighten, stabilize and synergize the components to improve the dispersion stability of the components under an aqueous system, and the obtained composition has better stability and compatibility.
Detailed Description
The present invention will be described in further detail with reference to examples, but embodiments of the present invention are not limited thereto.
Example 1
The collagen multiple peptide composition comprises the following raw materials in percentage by mass:
34% water, 15% palmitoyl tripeptide-1, 15% palmitoyl pentapeptide-4, 15% acetyl hexapeptide-8, 5% palmitoyl tetrapeptide-7, 2% acetyl tetrapeptide-5, 3% crock (HYPNEA MUSCIFORMIS) extract, 3% CHONDRUS CRISPUS (CHONDRUS CRISPUS) extract, 3% cyclopentadimethicone, 3% polypeptide modified cyclosiloxane brightness stabilizing synergistic component, 2% hydrolyzed collagen (HYDROLYZED COLLAGEN).
The preparation method of the collagen multiple peptide composition comprises the following steps: weighing the components according to the mass percentage, sequentially adding the palmitoyl tripeptide-1, the palmitoyl pentapeptide-4, the acetyl hexapeptide-8, the palmitoyl tetrapeptide-7, the acetyl tetrapeptide-5 and the hydrolyzed collagen into water for uniform dissolution, then adding the polypeptide modified cyclosiloxane for uniform brightness and stable synergistic component, the crocus sativus extract and the chondrus crispus extract for uniform stirring and dissolution, and finally adding the cyclopentamethylsilicone for uniform stirring and mixing to obtain the collagen multiple peptide composition.
The polypeptide modified cyclosiloxane uniform brightness stable synergistic component is prepared by the following method:
adding 2,4,6,8, 10-pentamethyl cyclopentasiloxane (containing hydrogen D5) and allyl glycidyl ether into an isopropanol solvent, wherein the addition amount of the allyl glycidyl ether is 5 times of the molar amount of the hydrogen D5, heating to 75-80 ℃, adding 50ppm chloroplatinic acid catalyst, stirring and reacting for 4 hours, and detecting that the content of active hydrogen in a reaction product is reduced to below 0.05%, thus obtaining epoxy modified cyclosiloxane; then adding collagen tripeptide with the molar weight of allyl glycidyl ether being 1.1 times, continuously stirring and reacting for 2 hours, and removing isopropanol solvent and low-boiling substances in vacuum after the reaction is finished to obtain the polypeptide modified cyclosiloxane even, bright, stable and synergistic component.
Example 2
The collagen multiple peptide composition comprises the following raw materials in percentage by mass:
45% water, 10% palmitoyl tripeptide-1, 10% palmitoyl pentapeptide-4, 10% acetyl hexapeptide-8, 3% palmitoyl tetrapeptide-7, 1% acetyl tetrapeptide-5, 5% crock (HYPNEA MUSCIFORMIS) extract, 5% CHONDRUS CRISPUS (CHONDRUS CRISPUS) extract, 5% cyclopentadimethicone, 5% polypeptide modified cyclosiloxane brightness stabilizing synergistic component, 1% hydrolyzed collagen (HYDROLYZED COLLAGEN).
The preparation method of the collagen multiple peptide composition comprises the following steps: weighing the components according to the mass percentage, sequentially adding the palmitoyl tripeptide-1, the palmitoyl pentapeptide-4, the acetyl hexapeptide-8, the palmitoyl tetrapeptide-7, the acetyl tetrapeptide-5 and the hydrolyzed collagen into water for uniform dissolution, then adding the polypeptide modified cyclosiloxane for uniform brightness and stable synergistic component, the crocus sativus extract and the chondrus crispus extract for uniform stirring and dissolution, and finally adding the cyclopentamethylsilicone for uniform stirring and mixing to obtain the collagen multiple peptide composition.
The polypeptide modified cyclosiloxane uniform brightness stable synergistic component is prepared by the following method:
adding 2,4,6, 8-tetramethyl cyclotetrasiloxane (containing hydrogen D4) and allyl glycidyl ether into an ethanol solvent, wherein the addition amount of the allyl glycidyl ether is 4 times of the molar amount of the hydrogen D4, heating to 75-80 ℃, adding 50ppm chloroplatinic acid catalyst, stirring and reacting for 5 hours, and detecting that the content of active hydrogen in a reaction product is reduced to below 0.05%, thus obtaining epoxy modified cyclosiloxane; then adding acetyl hexapeptide-39 with the molar weight of 1 time of allyl glycidyl ether, continuously stirring and reacting for 2 hours, and removing ethanol solvent and low-boiling substances in vacuum after the reaction is finished to obtain the polypeptide modified cyclosiloxane even, bright, stable and synergistic component.
Example 3
The collagen multiple peptide composition comprises the following raw materials in percentage by mass:
18% water, 20% palmitoyl tripeptide-1, 20% palmitoyl pentapeptide-4, 20% acetyl hexapeptide-8, 8% palmitoyl tetrapeptide-7, 3% acetyl tetrapeptide-5, 2% extract of crocus sativus (HYPNEA MUSCIFORMIS), 2% extract of Chondrus CRISPUS (CHONDRUS CRISPUS), 2% cyclopentamethylsiloxane, 2% polypeptide modified cyclosiloxane, a lightening stability enhancing component, 3% hydrolyzed collagen (HYDROLYZED COLLAGEN).
The preparation method of the collagen multiple peptide composition comprises the following steps: weighing the components according to the mass percentage, sequentially adding the palmitoyl tripeptide-1, the palmitoyl pentapeptide-4, the acetyl hexapeptide-8, the palmitoyl tetrapeptide-7, the acetyl tetrapeptide-5 and the hydrolyzed collagen into water for uniform dissolution, then adding the polypeptide modified cyclosiloxane for uniform brightness and stable synergistic component, the crocus sativus extract and the chondrus crispus extract for uniform stirring and dissolution, and finally adding the cyclopentamethylsilicone for uniform stirring and mixing to obtain the collagen multiple peptide composition.
The polypeptide modified cyclosiloxane uniform brightness stable synergistic component is prepared by the following method:
adding 2,4,6,8, 10-pentamethyl cyclopentasiloxane (containing hydrogen D5) and allyl glycidyl ether into a mixed solvent of ethanol and isopropanol, wherein the addition amount of the allyl glycidyl ether is 5 times of the molar amount of the hydrogen D5, heating to 75-80 ℃, adding 50ppm chloroplatinic acid catalyst, stirring and reacting for 3 hours, and detecting that the active hydrogen content in a reaction product is reduced to below 0.05%, thus obtaining epoxy modified cyclosiloxane; then adding palmitoyl pentapeptide-4 with the molar weight of allyl glycidyl ether being 1.2 times, continuously stirring and reacting for 2 hours, and removing ethanol solvent and low-boiling substances in vacuum after the reaction is finished to obtain the polypeptide modified cyclosiloxane even, bright, stable and synergistic components.
Comparative example 1
In this comparative example, as compared with example 1, the collagen multiplex peptide composition was not added with the hook and the chondrus crispus extracts, and the remaining effective mass percentage was kept unchanged.
Comparative example 2
In this comparative example, compared with example 1, no cyclopenta-dimethicone was added to the collagen multiplex composition, and the remaining active mass percentage remained unchanged.
Comparative example 3
Compared with the comparative example 1, the polypeptide modified cyclosiloxane is not added into the collagen multi-peptide composition component, so that the composition is even, bright, stable and synergistic, and the mass percentage of the rest effective substances is kept unchanged.
Comparative example 4
Compared with the example 1, the comparative example adopts equivalent polypeptide modified linear polysiloxane to replace polypeptide modified cyclosiloxane to uniformly lighten and stabilize synergistic components, and the rest is the same.
The polypeptide modified linear polysiloxane is prepared by the following method:
adding hydrogen-containing silicone oil with hydrogen content of 0.5% (viscosity of 120mPa.s at 25 ℃) and allyl glycidyl ether into an isopropanol solvent, wherein the addition amount of the allyl glycidyl ether is 1 time of the hydrogen-containing molar weight of the hydrogen-containing silicone oil, heating to 75-80 ℃, adding 50ppm chloroplatinic acid catalyst, stirring and reacting for 4 hours, and detecting that the active hydrogen content in a reaction product is reduced to below 0.05%, thus obtaining epoxy modified polysiloxane; then adding collagen tripeptide with the molar weight of allyl glycidyl ether being 1.1 times, continuously stirring and reacting for 2 hours, and removing isopropanol solvent and low-boiling substances in vacuum after the reaction is finished to obtain the polypeptide modified linear polysiloxane.
The compositions obtained in the above examples and comparative examples were tested and test specimens were prepared according to the following basic formulation: 6% of collagen multi-peptide composition, 5% of glycerol, 3% of butanediol, 2% of 1, 2-hexanediol, 5% of squalane, 5% of C12-13 alkanol polyether-9 2%, 0.2% of carbomer, 0.1% of EDTA-2Na and 76.7% of water.
1. Safety test
The safety performance test was performed on the test samples prepared from the collagen multipeptides composition of examples 1 to 3 and comparative examples 1 to 4 as follows:
(1) Erythrocyte hemolysis assay:
preparation of erythrocyte suspensions: healthy rabbits are selected, 9mL of heart blood is taken, 1mL of 2% potassium oxalate solution is added, centrifugation is carried out, supernatant fluid is removed, 20mmol/L PBS solution is used for diluting sediment to 20mL, and the sediment is preserved at 4 ℃ for standby. Samples were selected for dilution with PBS solution to different concentrations, each sample being set with 5 concentration gradients. Taking 10mL of a dilution of a sample to be tested, adding 200 mu L of the erythrocyte suspension (controlling the final concentration of the sample to be 5, 10, 20, 50 and 100mg/mL respectively), taking distilled water as a total hemolysis control, taking a PBS solution as a negative control, gently mixing, incubating for 30min at 37 ℃, centrifuging for 10min at a rotating speed of 2000r/min, taking a supernatant, testing the absorbance (A560) of the supernatant at 560nm by using a spectrophotometer, and calculating the hemolysis rate according to the following formula:
hemolysis ratio= (experimental group a 560-negative control group a 560) ×100%/(total hemolysis control group a 560-negative control group a 560).
A standard curve of the hemolysis rate-sample concentration was drawn, and the sample concentration (HD 50, mg/L) at which 50% of the erythrocytes were hemolyzed was calculated.
(2) Protein denaturation experiment:
diluting a sample to 10g/L by using a PBS solution, taking 10mL of a dilution of the sample to be detected, adding 200 mu L of the erythrocyte suspension, taking distilled water as a blank control, taking 1mg/mL of Sodium Dodecyl Sulfate (SDS) solution as a positive control, gently mixing, incubating for 30min at 37 ℃, centrifuging for 10min at a rotating speed of 2000r/min, taking a supernatant, respectively testing absorbance A540 and A575 at 540nm and 575nm by using a spectrophotometer, and calculating a protein denaturation index (DI,%) according to the following formula:
DI＝(R1-R2)×100％/(R1-R3)；
wherein, r1=blank control group a 575/blank control group a540, r2=test group a 575/test group a540, r3=positive control group a 575/positive control group a540.
The irritation of the sample to be tested is evaluated according to the L/D value, wherein the L/D value is HD50/DI, and the irritation grading standard of the erythrocyte hemolysis experiment is as follows:
when the L/D is more than 100, classifying the mixture into non-irritant; when L/D is more than 10 and less than or equal to 100, classifying the mixture into microstimulation; when L/D is more than 1 and less than or equal to 10, classifying the mixture as mild irritation; when L/D is more than 0.1 and less than or equal to 1, grading to be moderate irritation; when L/D is less than or equal to 0.1, the classification is heavy irritation.
The results of the irritation test for each sample are shown in table 1:
TABLE 1
| Sample of | Example 1 | Example 2 | Example 3 | Comparative example 1 | Comparative example 2 | Comparative example 3 | Comparative example 4 |
| Grading | No irritation | No irritation | No irritation | No irritation | No irritation | No irritation | No irritation |
As can be seen from the results in Table 1, the collagen multipeptides of the present invention has a mild formulation and no irritation.
2. Anti-aging repair efficacy test
The test samples prepared from the collagen multipeptides composition of examples 1 to 3 and comparative examples 1 to 4 were subjected to an anti-aging repair efficacy test by the following method:
(1) Anti-wrinkle effect test, using the method for promoting human skin fibroblast proliferation (MTT test):
taking human skin fibroblast in logarithmic growth phase, digesting, and administering a medium containing 15% fetal bovine serum and 1% diabody DMEM medium was prepared at a concentration of 1X 10 5 Cell suspension/mL, inoculated in 96-well plate at 150. Mu.L per well, 37℃and 5% CO 2 After culturing in an incubator for 24 hours, the culture medium is replaced by DMEM culture medium containing 50 mug/mL of sample to be tested, 15% fetal bovine serum and 1% double antibody for continuous culture, after continuous culture for 24 hours, the culture medium is sucked, PBS is used for washing, 150 mug of DMEM culture medium containing 15% fetal bovine serum and 1% double antibody and 20 mug LMTT solution (5 mg/mL) are added, 37 ℃ and 5% CO are added 2 Culturing for 4h, absorbing supernatant, adding 150 μl of DMSO into each well, shaking for 10min, and dissolving the crystals completely. Meanwhile, a control group is arranged, wherein the control group is to replace a sample to be tested with normal saline, and the rest is identical, and each group has 5 compound holes. Absorbance was measured at 490nm for each well, 5 sets of experiments were performed for each set, averaged, and proliferation rate calculated. Proliferation rate (%) = (absorbance value of sample to be measured-absorbance value of control group)/(absorbance value of control group×100%, the result is shown in table 2 below.
TABLE 2
| Sample of | Example 1 | Example 2 | Example 3 | Comparative example 1 | Comparative example 2 | Comparative example 3 | Comparative example 4 |
| Proliferation promoting rate | 121.45％ | 110.38％ | 126.72％ | 77.59％ | 115.43％ | 89.52％ | 95.24％ |
From the results shown in Table 2, the collagen multiple peptide composition of the invention has a good effect of promoting proliferation of human skin fibroblasts, and can effectively inhibit aging of skin cells. The comparative example 1, in which the crocus sativus extract and the carrageenan extract are not added, and the comparative example 3, in which the polypeptide modified cyclosiloxane is not added, shows that the proliferation promoting rate is remarkably reduced, and the crocus sativus extract, the carrageenan extract, the polypeptide and the polypeptide modified cyclosiloxane are obviously synergistic. Comparative example 4 the polypeptide modified linear polysiloxane was used to replace the polypeptide modified cyclosiloxane of the present invention to lighten the stable synergistic components, which also resulted in a significant decrease in proliferation promoting rate. The polypeptide modified cyclosiloxane disclosed by the invention can better promote the performance of the functional components of the polypeptide compared with the polypeptide modified linear polysiloxane. The reason for this is probably that the polypeptide modified cyclosiloxane of the present invention has polypeptide modified chains extending outside the cyclosiloxane, and can well synergistically promote the performance of the polypeptide functional components. The polypeptide modified linear polysiloxane has polypeptide modified branched chain which is easy to be wrapped by hydrophobic linear polysiloxane, and the modified effect of the polypeptide modified linear polysiloxane cannot be well exerted.
(2) Skin elasticity test:
female volunteers 80 persons within 50-70kg of age 30-45 years old were selected and randomly divided into 8 groups of 10 persons each, respectively, control group, examples 1-3 group and comparative examples 1-4 group. A fixed area with the size of 2cm multiplied by 2cm is selected on the arm of a subject, 0.5g of a sample to be tested is smeared on each day, and a basic formula sample without adding the collagen multiple peptide combination component is smeared on a control group. The application was continued for 7 days. The skin elasticity of the test skin was measured by using the skin elasticity tester MPA580 of German CK company, and the average value of R2 (R2 value means the ratio of the rebound quantity of the skin without negative pressure to the maximum stretching quantity with negative pressure) was recorded, and the closer the ratio to 1, the better the skin elasticity was. The results are shown in Table 3 below.
TABLE 3 Table 3
| Sample of | Control group | Example 1 | Example 2 | Example 3 | Comparative example 1 | Comparative example 2 | Comparative example 3 | Comparative example 4 |
| R2 value | 0.62±0.21 | 0.94±0.08 | 0.91±0.14 | 0.95±0.17 | 0.79±0.12 | 0.93±0.19 | 0.83±0.22 | 0.89±0.17 |
As shown in the results of Table 3, the collagen multiple peptide composition of the present invention can promote skin elasticity recovery, and has good anti-aging and repairing effects. Meanwhile, the results of comparative example 1 and comparative example 3 further prove that the uniform brightness stable synergistic components of the crocus sativus extract, the carrageenan extract, the polypeptide and the polypeptide modified cyclosiloxane have obvious synergistic effects.
3. Skin feel test
Female volunteers 70 persons within 50-70kg of age 30-45 years old were selected and randomized into 7 groups of 10 persons each, examples 1-3 and comparative examples 1-4, respectively. The face of the subject is uniformly circled and smeared with 0.5g of sample to be measured, and the soft and moist skin feeling of the skin of the face after being smeared is scored, wherein the soft and moist skin feeling is the best of 5 points, the worst of the dry and tight skin feeling is the worst of 0 point, the average value is taken, and the result is shown in the following table 4.
TABLE 4 Table 4
| Sample of | Example 1 | Example 2 | Example 3 | Comparative example 1 | Comparative example 2 | Comparative example 3 | Comparative example 4 |
| Skin feel score | 4.8 | 4.5 | 4.9 | 4.8 | 3.2 | 3.9 | 4.7 |
From the results shown in Table 4, the addition of cyclopentadimethicone has the most remarkable effect of improving skin feel, and the polypeptide modified cyclopentadimethicone has uniform brightness, stable synergistic components and is beneficial to promoting the exertion of the effect of improving the skin feel of the cyclopentadimethicone.
4. Stability test
The collagen multipeptides composition of examples 1 to 3 and comparative examples 1 to 4 and the formulations prepared according to the basic formulations were tested for high temperature stability (45 ℃,14 d) and low temperature stability (-15 ℃,14 d), respectively, and sample uniformity and delamination were observed, and the results are shown in Table 5 below.
TABLE 5
As can be seen from the results in Table 5, the invention can significantly improve the stability of the composition and the compatibility of the formulation by adding the polypeptide modified cyclosiloxane light-stabilizing synergistic component. In addition, as can be seen from the results of comparative example 4, the stability of the collagen multipeptides composition obtained by modifying the linear polysiloxane with the polypeptide was poor. The reason for this is that the polypeptide-modified linear polysiloxane has its polypeptide-modified hydrophilic chain branched on the inner side, and is mainly suitable for water-in-oil (W/O) systems, and the collagen multi-peptide composition of the present invention is a typical aqueous system, thus resulting in poor stability. The polypeptide modified cyclosiloxane uniform brightness stable synergistic component has the polypeptide modified hydrophilic chain extending outside the cyclosiloxane, and can form a good oil-in-water (O/W) system to stably disperse a small amount of oily cyclopentamethyldisiloxane skin feel regulator, thereby remarkably improving the stability.
The above examples are preferred embodiments of the present invention, but the embodiments of the present invention are not limited to the above examples, and any other changes, modifications, substitutions, combinations, and simplifications that do not depart from the spirit and principle of the present invention should be made in the equivalent manner, and the embodiments are included in the protection scope of the present invention.
Claims (10)
1. The preparation method of the polypeptide modified cyclosiloxane uniform brightness stable synergistic component is characterized by comprising the following preparation steps:
adding cyclic hydrogen-containing polysiloxane and allyl glycidyl ether into an alcohol solvent, heating to 60-90 ℃, adding chloroplatinic acid catalyst for reaction, and obtaining epoxy modified cyclosiloxane; then adding polypeptide compound to continue stirring reaction, and removing alcohol solvent and low-boiling-point substances in vacuum after the reaction is completed to obtain polypeptide modified cyclosiloxane uniform brightness stable synergistic component.
2. The method for preparing a polypeptide modified cyclosiloxane light-stabilizing synergistic ingredient according to claim 1, wherein the cyclic hydrogen-containing polysiloxane is at least one of 2,4,6, 8-tetramethyl cyclotetrasiloxane and 2,4,6,8, 10-pentamethyl cyclopentasiloxane.
3. The method for preparing a polypeptide modified cyclosiloxane brightening stable synergistic composition according to claim 2, wherein the molar ratio of the cyclic hydrogen-containing polysiloxane to the allyl glycidyl ether is 1:3-5.
4. The method for preparing a polypeptide-modified cyclosiloxane brightening stable synergistic composition according to claim 1, wherein the alcohol solvent is one or a mixed solvent of more than two of ethanol, propanol and isopropanol.
5. The method for preparing a polypeptide modified cyclosiloxane brightness stabilizing synergistic component according to claim 1, wherein the polypeptide compound is at least one selected from collagen tripeptide, palmitoyl tetrapeptide, palmitoyl pentapeptide and acetyl hexapeptide.
6. The method for preparing a polypeptide modified cyclosiloxane light-stabilizing synergistic ingredient according to claim 5, wherein the addition amount of the polypeptide compound is 1-1.2 times of the molar amount of allyl glycidyl ether.
7. A polypeptide modified cyclosiloxane brightness-stabilizing synergistic composition, characterized in that it is prepared by the method of any one of claims 1-6.
8. A collagen multipeptid composition prepared from the polypeptide-modified cyclosiloxane brightness-stabilizing synergistic composition of claim 7, comprising the following raw materials:
water, palmitoyl tripeptide-1, palmitoyl pentapeptide-4, acetyl hexapeptide-8, palmitoyl tetrapeptide-7, acetyl tetrapeptide-5, crocus sativus extract, chondrus crispus extract, cyclopentamethylsiloxane, polypeptide modified cyclosiloxane, brightness stabilizing synergistic components and hydrolyzed collagen.
9. The collagen multiple peptide composition according to claim 8, wherein the mass percentage of each raw material is as follows:
10. a method for preparing a collagen multipeptides composition according to claim 8 or 9, comprising the steps of:
sequentially adding palmitoyl tripeptide-1, palmitoyl pentapeptide-4, acetyl hexapeptide-8, palmitoyl tetrapeptide-7, acetyl tetrapeptide-5 and hydrolyzed collagen into water to dissolve uniformly, then adding polypeptide modified cyclosiloxane to uniformly lighten, stabilize and synergistic components, and adding the crocus sativus extract and the chondrus crispus extract to stir and dissolve uniformly, and finally adding the cyclopentamethylsiloxane to stir and mix uniformly to obtain the collagen multiple peptide composition.
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