CN115475277A - Recombined III-type humanized triple-helical-structure collagen dressing - Google Patents
Recombined III-type humanized triple-helical-structure collagen dressing Download PDFInfo
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- CN115475277A CN115475277A CN202211330068.7A CN202211330068A CN115475277A CN 115475277 A CN115475277 A CN 115475277A CN 202211330068 A CN202211330068 A CN 202211330068A CN 115475277 A CN115475277 A CN 115475277A
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
- A61L26/00—Chemical aspects of, or use of materials for, wound dressings or bandages in liquid, gel or powder form
- A61L26/0009—Chemical aspects of, or use of materials for, wound dressings or bandages in liquid, gel or powder form containing macromolecular materials
- A61L26/0028—Polypeptides; Proteins; Degradation products thereof
- A61L26/0033—Collagen
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
- A61L26/00—Chemical aspects of, or use of materials for, wound dressings or bandages in liquid, gel or powder form
- A61L26/0009—Chemical aspects of, or use of materials for, wound dressings or bandages in liquid, gel or powder form containing macromolecular materials
- A61L26/0014—Chemical aspects of, or use of materials for, wound dressings or bandages in liquid, gel or powder form containing macromolecular materials obtained by reactions only involving carbon-to-carbon unsaturated bonds
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
- A61L26/00—Chemical aspects of, or use of materials for, wound dressings or bandages in liquid, gel or powder form
- A61L26/0061—Use of materials characterised by their function or physical properties
- A61L26/008—Hydrogels or hydrocolloids
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
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- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Epidemiology (AREA)
- Materials Engineering (AREA)
- Animal Behavior & Ethology (AREA)
- Engineering & Computer Science (AREA)
- Public Health (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Dispersion Chemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The invention discloses a recombinant III-type humanized triple-helical-structure collagen dressing, and belongs to the technical field of biological medicines. In the dressing, the recombinant III type collagen has a triple helix structure, and can form a protective film on the surface of a damaged tissue to isolate and screen skin wound surfaces; the adhesive has cell adhesion and promotes the repair of damaged parts; can regulate oxygen tension of wound surface, improve cell activity, and fill and repair damaged and aged skin. The D- (+) -trehalose dihydrate has excellent characteristics of keeping cell activity and biological macromolecule activity, and has film forming property and stability; the butanediol has moisturizing effect, and the glycerin is a moisturizing agent, can improve the solubility and permeability of the skin care product, can adjust the hydration function of the skin, increase the water content, improve the dryness of the skin, promote the self-repair of damaged cells, and protect the skin from the stimulation of the external environment. Is suitable for the superficial second degree trauma of skin and the adjuvant treatment of laser cosmetology to recover the barrier function of skin.
Description
Technical Field
The invention belongs to the technical field of biological medicines, and particularly relates to a recombinant III-type humanized triple-helical-structure collagen dressing.
Background
Skin superficial abrasion, cut wound, small wound, laser, photon, tartaric acid skin change and micro plastic surgery are common skin injuries in clinic, if the wound surface is not properly treated, microbial infection of the wound can be caused, the wound can sometimes go deep into tissues to cause tissue necrosis, and if the wound surface is serious, the life can be threatened. Therefore, when superficial damage occurs to the skin, debridement treatment and protection should be performed in time.
At present, the clinical treatment of wounds still adopts the traditional method, and the wounds are cleaned by disinfectants such as iodophor, hydrogen peroxide or normal saline and then covered by cotton gauze. The traditional gauze dressing has soft texture, strong absorption capacity, capability of preventing the seepage accumulation of the wound surface and certain protection effect on the wound surface. However, as the research on wound healing progresses, it is recognized that the purpose of using a dressing is far beyond covering the wound surface, and the dressing must also help the wound healing.
The former view is that a dry environment should be created for the wound as much as possible, so that the infection chance is reduced, and the wound healing is facilitated. However, recent studies have shown that wounds heal more rapidly in a moist environment. Therefore, the traditional gauze dressing has the limitations of no promotion effect on wound healing, no moisturizing effect, easy granulation tissue growth into gauze meshes to cause adhesion and scabbing, easy secondary injury to the wound during dressing change, easy scar formation of the focus after healing and the like. Therefore, it is very important to find a wound dressing product which is convenient, high in safety and good in moisturizing performance.
Along with improvement of living standard of people, the application of laser technology to shaping and beautifying is more and more extensive, and the requirement of people on the repair effect of skin after laser beautifying is higher and higher, however, fewer in-vitro absorbable medical supplies for the auxiliary treatment after laser shaping and beautifying are provided.
At present, the rhythm of life and work of people is fast, more time is not needed for treating small wounds of skin in medical institutions, and a product is expected to be provided at home to conveniently protect the wounds and protect the wounds from being infected by microorganisms. With the progress of materials science and industry, a good foundation is provided for the research and development of novel wound dressings.
Therefore, research and development of medical products with good repair effects are urgently needed to fill the domestic blank market.
Disclosure of Invention
The invention aims to provide a recombinant III-type humanized triple-helical-structure collagen dressing, and a product prepared from the dressing has the function of promoting the repair of a skin injury part, can be externally applied to a wound surface to form a protective layer, shields the wound, provides a moist healing environment for the wound, and solves the technical problems that the existing product is easy to cause infection in the treatment of a minimally invasive wound, the wound healing rate is low, and the dry environment is easy to cause the adhesion of skin tissues and a gauze dressing to cause secondary damage to the wound surface.
The invention is realized by the following technical scheme:
a recombinant III-type humanized triple-helical-structure collagen dressing is mainly prepared from the following raw materials in parts by mass:
0.03-0.10 wt% of recombinant III type humanized triple-helical structure collagen, 0.06-0.18 wt% of D- (+) -trehalose dihydrate, 0.2-0.8 wt% of carbomer, 1.5-3.5 wt% of butanediol, 1-2.5 wt% of glycerol, 0.1-0.5 wt% of triethanolamine and the balance of purified water.
Preferably, the recombinant III type humanized triple-helical-structure collagen dressing is mainly prepared from the following raw materials in percentage by mass:
0.07wt% of recombinant III type humanized triple-helical-structure collagen, 0.15wt% of D- (+) -trehalose dihydrate, 0.5wt% of carbomer, 3wt% of butanediol, 2wt% of glycerol, 0.35wt% of triethanolamine and the balance of purified water.
The recombined III-type humanized triple-helical-structure collagen dressing mainly comprises a triple-helical-structure recombined III-type humanized triple-helical-structure collagen, D- (+) -trehalose dihydrate, glycerol, carbomer, butanediol and triethanolamine.
Among them, the recombinant type iii humanized triple helix structure collagen has a triple helix structure, and the triple helix(s) is a set of three identical geometric helices having the same axis but different degrees of translation along the axis. This means that each helix remains at the same distance from the central axis. Like a single helix, a triple helix can be characterized by its pitch, diameter and convention. Examples of triple helices include triple stranded DNA, collagen helices of triple RNA, and collagen-like proteins. When the amino acid sequences are arranged, every two amino acids (Proline) or Hydroxyproline (Hydroxyproline)) have Glycine (Glycine), the bend formed by the Glycine (Glycine) fills the interior of the helix, and the Proline (Proline) and Hydroxyproline (Hydroxyproline) chains form a smooth bend around the helix, so that a compact and stable three-dimensional helical structure is formed. This stable triple helix structure is formed by a repeating sequence of three amino acids — every third amino acid is a Glycine (Glycine). Glycine (Glycine) is a small amino acid that can be well assembled inside the helix. The remaining positions in the chain are substituted with other amino acids: such as Proline (Proline) and Hydroxyproline (Hydroxyproline). The recombined III-type humanized triple-helical-structure collagen has the effects of increasing elasticity, moisturizing, increasing elasticity, resisting wrinkles, removing freckles and the like, and can form a layer of protective film on the surface of a damaged tissue to isolate and screen skin wound surfaces; the cell adhesive has better cell adhesion, and promotes the repair of the damaged part; can regulate oxygen tension of wound surface, improve cell activity, and fill and repair damaged and aged skin. The D- (+) -trehalose dihydrate has excellent characteristics of keeping cell activity and biological macromolecule activity, and has film forming characteristics and stability; the butanediol has the function of moisturizing, and the glycerin is the most common moisturizing agent, can improve the solubility and the permeability of the skin care product, can adjust the hydration function of the skin, increase the water content, improve the dryness of the skin, promote the self-repair of damaged cells, and protect the skin from the stimulation of the external environment.
Recombinant type iii humanized triple helix collagen: CAS number: 2406308-23-2, molecular formula: c 1798 H 2819 N 603 O 601 S 2 Molecular weight: 43.6KDa, the recombinant III type humanized triple-helical structure collagen is composed of water-soluble collagen peptide, and has the characteristic structure of collagen: G-X-Y repeating structure, G represents glycine, and Y represents proline. Solubility: solubility > 5wt% (20 ℃), thermal stability: the fermentation liquid is heated to 100 ℃ for 30min and is stable. Similarity to human collagen sequence: 100wt%. Recombinant type III humanizationThe collagen with the triple-helical structure is from a yeast fermentation product, the yeast is a eukaryotic cell, has protein post-translational modification capacity similar to that of a human cell, can be modified and processed into collagen with physiological activity after being synthesized, can be recognized and adhered by a human cell, and stimulates the cell to synthesize the collagen through a signal conduction path. The excellent triple-helix structural characteristics of the collagen are utilized in the product, the function of the protein is determined by the structure of the collagen, and only the collagen with a complete triple-helix stable structure can exert all the effects of the collagen. This stable triple helix structure is formed by a repeating sequence of three amino acids — every third amino acid is a Glycine (Glycine). Glycine (Glycine) is a small amino acid that can be well assembled inside the helix to form a membrane on the skin surface and to adhere to cells.
D- (+) -trehalose dihydrate: CAS number: 6138-23-4, molecular formula C 12 H 22 O 11 ·2H 2 O, recorded in the fourth part of the Chinese pharmacopoeia; trehalose has been successfully applied to replace plasma protein in medicine as a stabilizer for bioactive substances such as blood products, vaccines, lymphocytes, cell tissues and the like, and can be applied to the preservation of biological reagents for research, such as various tool enzymes, cell membranes, organelles, antibodies, antigens, viruses and the like, so that the life science research is more convenient, faster and effective; the cosmetic use of trehalose is based on its excellent properties of maintaining cell viability and biomacromolecule activity. Skin cells, especially epidermal cells, are easily subjected to keratinization due to water loss and even death and falling off under the environments of high temperature, high cold, dryness, strong ultraviolet radiation and the like, so that the skin is damaged. Under the condition, trehalose can form a special protective film on the cell surface layer, and mucus precipitated from the film not only moistens skin cells, but also has the function of radiating external heat. Thereby protecting the skin from damage. The product has excellent film-forming performance and is also a good stabilizer.
An application of a recombined III-type humanized triple-helical-structure collagen dressing in preparing a recombined III-type humanized triple-helical-structure collagen gel finished product or a recombined III-type humanized triple-helical-structure collagen stock solution finished product.
A method for preparing a recombinant III type humanized triple-helical structure collagen gel finished product is prepared by adopting the recombinant III type humanized triple-helical structure collagen dressing and comprises the following steps:
(1) Selecting carbomer and purified water according to corresponding mass fraction, and emulsifying at homogenizing speed of 20-30HZ to obtain a standby product A;
(2) Selecting triethanolamine and purified water according to corresponding mass fractions, and mixing and dissolving to obtain a standby substance B;
(3) Selecting recombinant III type humanized triple-helical-structure collagen and purified water according to corresponding mass fractions, and mixing and dissolving to obtain a spare substance C;
(4) Selecting glycerol, butanediol and D- (+) -trehalose dihydrate according to corresponding mass fractions, stirring and mixing, mixing with the standby material A, homogenizing, heating to 80-90 deg.C, keeping the temperature for 20-30min, cooling to 50-60 deg.C, adding the standby material B, and stirring;
(5) And continuously cooling to not higher than 45 ℃, adding the standby material C, homogenizing until the material body is uniformly dispersed, clear and transparent, filtering, and discharging to obtain a finished product.
Preferably, in the step (4), when the glycerol, the butanediol and the D- (+) -trehalose dihydrate are stirred and mixed, the stirring time is 3-5 minutes, and the stirring speed is 600-800 revolutions per minute;
during the homogenization treatment, high-speed homogenization is adopted for 5-8 minutes, and the homogenization speed is 30-40HZ;
and when the standby material B is added and stirred, homogenizing at a low speed of 20-30HZ, and fully stirring for 2-3 minutes at a stirring speed of 15-20HZ for stirring treatment.
Preferably, in the step (5), the homogenization treatment time is 3-5 minutes, and the homogenization treatment speed is 15-20HZ;
and 200-400 meshes of filter cloth is adopted during filtering.
A method for preparing a recombinant III-type humanized triple-helical-structure collagen stock solution finished product is prepared by adopting the recombinant III-type humanized triple-helical-structure collagen dressing and comprises the following steps:
(1) Selecting triethanolamine and purified water according to corresponding mass fractions, and mixing and dissolving to obtain a standby substance A;
(2) Selecting recombinant III type humanized triple-helical-structure collagen and purified water according to corresponding mass fractions, and mixing and dissolving to obtain a spare substance B;
(3) Selecting glycerol, butanediol and D- (+) -trehalose dihydrate according to corresponding mass fractions, stirring and mixing, adding carbomer and purified water, heating, homogenizing, keeping the temperature for 20-30min, cooling to 50-60 deg.C, adding the product A, and stirring and mixing;
(4) And continuously cooling to not higher than 45 ℃, adding the standby material B, homogenizing until the material body is uniformly dispersed, clarified and transparent, filtering, and discharging to obtain a finished product.
Preferably, in the step (3), when the glycerol, the butanediol and the D- (+) -trehalose dihydrate are stirred and mixed, the stirring time is 3-5 minutes, and the stirring speed is 600-800 revolutions per minute;
heating to 85-92 deg.C, homogenizing at 30-40Hz for 5-8 min;
and when the standby material A is added, stirring and mixing, homogenizing at a low speed of 20-30HZ, and fully stirring for 2-3 minutes at a stirring speed of 15-20HZ for stirring treatment.
Preferably, in the step (4), the homogenization treatment time is 3-5 minutes, and the homogenization treatment speed is 15-20HZ;
and filtering cloth of 200-400 meshes is adopted during filtering.
Compared with the prior art, the invention at least has the following technical effects:
the invention provides a recombined III type humanized triple-helix collagen dressing which mainly comprises a triple-helix recombined III type collagen, D- (+) -trehalose dihydrate, glycerol, carbomer, butanediol and triethanolamine.
Wherein the recombinant type III collagen: the contained recombinant III-type humanized triple-helix collagen has a triple-helix structure, and forms a supercoiled structure with the collagen fractured in the wound surface through intermolecular van der Waals force, and the reticular supercoiled structure can form a layer of protective film on the surface of the damaged tissue to isolate and shield the skin wound surface; (2) the recombined III type humanized triple-helical structure collagen has better cell adhesion (the charged amino acid residues of the recombined III type humanized triple-helical structure collagen and the charges on the surface of cells are adhered to each other through physical charge attraction), thereby providing external support for the cells and promoting the repair of damaged parts. (3) According to the theory of moist healing, the moist environment can increase the migration speed of surface cells, adjust the oxygen tension of the wound surface, promote the formation of capillaries, be beneficial to the dissolution and absorption of necrotic cells and fibrin, promote the release of various growth factors and accelerate the healing of the wound, and the added various humectants and film forming agents promote the product to form a transparent hydration film on the surface layer of the skin, prevent the evaporation of water in the skin, play a role of physical barrier and provide a moist microenvironment for the healing of the wound surface.
And (II) the recombined III-type humanized triple-helical-structure collagen dressing product has the functions of nourishing, resisting aging, tightening, removing wrinkles, moisturizing, whitening and safely repairing. The skin care product can be perfectly combined with the extracellular matrix of human epidermal tissue, provides a very good tissue environment for maintaining cell activity, and effectively inhibits apoptosis of cells, thereby realizing the anti-aging effect of surface skin; the compact and regular supercoiled collagen fiber net is formed by means of the triple-helix stable structure of the recombinant III type collagen, so that the moisture of the stratum corneum of the skin is kept, the metabolism of skin tissues is promoted, the blood circulation of the skin on the surface layer is enhanced, wrinkles disappear from the skin on the surface layer, and the effects of tightening and removing the wrinkles are achieved
And thirdly, a large amount of hydrophilic amino acids contained in the recombinant type III collagen can not only create a good environment for cell activity, but also provide recombinant bound water for surface skin. The water content of the skin is ensured, and the water content indirectly acts on the glossiness of the skin, so that the whitening effect can be achieved. The three-helix stable structure has very strong water locking capacity, can activate the metabolic function of cells, reduce the pigmentation of the skin on the surface layer, avoid the formation of color spots and provide sufficient water source for the white skin; has a functional structure sequence which is similar to 100wt percent of type III collagen produced by human bodies, so that the probability of occurrence of rejection reaction is minimized, the survival rate of different cell lines is influenced by 0, the safety level can also assist the normal growth and renewal of skin cells, rebuild the original contour of the skin and achieve the effect of repair.
And (IV) the recombined III type collagen exerts excellent biological activity and histocompatibility, promotes fibroblast proliferation of a dermis layer, improves cell activity, is absorbed by fibroblasts as raw materials for synthesizing collagen, stimulates cells to synthesize more collagen, fills and repairs damaged and aged skin, reconstructs a reticular structure, enhances the expansion force of the damaged skin and recovers the elasticity of the skin. The skin is anti-aging and repaired, the skin is calmed, the allergy is removed, the scar and the mark are removed, and the water is supplemented and the skin is lightened.
The recombinant III type collagen is obtained by optimizing, recombining and expressing a human collagen III type original gene sequence by utilizing a genetic engineering technology, is highly consistent with a human natural collagen amino acid sequence, is obtained by recombination, optimization and expression, is rich in hydrophilic amino acid residues, and has higher biological activity, hydrophilicity and low immunological rejection. Meanwhile, the skin-care product also has the tendency of guiding epithelial cells to rapidly migrate to the damaged part, promoting the skin regeneration speed and shortening the wound healing time, thereby recovering the skin barrier function.
The invention develops a medical recombined III type humanized triple-helical structure collagen dressing by taking recombined III type collagen as a main raw material, and the dressing is mainly used for recovering the barrier function of skin in superficial second-degree trauma and auxiliary treatment of laser cosmetology.
Drawings
FIG. 1 is a schematic view of a skin area to which an experimental treatment was applied in accordance with test example.
Detailed Description
Embodiments of the present invention will be described in detail with reference to the following examples, but it will be understood by those skilled in the art that the following examples are merely illustrative of the present invention and should not be construed as limiting the scope of the present invention, and that the specific conditions not specified in the examples are conducted under conventional conditions or conditions suggested by the manufacturer, and that reagents or equipment not specified by the manufacturer are all conventional products which can be obtained by commercial purchase.
The technical scheme of a specific implementation mode of the invention is as follows:
the recombinant III-type humanized triple-helical-structure collagen dressing is mainly prepared from the following raw materials in percentage by mass:
0.03-0.10 wt% of recombinant III type humanized triple-helical structure collagen, 0.06-0.18 wt% of D- (+) -trehalose dihydrate, 0.2-0.8 wt% of carbomer, 1.5-3.5 wt% of butanediol, 1-2.5 wt% of glycerol, 0.1-0.5 wt% of triethanolamine and the balance of purified water.
Preferably, the recombinant III type humanized triple-helical-structure collagen dressing is mainly prepared from the following raw materials in percentage by mass:
0.07wt% of recombinant III type humanized triple-helical-structure collagen, 0.15wt% of D- (+) -trehalose dihydrate, 0.5wt% of carbomer, 3wt% of butanediol, 2wt% of glycerol, 0.35wt% of triethanolamine and the balance of purified water.
An application of a recombined III-type humanized triple-helical-structure collagen dressing in preparing a recombined III-type humanized triple-helical-structure collagen gel finished product or a recombined III-type humanized triple-helical-structure collagen stock solution finished product.
A method for preparing a recombinant III type humanized triple-helical structure collagen gel finished product is prepared by adopting the recombinant III type humanized triple-helical structure collagen dressing and comprises the following steps:
(1) Selecting carbomer and purified water according to corresponding mass fraction, and emulsifying at homogenizing speed of 20-30HZ to obtain a standby product A;
(2) Selecting triethanolamine and purified water according to corresponding mass fractions, and mixing and dissolving to obtain a standby substance B;
(3) Selecting recombinant III type humanized triple-helical-structure collagen according to corresponding mass fractions, and mixing and dissolving the recombinant III type humanized triple-helical-structure collagen with purified water to obtain a spare substance C;
(4) Selecting glycerol, butanediol and D- (+) -trehalose dihydrate according to corresponding mass fractions, stirring and mixing, mixing with the standby substance A, homogenizing, heating to 80-90 ℃, keeping the temperature for 20-30min, cooling to 50-60 ℃, adding the standby substance B, and stirring;
(5) And continuously cooling to not higher than 45 ℃, adding the standby material C, homogenizing until the material body is uniformly dispersed, clarified and transparent, filtering, and discharging to obtain a finished product.
Preferably, in the step (4), when the glycerol, the butanediol and the D- (+) -trehalose dihydrate are stirred and mixed, the stirring time is 3-5 minutes, and the stirring speed is 600-800 revolutions per minute;
during the homogenization treatment, high-speed homogenization is adopted for 5-8 minutes, and the homogenization speed is 30-40HZ;
and when the standby material B is added and stirred, homogenizing at a low speed of 20-30HZ, and fully stirring for 2-3 minutes at a stirring speed of 15-20HZ for stirring treatment.
Preferably, in the step (5), the homogenization treatment time is 3-5 minutes, and the homogenization treatment speed is 15-20HZ;
and 200-400 meshes of filter cloth is adopted during filtering.
A method for preparing a recombinant III-type humanized triple-helical-structure collagen stock solution finished product is prepared by adopting the recombinant III-type humanized triple-helical-structure collagen dressing and comprises the following steps:
(1) Selecting triethanolamine and purified water according to corresponding mass fractions, and mixing and dissolving to obtain a standby substance A;
(2) Selecting recombinant III type humanized triple-helical-structure collagen and purified water according to corresponding mass fractions, and mixing and dissolving to obtain a spare substance B;
(3) Selecting glycerol, butanediol and D- (+) -trehalose dihydrate according to corresponding mass fractions, stirring and mixing, adding carbomer and purified water, heating, homogenizing, keeping the temperature for 20-30min, cooling to 50-60 ℃, adding the standby substance A, and stirring and mixing;
(4) And continuously cooling to not higher than 45 ℃, adding the standby material B, homogenizing until the material body is uniformly dispersed, clarified and transparent, filtering, and discharging to obtain a finished product.
Preferably, in the step (3), when the glycerol, the butanediol and the D- (+) -trehalose dihydrate are stirred and mixed, the stirring time is 3-5 minutes, and the stirring speed is 600-800 revolutions per minute;
heating to 85-92 deg.C, homogenizing at 30-40Hz for 5-8 min;
and when the standby material A is added, stirring and mixing, homogenizing at a low speed of 20-30HZ, and fully stirring for 2-3 minutes at a stirring speed of 15-20HZ for stirring treatment.
Preferably, in the step (4), the homogenization treatment time is 3-5 minutes, and the homogenization treatment speed is 15-20HZ;
and 200-400 meshes of filter cloth is adopted during filtering.
Example 1:
a preparation method of a recombinant III-type humanized triple-helical-structure collagen gel finished product comprises the following steps:
(1) Adding 899.3g of weighed purified water and 5g of carbomer into an emulsifying pot, and opening the homogenizing speed to be 20-30HZ;
(2) Weighing 10g of purified water and 3.5g of triethanolamine in the formula, and fully stirring to dissolve the purified water and the triethanolamine;
(3) Weighing 30g of purified water and 0.7g of recombinant III type humanized triple-helical structure collagen in the formula, and fully stirring to dissolve the purified water and the recombinant III type humanized triple-helical structure collagen;
(4) Putting 20g of glycerol, 30g of butanediol and 1.5g of D- (+) -trehalose dihydrate into a container, stirring for 3 minutes by using an electric stirrer at the speed of 600-800 revolutions per minute, fully stirring and dissolving, then adding into an emulsifying pot, homogenizing for 5 minutes at a high speed at the speed of 30-40HZ, heating to about 90 ℃, preserving heat for 20 minutes, and cooling the materials by cooling water; when the temperature of the materials is reduced to about 60 ℃, adding the triethanolamine solution which is dissolved separately in advance in the step (2), homogenizing at a low speed of 20-30HZ again, and fully stirring for 2-3 minutes at a stirring speed of 15-20HZ;
(4) And (3) when the temperature is reduced to below 45 ℃, adding the recombinant III type humanized triple-helical structure collagen solution in the step (3) into an emulsifying pot, fully stirring for 3 minutes at the stirring speed of 15-20HZ until the material body is uniformly dispersed, clarified and transparent, sampling, testing and discharging after passing the inspection, filtering by using 200-mesh filter cloth, and discharging.
Example 2:
a method for preparing a recombinant III-type humanized triple-helical-structure collagen gel finished product comprises the following steps:
(1) Adding 899.3g of weighed purified water and 5g of carbomer into an emulsifying pot, and opening the homogenizing speed to be 20-30HZ;
(2) Weighing 10g of purified water and 3.5g of triethanolamine in the formula, and fully stirring to dissolve the purified water and the triethanolamine;
(3) Weighing 30g of purified water and 0.7g of recombinant III type humanized triple-helical structure collagen in the formula, and fully stirring to dissolve the purified water and the recombinant III type humanized triple-helical structure collagen;
(4) Putting 20g of glycerol, 30g of butanediol and 1.5g of D- (+) -trehalose dihydrate into a container, stirring for 5 minutes by using an electric stirrer at the speed of 600-800 revolutions per minute, fully stirring and dissolving, then adding into an emulsifying pot, homogenizing for 8 minutes at a high speed at the speed of 30-40HZ, heating to about 80 ℃, preserving heat for 30 minutes, and cooling the materials by cooling water; when the temperature of the materials is reduced to about 50 ℃, adding the triethanolamine solution which is dissolved separately in advance in the step (2), homogenizing at a low speed of 20-30HZ again, and fully stirring for 2-3 minutes at a stirring speed of 15-20HZ;
(4) And (4) when the temperature is reduced to be below 45 ℃, adding the recombined III type humanized triple-helical-structure collagen solution in the step (3) into an emulsifying pot, fully stirring for 5 minutes at the stirring speed of 15-20HZ until the material body is uniformly dispersed, clarified and transparent, sampling and inspecting, filtering with 400-mesh filter cloth, and discharging.
Example 3:
a preparation method of a recombinant III type humanized triple-helical structure collagen stock solution finished product comprises the following steps:
(1) Adding 924.3g of purified water into an emulsifying pot, opening the homogenizing speed to 20-30HZ, and adding carbomer;
(2) Weighing 10g of purified water and 3.5g of triethanolamine in the formula, and fully stirring to dissolve the purified water and the triethanolamine;
(3) Weighing 30g of purified water in the prescription to dissolve the recombinant III type humanized triple-helical structure collagen in the prescription amount;
(4) Putting glycerol, butanediol, xanthan gum and D- (+) -trehalose dihydrate into a container, stirring with an electric stirrer at a speed of 600-800 r/min for 3-5 min, stirring uniformly, pouring into an emulsifying pot, heating to about 92 ℃, homogenizing at a high speed of 30-40HZ for 5-8 min, and keeping the temperature for 30 min. Cooling water is started to cool the materials, and when the temperature of the materials is reduced to about 60 ℃. Adding the triethanolamine solution obtained in the step (2), homogenizing at low speed of 20-30HZ again, and stirring for 2-3 min at 15-20HZ;
(5) And (3) when the temperature is reduced to below 45 ℃, adding the recombinant III type humanized triple-helical structure collagen solution in the step (3) into an emulsifying pot, stirring at the speed of 15-20HZ, uniformly dispersing until the material body is clear and transparent, sampling, inspecting, filtering by using 200-mesh filter cloth, and discharging.
Example 4:
a preparation method of a recombinant III type humanized triple-helical structure collagen stock solution finished product comprises the following steps:
(1) Adding 924.3g of purified water into an emulsifying pot, opening the homogenizing speed to 20-30HZ, and adding carbomer;
(2) Weighing 10g of purified water and 3.5g of triethanolamine in the formula, and fully stirring to dissolve the purified water and the triethanolamine;
(3) Weighing 30g of purified water in the prescription, and dissolving the recombinant III type humanized triple-helical-structure collagen in the prescription amount;
(4) Putting glycerol, butanediol, xanthan gum and D- (+) -trehalose dihydrate into a container, stirring for 3-5 minutes by using an electric stirrer at the speed of 600-800 revolutions per minute, pouring into an emulsifying pot after fully stirring uniformly, heating to about 85 ℃, homogenizing at high speed for 5-8 minutes at the homogenizing speed of 30-40HZ, and preserving heat for 20 minutes. Cooling water is started to cool the materials, and when the temperature of the materials is reduced to about 50 ℃. Adding the triethanolamine solution obtained in the step (2), homogenizing at low speed of 20-30HZ again, and stirring for 2-3 min at 15-20HZ;
(5) And (4) when the temperature is reduced to be below 45 ℃, adding the recombinant III type humanized triple-helical-structure collagen solution obtained in the step (3) into an emulsifying pot, stirring at the speed of 15-20HZ, uniformly dispersing until the material body is clear and transparent, sampling, inspecting, filtering by using 400-mesh filter cloth, and discharging.
The using method comprises the following steps: clean the skin of the affected part, apply it on the affected part.
1. The adjuvant therapy of dermatitis eczema, atopic dermatitis, hormone-dependent dermatitis, xeroderma, sensitive skin, skin inflammation caused by various reasons such as laser treatment, and the like: 2-3 times a day, and one treatment course is every two weeks.
2. Mild to moderate acne and adjuvant treatment of pigmentation and scar after acne healing: patients with mild acne take 2-3 times per day, and every two weeks is a treatment course; moderate acne patients take 2 to 3 times a day, and one treatment course is every four weeks.
3. Auxiliary treatment of pigmentation and scar caused by laser treatment: 2-3 times a day, and one treatment course is every two weeks.
4. Wound healing and skin repair: 2-3 times a day, and one treatment course is every two weeks.
Test examples:
the first test: skin irritation test
The method comprises the following steps: acute skin irritation test, the test example prepared in example 1 was soaked in water-absorbent gauze and applied to the back skin of the test rabbit, the application was removed after at least 4 hours of contact, and the test site was marked.
The negative control group was operated by the same method as above: 0.9wt% sodium chloride injection was impregnated into water absorbent gauze.
At 1h, 24h, 48h and 72h after the removal of the patch, the test site and its skin tissue reactions were observed, including records of erythema, edema and necrosis, and graded scores were made based on the occurrence of erythema and edema. The skin irritation test was repeated, and after the observation of acute skin irritation for 72 hours, the test example and the negative control group were applied by the same method every day, and the condition of the contact site was recorded before each contact. The primary stimulation index for the test case was determined by adding the total primary stimulation score for each animal and dividing by the total number of animals (typically 3). The primary stimulation score of the test example was subtracted from the negative control score to obtain the primary stimulation score. This value is the primary stimulation index. Multiple contact tests were prescribed to calculate a cumulative stimulation index.
As a result: test example primary irritation index 0 for acute skin irritation test of experimental rabbits; experimental example the primary stimulation index of the skin irritation test was 0 in the experimental rabbits.
And (4) conclusion: under the test condition, the primary irritation index of the product prepared in the example 1 to the acute skin irritation test of the experimental rabbit is 0; the primary irritation index was 0 for the experimental rabbits in the repeated skin irritation test. The type of skin irritation response is a very mild microstimulation response.
A specific test method;
preparation before testing: prior to testing, animals were identified and sufficient area of fur (approximately 10 cm. Times.15 cm area) was removed on both sides of the animal's dorsal spine for testing and observation.
The test steps are as follows: the test and negative control groups were placed on the corresponding skin areas on the back of the animals, covered with a layer of cellophane and then semi-closed with pressure sensitive adhesive tape for at least 4 hours. The contact test was repeated and applied 1 time per day for 14 days continuously after 72 hours of observation in the acute skin irritation test. The remaining test substance was removed by water by clipping before each application from the next day.
The test area of the negative control group and the test area of the test example were treated in the same manner. The area of application to the skin is shown in detail in figure 1. FIG. 1 illustrates schematically: 1-a head; 2-test site; 3-negative control site; 4-the dehaired dorsal region; 5-tail.
And (3) test observation: acute skin irritation test, the patch was removed after the contact period was complete and the remaining test material was removed with warm water. Each contact site was observed and recorded at 1h, 24h, 48h and 72h after removal of the patch, and the skin erythema and edema at each contact site at each prescribed time period was described and scored by a skin reaction score system. The contact skin irritation test was repeated and the contact site was recorded 72h after the observation of the acute skin irritation test, each time (1 + -0.1) h after removal of the patch and before re-contact. After the last contact, each contact site was observed and recorded at 1h, 24h, 48h and 72h after removal of the patch, respectively.
Acute skin irritation dosing date: 2021, 8 months and 30 days
Acute skin irritation observation date: 30/8/2021-2/9/2021
Repeated contact skin irritation dosing date: 9/month 2/2021-9/month 15/2021
Repeat contact skin irritation observation date: 9/month 2/2021-9/month 18/2021
Results and evaluation: skin irritation test observation scoring criteria: no erythema, 0 point; very mild erythema (barely visible), 1 point; clear erythema, 2 points; moderate erythema, score 3; eschar formation from severe erythema (purplish red) to failure to grade erythema, score 4. No edema, score 0; very mild edema (barely visible), 1 point; clear edema (sharp swollen edge), 2 points; moderate edema (skin doming about 1 mm), score 3; severe edema (skin doming over 1mm and beyond the contact area), score 4. The highest score total score was 8.
Evaluation criteria for skin irritation intensity: 0-0.4 min, and is extremely light; 0.5-1.9 min, light; 2.0-4.9 points, medium; 5.0-8.0 minutes, severe.
Acute skin irritation test the Primary Irritation Index (PII) was determined as specified below. Calculations were performed using only the observed data for (24 ± 2) h, (48 ± 2) h and (72 ± 2) h. The recovery observations before the trial or after 72h were not used for calculation. After 72h scoring, the total erythema and edema scores for each animal at (24. + -.2) h, (48. + -.2) h and (72. + -.2) h were added to the negative control and the sum of all scores was divided by 6 (two trials/observation sites, 3 time points) to calculate the primary stimulation index for an animal. The primary stimulation index of the experimental test case was obtained by adding the total primary stimulation score of each animal and dividing by the total number of animals (generally 3).
When a blank or negative control is used, a control primary stimulation score is calculated and subtracted from the test material primary stimulation score to obtain the primary stimulation score.
The contact test is repeated and the primary stimulation score should be calculated for each animal as described above, taking into account all evaluation endpoints. Cumulative stimulation indices were calculated as specified below.
All animal stimulation scores were added and divided by the total number of animals. This value is the cumulative stimulation index.
The cumulative stimulation index is used for reporting the corresponding response type according to the stimulation response given by the skin stimulation intensity evaluation standard.
Test example primary stimulation index of acute skin stimulation test of experimental rabbit is 0; experimental example the primary irritation index was 0 for the experimental rabbits in the repeated contact skin irritation test. The results are shown in the following table:
TABLE 1 Rabbit skin irritation response Scoring results (Single contact test)
TABLE 2 evaluation results of rabbit skin irritation response (repeated contact test)
Test example two: skin sensitization test
The method comprises the following steps: after the guinea pigs were induced by repeated contact with the test example over a period of time (negative control group was given 0.9wt% sodium chloride injection to soak the absorbent gauze; positive control was given 1-chloro-2, 4-dinitrobenzene to soak the absorbent gauze), all test animals in the test group were challenged on the shaved untested sites with the test example. And skin reactions were graded at the challenge sites for all animals 24h, 48h after patch removal. The negative control group animals were operated in the same manner.
As a result: no application test reaction is seen on the skin of the excitation part of the test group animal and the negative control group animal, the scoring grades are 0, and the sensitization incidence rate is 0.
And (4) conclusion: under the present test conditions, the test examples did not cause skin sensitization in guinea pigs in the guinea pig skin sensitization test.
The experimental method comprises the following steps: negative control: 0.9wt% sodium chloride injection and water-absorbing gauze, storing under sealed condition.
Preparing a test article: 0.5 mL/part of the product prepared in example 3 was soaked in 2.5cm × 2.5cm absorbent gauze; negative control A2.5 cm by 2.5cm absorbent gauze was soaked with 0.5 mL/portion of 0.9wt% sodium chloride injection.
Preparation of positive control: inducing, weighing 100mg of 1-chloro-2, 4-dinitrobenzene, adding 75wt% ethanol solution to prepare 1wt% solution, and soaking 0.5 mL/part of 2.5cm × 2.5cm water-absorbing gauze; 50mg of 1-chloro-2, 4-dinitrobenzene is weighed and added with 75wt% ethanol solution to prepare 0.1wt% solution, and 0.5 mL/part of water-absorbing gauze with the thickness of 2.5cm multiplied by 2.5cm is soaked.
The test method comprises the following steps: preparing: all test site furs of the animals were shaved before the start of the test, and healthy, skin-intact animals were selected for the test.
An induction stage: a2.5 cm by 2.5cm absorbent gauze was soaked with 0.5 mL/portion of the sample, placed on cellophane, and fixed to the upper left back of each animal with a pressure sensitive adhesive tape. The fixture and the applicator were removed after 6 h. This procedure was repeated for 3 consecutive days a week, and continued for 3 weeks as described above. The control animals were treated in the same manner as above by impregnating a 2.5cm x 2.5cm absorbent gauze with 0.5 mL/portion of 0.9wt% NaCl injection.
And (3) an excitation phase: all test and control animals were challenged with the test example 14d after the last induction application.
A2.5 cm × 2.5cm absorbent gauze soaked in 0.5 mL/portion of test example was placed on a glass paper of the same size, and the gauze was fixed to the upper right back of each animal by pressure-sensitive adhesive tape sealing. After 6h the fixtures and patches were removed, and 24h the affected area and surrounding animal hair were shaved off and the hair area was washed away with warm water.
The induction date: 23/8/2021-25/8/2021; 23/8/2021-1/9/1/2021; 6/2021/9/8/2021/9/2021; excitation date: 2021, 9 and 22 months.
And (4) observation: the skin reactions at the challenge sites of the test and control animals were observed 24h, 48h after removal of the patch and the skin erythema and edema responses at each challenge site and each observation time were described and graded according to Magnusson and Kligman grading standards. Grade: 0: no obvious change is caused; 1: diffuse or mottled erythema; 2: moderate fusional erythema; 3: severe erythema and/or edema.
And (4) observing results: all animals in the test group and the negative control group did not perform abnormally during the test.
Sensitization reaction result: no application test reaction is seen on the skin of the excitation part of the test group animal and the negative control group animal, no obvious sensitization reaction symptom is observed, the rating is 0, and the sensitization incidence rate is 0. Details are given in table 4.
After the positive control group animals are excited (24 hours and 48 hours), obvious application test reactions can be seen on the skin of the excited part (the positive control test is carried out every 6 months in the laboratory), the average score of the animals after the positive control group animals are excited is 3.0, and the sensitization incidence rate is 100wt%; the average score of the animals after 48 hours of excitation is 1.8, and the sensitization incidence rates are all 100wt%. See table 5 for details.
TABLE 4 results of sensitization test observations
TABLE 5 Observation of sensitization-positive reaction test
And (4) conclusion: under the present test conditions, the test examples did not cause skin sensitization in guinea pigs in the guinea pig skin sensitization test.
Finally, it should be noted that: the above description is only a preferred embodiment of the present invention, and is not intended to limit the scope of the present invention. Any modification, equivalent replacement, or improvement made within the spirit and principle of the present invention should be included in the protection scope of the present invention.
Claims (9)
1. The recombinant III-type humanized triple-helical-structure collagen dressing is characterized by being prepared from the following raw materials in parts by mass:
0.03-0.10 wt% of recombinant III type humanized triple-helical structure collagen, 0.06-0.18 wt% of D- (+) -trehalose dihydrate, 0.2-0.8 wt% of carbomer, 1.5-3.5 wt% of butanediol, 1-2.5 wt% of glycerol, 0.1-0.5 wt% of triethanolamine and the balance of purified water.
2. The recombinant III type humanized triple-helical structure collagen dressing according to claim 1, which is prepared by the following raw materials in percentage by mass:
0.07wt% of recombinant III type humanized triple-helical-structure collagen, 0.15wt% of D- (+) -trehalose dihydrate, 0.5wt% of carbomer, 3wt% of butanediol, 2wt% of glycerol, 0.35wt% of triethanolamine and the balance of purified water.
3. Use of the recombinant type iii humanized triple-helical-structure collagen dressing according to claim 1 or 2 in the preparation of a finished recombinant type iii humanized triple-helical-structure collagen gel or a finished recombinant type iii collagen stock solution.
4. A method for preparing a finished product of a recombinant type iii humanized triple-helical-structure collagen gel, which is prepared by using the recombinant type iii humanized triple-helical-structure collagen dressing as claimed in claim 1 or 2, and comprises the following steps:
(1) Selecting carbomer and purified water according to corresponding mass fraction, and emulsifying at homogenizing speed of 20-30HZ to obtain a spare substance A;
(2) Selecting triethanolamine and purified water according to corresponding mass fractions, and mixing and dissolving to obtain a standby substance B;
(3) Selecting recombinant III type humanized triple-helical-structure collagen according to corresponding mass fractions, and mixing and dissolving the recombinant III type humanized triple-helical-structure collagen with purified water to obtain a spare substance C;
(4) Selecting glycerol, butanediol and D- (+) -trehalose dihydrate according to corresponding mass fractions, stirring and mixing, mixing with the standby substance A, homogenizing, heating to 80-90 ℃, keeping the temperature for 20-30min, cooling to 50-60 ℃, adding the standby substance B, and stirring;
(5) And continuously cooling to not higher than 45 ℃, adding the standby material C, homogenizing until the material body is uniformly dispersed, clarified and transparent, filtering, and discharging to obtain a finished product.
5. The method for preparing the recombinant III type humanized triple-helical-structure collagen gel finished product according to claim 4, wherein in the step (4), when the glycerol, the butanediol and the D- (+) -trehalose dihydrate are stirred and mixed, the stirring time is 3-5 minutes, and the stirring speed is 600-800 r/min;
during the homogenization treatment, high-speed homogenization is adopted for 5-8 minutes, and the homogenization speed is 30-40HZ;
and when the standby material B is added and stirred, homogenizing at a low speed of 20-30HZ, and fully stirring for 2-3 minutes at a stirring speed of 15-20HZ for stirring treatment.
6. The method for preparing a recombinant III-type humanized triple-helical structure collagen gel product according to claim 4, wherein in the step (5), the homogenization treatment time is 3-5 minutes, and the homogenization treatment speed is 15-20HZ;
and 200-400 meshes of filter cloth is adopted during filtering.
7. A method for preparing a recombinant type iii humanized triple-helical-structure collagen stock solution finished product, which is prepared by using the recombinant type iii humanized triple-helical-structure collagen dressing as claimed in claim 1 or 2, and comprises the following steps:
(1) Selecting triethanolamine and purified water according to corresponding mass fraction, mixing and dissolving to obtain a standby substance A;
(2) Selecting recombinant III type humanized triple-helical-structure collagen and purified water according to corresponding mass fractions, and mixing and dissolving to obtain a spare substance B;
(3) Selecting glycerol, butanediol and D- (+) -trehalose dihydrate according to corresponding mass fractions, stirring and mixing, adding carbomer and purified water, heating, homogenizing, keeping the temperature for 20-30min, cooling to 50-60 ℃, adding the standby substance A, and stirring and mixing;
(4) And continuously cooling to not higher than 45 ℃, adding the standby material B, homogenizing until the material body is uniformly dispersed, clear and transparent, filtering, and discharging to obtain a finished product.
8. The method for preparing a recombinant III-type humanized triple-helical-structure collagen raw liquid finished product according to claim 7, wherein in the step (3), when the glycerol, the butanediol and the D- (+) -trehalose dihydrate are stirred and mixed, the stirring time is 3-5 minutes, and the stirring speed is 600-800 rpm;
heating to 85-92 deg.C, homogenizing at 30-40Hz for 5-8 min;
and when the standby material A is added, stirring and mixing, homogenizing at a low speed of 20-30HZ, and fully stirring for 2-3 minutes at a stirring speed of 15-20HZ for stirring treatment.
9. The method for preparing a recombinant III-type humanized triple-helical structure collagen solution as claimed in claim 7, wherein in the step (4), the homogenization treatment time is 3-5 minutes, and the homogenization treatment speed is 15-20HZ;
and 200-400 meshes of filter cloth is adopted during filtering.
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Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN115804864A (en) * | 2023-01-29 | 2023-03-17 | 南京天纵易康生物科技股份有限公司 | Synergistic promotion and repair heat-stable recombinant III-type humanized collagen gel and preparation method thereof |
| CN116688212A (en) * | 2023-07-11 | 2023-09-05 | 湖南银华棠医药科技有限公司 | III type recombinant collagen dressing with repairing and anti-aging effects and preparation method and application thereof |
| CN117064787A (en) * | 2023-09-01 | 2023-11-17 | 海南德诺海思生物科技有限公司 | Recombinant III type humanized collagen dressing mask for damaged skin barrier and preparation method thereof |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112088903A (en) * | 2020-09-28 | 2020-12-18 | 武汉愔紫生物科技有限公司 | Application of macromolecular protein in antibacterial and antiviral disinfectant |
| CN113304310A (en) * | 2021-06-04 | 2021-08-27 | 吉林省国大生物工程有限公司 | Medical wet dressing with repairing function and preparation method thereof |
| CN114191597A (en) * | 2021-12-16 | 2022-03-18 | 湖南银华棠医药科技有限公司 | Liquid dressing for repairing skin wound surface and preparation method and application thereof |
| CN114470314A (en) * | 2022-02-15 | 2022-05-13 | 海雅美生物技术(珠海)有限公司 | Recombinant humanized collagen gel dressing and preparation method and application thereof |
| CN114835920A (en) * | 2022-05-20 | 2022-08-02 | 湖南科妍创美医疗科技有限公司 | Recombinant collagen-polyglutamate hydrogel and preparation method thereof |
-
2022
- 2022-10-27 CN CN202211330068.7A patent/CN115475277A/en active Pending
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112088903A (en) * | 2020-09-28 | 2020-12-18 | 武汉愔紫生物科技有限公司 | Application of macromolecular protein in antibacterial and antiviral disinfectant |
| CN113304310A (en) * | 2021-06-04 | 2021-08-27 | 吉林省国大生物工程有限公司 | Medical wet dressing with repairing function and preparation method thereof |
| CN114191597A (en) * | 2021-12-16 | 2022-03-18 | 湖南银华棠医药科技有限公司 | Liquid dressing for repairing skin wound surface and preparation method and application thereof |
| CN114470314A (en) * | 2022-02-15 | 2022-05-13 | 海雅美生物技术(珠海)有限公司 | Recombinant humanized collagen gel dressing and preparation method and application thereof |
| CN114835920A (en) * | 2022-05-20 | 2022-08-02 | 湖南科妍创美医疗科技有限公司 | Recombinant collagen-polyglutamate hydrogel and preparation method thereof |
Non-Patent Citations (1)
| Title |
|---|
| 姜锡瑞: "《生物发酵产业技术》", 30 May 2016, 中国轻工业出版社, pages: 327 * |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN115804864A (en) * | 2023-01-29 | 2023-03-17 | 南京天纵易康生物科技股份有限公司 | Synergistic promotion and repair heat-stable recombinant III-type humanized collagen gel and preparation method thereof |
| CN116688212A (en) * | 2023-07-11 | 2023-09-05 | 湖南银华棠医药科技有限公司 | III type recombinant collagen dressing with repairing and anti-aging effects and preparation method and application thereof |
| CN116688212B (en) * | 2023-07-11 | 2024-03-08 | 湖南银华棠医药科技有限公司 | III type recombinant collagen dressing with repairing and anti-aging effects and preparation method and application thereof |
| CN117064787A (en) * | 2023-09-01 | 2023-11-17 | 海南德诺海思生物科技有限公司 | Recombinant III type humanized collagen dressing mask for damaged skin barrier and preparation method thereof |
| CN117064787B (en) * | 2023-09-01 | 2024-05-14 | 海南德诺海思生物科技有限公司 | Recombinant III type humanized collagen dressing mask for damaged skin barrier and preparation method thereof |
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