CN101314058A - Modification method for animal skin collagen - Google Patents

Modification method for animal skin collagen Download PDF

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Publication number
CN101314058A
CN101314058A CNA2007100491732A CN200710049173A CN101314058A CN 101314058 A CN101314058 A CN 101314058A CN A2007100491732 A CNA2007100491732 A CN A2007100491732A CN 200710049173 A CN200710049173 A CN 200710049173A CN 101314058 A CN101314058 A CN 101314058A
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China
Prior art keywords
collagen
bulk material
value
weight portions
genipin
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CNA2007100491732A
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Chinese (zh)
Inventor
但卫华
林海
但年华
黄惠兴
刘汝诚
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JIANGYIN BENXIANG BIOTECHOLOGY CO Ltd
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JIANGYIN BENXIANG BIOTECHOLOGY CO Ltd
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Priority to CNA2007100491732A priority Critical patent/CN101314058A/en
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Abstract

The invention discloses a method for modifying a collagen body of animal skin, which is characterized in that: 100 weight portions of collagen body material is taken and is added into 800 to 2,000 weight portions of 40 to 80v/v percent alcohol solution of 2-N-morpholino ethanesulfonic acid (MES) with a concentration between 20 and 70mmol/L and a pH value between 5.0 and 6.0 or a phosphate buffer solution (PBS) with the pH value between 5.0 and 6.0, the mixture is oscillated for 15 to 60min, then is respectively added with 2 to 30 weight portions of 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) and N-hydroxysuccinimide (NHS), is oscillated for 4 to 24h at room temperature to produce a collagen body modification material; or 100 weight portions of the collagen body material is taken, is added into 800 to 2,000 weight portions of the phosphate buffer solution (PBS) with the pH value between 6.0 and 8.0, is oscillated for 15 to 60min, then is added with 3 to 15 weight portions of genipin, and is oscillated for 10 to 24h at a temperature of between 20 and 40 DEG C to produce the collagen body modification material; then a monobasic sodium phosphate solution with the concentration of 0.1mol/L, the phosphate buffer solution with the pH value between 7.2 and 7.4 and double distilled water are orderly used to repeatedly clean the collagen body modification material, each cleaning time is not less than 60min, the cleaning time of each cleaning solution is not less than 3h, and the total cleaning time reaches more than 24h; and finally a modified collagen body material is produced by freeze drying.

Description

A kind of method of animal skin collagen modification
Technical field
The present invention relates to a kind of method of animal skin collagen being carried out modification with modifier such as carbodiimides, genipin.
Background technology
Collagen protein from animal skins, not only has unique physicochemical property, but also have premium properties such as excellent biological compatibility, biodegradable, hypoimmunity and anthemorrhagic performance, especially it is absorbed in animal body easily, hydrophilic is strong, have no side effect, safety is good, thereby is considered to one of ideal biomedical material.The collagen protein that is derived from animal skins can be divided into two classes, i.e. collagen body and hydrolytic collagen.The collagen body is meant with collagen to be that the animal tissue or the organ of main component is primary raw material, without or handle through a spot of chemistry or physical method, keep the animal tissue or the organ of natural collagen structure and character.
At present, all less relatively about the document of collagen body purification and modification both at home and abroad.But people such as Wei Hua utilize the natural animal skin to be primary raw material, carry out purification and the final collagen bulk material that obtains through a series of physics chemical action, keep natural collagen structure and character to a great extent and (but defended China, Liao Longli, Li Zhiqiang, etc. the acellular dermal matrix preparation methods. Chinese invention patent .200410022506.9).Collagen bulk material with this prepared has mechanical strength height, faint antigenicity, is easy to characteristics such as machine-shaping, has the potentiality that are applied to biomedical sector, as body surface repair in trauma material, artificial skin host material etc.In addition, people such as Chai Jiake also utilize Corii Sus domestica to be primary raw material, optionally go cell and with its as the artificial skin sub (Chai Jiake, Yang Hongming, Liu Qiang. selectivity goes the cell Corii Sus domestica as application of human body skin sub and preparation method thereof. Chinese invention patent .200303148291.0).
Though the collagen bulk material has excellent physical and mechanical properties, biology performance etc., the instability of its significant disadvantages such as degradation property has still limited its application as bio-medical material largely.Search to the bottom, the basic skills that changes this situation is that the cross-linked form of collagen fiber in the collagen bulk material and crosslinking degree are reached controlled grasp.In multiple modifying agent and method of modifying, carbodiimides and genipin have certain advantage.
1-ethyl-3-(3-dimethylaminopropyl) carbodiimides (1-ethyl-3-(3-dimethylaminopropyl) carbodiimide, EDC) be the agent of a kind of water miscible distance of zero mark degree protein cross, along with people to the further cognition of its modified-reaction ultimate principle and to the further approval of its modification characteristic make carbodiimides application more and more widely.At home and abroad, research about carbodiimides mainly is that tissue engineering bracket material or artificial skin sub are carried out modification, not only improve the physical and mechanical properties of material, stability [Heather M.Power, Steven T.Boyce.EDC cross-linking improves skin substitute strength and stability[J] .Biomaterials, 2006,27:5821-5827. Liu Ling Rong, Zhang Lihai, Ma Ruidong etc. the crosslinked collagen-chondroitin sulfate timbering material of carbodiimides makes up the research [J] of artificial dermis. Chinese reconstruction surgical magazine, 2003,17 (2): 83-87.], also further improve simultaneously the biocompatibility and combination property [the Heather M.Power of material, Steven T. Boyce.Wound closurewith EDC cross-linked cultured skin substitutes grafted to athymic mice[J] .Biomaterials.2006,10:1-9.].
Genipin is one of active component of the Chinese medicine Cortex Eucommiae, separates from geniposide, purifies and obtain.The Cortex Eucommiae is a kind of deciduous tree that belongs to Eucommiaceae, is China's special product, mainly is distributed in central and west regions.On chemical constitution, genipin is a kind of heterocyclic compound of iridoids, has a plurality of active function groups such as hydroxyl, carboxyl.Though have in recent years researcher begin to pay close attention to genipin [Dinke is firm. the reactivity research [J] of genipin and collagen. Chinese leather .2007,36 (5): 10-12,16.Butler, Michael F., Ng, Yiu-Fai; Pudney, Paul D.A.Mechanismand kinetics of the crosslinking reaction between biopolymers containing primary aminegroups and genipin[J] .Journal of Polymer Science, Part A:Polymer Chemistry.2003,41 (24): 3941-3953.], but its mechanism of crosslinking is still very not clear and definite, but confirmed that modifying process is spontaneous, and had extremely low cytotoxicity and genotoxicity.People such as Jin Xunjie compare with regard to the biological characteristics of genipin modified gelatin sill and glutaraldehyde modified gelatin sill, substantially think that genipin has better biology performance [Jin Xunjie, Yang Xiansheng, Ji Ye, Deng. the biological characteristics of protein-crosslinking agent genipin and glutaraldehyde is [J] relatively. Chinese clinical rehabilitation .2006,10 (25): 60-62.].In China Taiwan, early begin the correlational study of genipin, and obtained certain achievement [Fwu-Long Mi; Shin-Shing Shyu; Chih-Kang Peng.Characterization of ring-openingpolymerization of genipin and pH-dependent cross-linking reactions between chitosan andgenipin[J] .Journal of Polymer Science, Part A (Polymer Chemistry) .2005,43 (10): 1985-2000.Liang, Huang-Chien; Chang, Wen-Hisung; Liang, Hsiang-Fa; Etal.Crosslinkingstructures of gelatin hydrogels crosslinked with genipin or a water-soluble carbodiimide[J] .Journal ofApplied Polymer Science.2004,91 (6): 4017-4026.].Abroad, the research worker is used for the study on the modification of the various materials of organizational project with genipin, as medicament slow release material [Jin, J.; Song, M.Chitosan andchitosan-PEO blend membranes crosslinked by genipin for drug release[J] .Journal ofApplied Polymer Science.2006,102 (1): 436-44.], degradable type PEG gel [Moffat, Kristen L., Marra, Kacey G.Biodegradable poly (ethylene glycol) hydrogels crosslinked with genipin fortissue engineering applications[J] .Journal of Biomedical Materials Research-Part BApplied Biomaterials.2004,71 (1): 181-187.]
Up to the present, still not having documents and materials both at home and abroad utilizes carbodiimides or genipin the collagen bulk material to be carried out the report of modification.Therefore, utilize animal skins to prepare the collagen bulk material and adopt carbodiimides or genipin carries out modification for primary raw material, further strengthen the combination property of collagen bulk material, the application of expanding its biomedical sector is a kind of opening one's minds of being significant.
In sum, technology has the following disadvantages now:
1. prior art adopts chemical method such as glutaraldehyde or adopts physical methods such as irradiation, hot dehydrogenation that the collagen bulk material that is applied to biomedical sector is carried out modification, has certain cytotoxicity or crosslinking degree and is difficult to shortcomings such as control.
2. prior art employing carbodiimides or genipin mainly concentrate on natural macromolecular materials such as hydrolytic collagen, chitosan to the modification of tissue engineering bracket material, have ignored the feasibility and the potentiality that are applied to the collagen bulk material.
Summary of the invention
The objective of the invention is to provides a kind of range of application more broad collagen bulk material and method of modifying thereof for biomedical sector, be characterized in utilizing the natural animal skin to obtain the collagen bulk material for raw material, through obtaining the collagen bulk material after the carbodiimides of specified conditions or the genipin modification, have advantages such as reaction condition gentleness, crosslinking degree be controlled.
The objective of the invention is to realize that wherein said raw material umber is parts by weight except that specifying by following technical measures:
100 parts of collagen bulk materials (thickness 0.1-1.0mm)
2~30 parts of carbodiimides
3~15 parts of genipin
Described collagen bulk material is to be the qualified cell collagen bulk material that takes off of primary raw material preparation with the animal skin.
Described carbodiimides, genipin are commercially available analytical reagent.The chemical reagent that other is addressed is commercially available analytical pure material without specified otherwise, and uses preceding without operations such as any purifications.
Above-mentioned collagen bulk material adopts the method for modifying of carbodiimides, and it is characterized in that: described method is to divide 4 steps according to following technology:
(1) pH value is regulated
Take by weighing collagen bulk material 100 weight portions, adding 800~2000 weight portion concentration is 20~70mmol/L, pH value is 5.0~6.0 2-N-morpholino ethane sulfonic acid (2-N-morpholino ethanesulfonic acid, MES) in 40~80v/v% alcoholic solution or pH value be in 5.0~6.0 the phosphate buffer (PBS), vibration 15~60min;
(2) modification
In above-mentioned pH value regulator solution, add respectively the EDC of 2~30 weight portions and N-maloyl imines (N-hydroxysuccinimide, NHS), room temperature condition down vibration 4~24h to obtain the collagen body material modified;
(3) clean
Clean repeatedly with sodium dihydrogen phosphate, the phosphate buffer of pH 7.2~7.4, the distilled water of 0.1mol/L successively above-mentioned collagen body is material modified, the each cleaning is no less than 60 min, every kind of cleanout fluid cleans and is no less than 3h, and the total scavenging period of accumulative total reaches more than the 24h;
(4) drying
Collagen bulk material lyophilization after the above-mentioned cleaning is promptly obtained the modified collagen bulk material.
Above-mentioned collagen bulk material adopts the method for modifying of genipin, and it is characterized in that: described method is to divide 4 steps according to following technology:
(1) pH value is regulated
Take by weighing collagen bulk material 100 weight portions, add 800~2000 weight portion pH value and be in 6.0~8.0 the phosphate buffer (PBS), vibration 15~60min;
(2) modification
In above-mentioned pH value regulator solution, add the genipin of 3~15 weight portions, it is material modified that the 10~24h that vibrates under 20~40 ℃ of conditions obtains the collagen body;
(3) clean
Clean repeatedly with sodium dihydrogen phosphate, the phosphate buffer of pH 7.2~7.4, the distilled water of 0.1mol/L successively above-mentioned collagen body is material modified, the each cleaning is no less than 30min, every kind of cleanout fluid cleans and is no less than 1h, and the total scavenging period of accumulative total reaches more than the 3h;
(4) drying
Collagen bulk material lyophilization after the above-mentioned cleaning is promptly obtained the modified collagen bulk material.
In view of collagen particular structure and performance, the research of collagen base biological medical material is subjected to especially paying close attention to.The collagen bulk material has acted on the good characteristic of collagen protein, have performances such as biocompatibility, biodegradable, after passing through carbodiimides or genipin modification simultaneously, overcome the shortcoming of material itself, and can reach the purpose controlled by the control of modification degree, thereby expand the application category of collagen bulk material greatly the target material degradation property.Compare with the existing processes technology, the present invention has the following advantages:
(1) simple, the mild condition of modified technique, easy operating, the practical situation of incorporating collagen bulk material improves process conditions, gives full play to the efficient of modifier;
(2) the collagen bulk material biocompatibility that utilizes carbodiimides or genipin modification to obtain is fabulous, and excellent combination property has further been expanded the application category of collagen bulk material.
The specific embodiment
Below by implementing that the present invention is carried out concrete description; be necessary to be pointed out that at this present embodiment only is used for the present invention is further specified; and can not be interpreted as limiting the scope of the invention, the person skilled in the art in this field can make some nonessential improvement and adjustment according to the content of foregoing invention.
Embodiment 1
(1) pH value is regulated
Take by weighing collagen bulk material 100 weight portions, adding 800 weight portion concentration is 70mmol/L, and pH value is in the 80v/v% alcoholic solution of 6.0 MES, vibration 15min;
(2) modification
In above-mentioned pH value regulator solution, add the EDC and the NHS of 30 weight portions respectively, room temperature condition vibration 4h acquisition collagen body down is material modified;
(3) clean
Clean repeatedly with sodium dihydrogen phosphate, the phosphate buffer of pH 7.2, the distilled water of 0.1mol/L successively above-mentioned collagen body is material modified, the each cleaning is no less than 60min, every kind of cleanout fluid cleans and is no less than 3h, and the total scavenging period of accumulative total reaches more than the 24h;
(4) drying
Collagen bulk material lyophilization after the above-mentioned cleaning is promptly obtained the modified collagen bulk material.
Embodiment 2
(1) pH value is regulated
Take by weighing collagen bulk material 100 weight portions, adding 2000 weight portion concentration is 20mmol/L, and pH value is in the 40v/v% alcoholic solution of 5.0MES, vibration 60min;
(2) modification
In above-mentioned pH value regulator solution, add the EDC and the NHS of 2 weight portions respectively, room temperature condition vibration 24h acquisition collagen body down is material modified;
(3) clean
Clean repeatedly with sodium dihydrogen phosphate, the phosphate buffer of pH 7.4, the distilled water of 0.1mol/L successively above-mentioned collagen body is material modified, the each cleaning is no less than 60min, every kind of cleanout fluid cleans and is no less than 3h, and the total scavenging period of accumulative total reaches more than the 24h;
(4) drying
Collagen bulk material lyophilization after the above-mentioned cleaning is promptly obtained the modified collagen bulk material.
Embodiment 3
(1) pH value is regulated
Take by weighing collagen bulk material 100 weight portions, adding 1200 weight portion concentration is 50mmol/L, and pH value is in the phosphate buffer (PBS) of 5.5 MES, vibration 60min;
(2) modification
In above-mentioned pH value regulator solution, add the EDC and the NHS of 15 weight portions respectively, room temperature condition vibration 8h acquisition collagen body down is material modified;
(3) clean
Clean repeatedly with sodium dihydrogen phosphate, the phosphate buffer of pH 7.2, the distilled water of 0.1mol/L successively above-mentioned collagen body is material modified, the each cleaning is no less than 60min, every kind of cleanout fluid cleans and is no less than 3h, and the total scavenging period of accumulative total reaches more than the 24h;
(4) drying
Collagen bulk material lyophilization after the above-mentioned cleaning is promptly obtained the modified collagen bulk material.
Embodiment 4
(1) pH value is regulated
Take by weighing collagen bulk material 100 weight portions, add 800 weight portion pH value and be in 6.0 the phosphate buffer (PBS), vibration 60min;
(2) modification
In above-mentioned pH value regulator solution, add the genipin of 3 weight portions, vibration 24h acquisition collagen body is material modified under 20 ℃ of conditions;
(3) clean
Clean repeatedly with sodium dihydrogen phosphate, the phosphate buffer of pH 7.2, the distilled water of 0.1mol/L successively above-mentioned collagen body is material modified, the each cleaning is no less than 30min, every kind of cleanout fluid cleans and is no less than 1h, and the total scavenging period of accumulative total reaches more than the 3h;
(4) drying
Collagen bulk material lyophilization after the above-mentioned cleaning is promptly obtained the modified collagen bulk material.
Embodiment 5
(1) pH value is regulated
Take by weighing collagen bulk material 100 weight portions, add 2000 weight portion pH value and be in 8.0 the phosphate buffer (PBS), vibration 15min;
(2) modification
In above-mentioned pH value regulator solution, add the genipin of 15 weight portions, vibration 10h acquisition collagen body is material modified under 40 ℃ of conditions;
(3) clean
Clean repeatedly with sodium dihydrogen phosphate, the phosphate buffer of pH 7.4, the distilled water of 0.1mol/L successively above-mentioned collagen body is material modified, the each cleaning is no less than 30min, every kind of cleanout fluid cleans and is no less than 1h, and the total scavenging period of accumulative total reaches more than the 3h;
(4) drying
Collagen bulk material lyophilization after the above-mentioned cleaning is promptly obtained the modified collagen bulk material.
Embodiment 6
(1) pH value is regulated
Take by weighing collagen bulk material 100 weight portions, add 1600 weight portion pH value and be in 7.5 the phosphate buffer (PBS), vibration 40min;
(2) modification
In above-mentioned pH value regulator solution, add the genipin of 10 weight portions, vibration 16h acquisition collagen body is material modified under 35 ℃ of conditions;
(3) clean
Clean repeatedly with sodium dihydrogen phosphate, the phosphate buffer of pH 7.2, the distilled water of 0.1mol/L successively above-mentioned collagen body is material modified, the each cleaning is no less than 30min, every kind of cleanout fluid cleans and is no less than 1h, and the total scavenging period of accumulative total reaches more than the 3h;
(4) drying
Collagen bulk material lyophilization after the above-mentioned cleaning is promptly obtained the modified collagen bulk material.

Claims (3)

1. the method for an animal skin collagen modification is characterized in that with the animal skin being the collagen bulk material of primary raw material preparation, and commercially available carbodiimides and genipin are primary raw material.Obtain the collagen bulk material of modification through processes such as pH value adjusting, modification, cleaning, dryings.Wherein, the percentage by weight of each component raw material composition is counted:
100 parts of collagen bulk materials (thickness 0.1-1.0mm)
2~30 parts of carbodiimides
3~15 parts of genipin
2. the carbodiimides method of modifying of collagen bulk material as claimed in claim 1 is characterized in that this method may further comprise the steps:
(1) pH value is regulated
Take by weighing collagen bulk material 100 weight portions, adding 800~2000 weight portion concentration is 20~70mmol/L, pH value is 5.0~6.0 2-N-morpholino ethane sulfonic acid (2-N-morpholino ethanesulfonic acid, MES) in 40~80v/v% alcoholic solution or pH value be in 5.0~6.0 the phosphate buffer (PBS), vibration 15~60min;
(2) modification
In above-mentioned pH value regulator solution, 1-ethyl-3-(3-dimethylaminopropyl) carbodiimides (1-ethyl-3-(3-dimethylaminopropyl) carbodiimide that adds 2~30 weight portions respectively, EDC) and N-maloyl imines (N-hydroxysuccinimide, NHS), vibration 4~24h acquisition collagen body is material modified down for room temperature condition;
(3) clean
Clean repeatedly with sodium dihydrogen phosphate, the phosphate buffer of pH 7.2~7.4, the distilled water of 0.1mol/L successively above-mentioned collagen body is material modified, the each cleaning is no less than 60min, every kind of cleanout fluid cleans and is no less than 3h, and the total scavenging period of accumulative total reaches more than the 24h;
(4) drying
Collagen bulk material lyophilization after the above-mentioned cleaning is promptly obtained the modified collagen bulk material.
3. the genipin method of modifying of collagen bulk material as claimed in claim 1 is characterized in that this method may further comprise the steps:
(1) pH value is regulated
Take by weighing collagen bulk material 100 weight portions, add 800~2000 weight portion pH value and be in 6.0~8.0 the phosphate buffer (PBS), vibration 15~60min;
(2) modification
In above-mentioned pH value regulator solution, add the genipin of 3~15 weight portions, it is material modified that the 10~24h that vibrates under 20~40 ℃ of conditions obtains the collagen body;
(3) clean
Clean repeatedly with sodium dihydrogen phosphate, the phosphate buffer of pH 7.2~7.4, the distilled water of 0.1mol/L successively above-mentioned collagen body is material modified, the each cleaning is no less than 30min, every kind of cleanout fluid cleans and is no less than 1h, and the total scavenging period of accumulative total reaches more than the 3h;
(4) drying
Collagen bulk material lyophilization after the above-mentioned cleaning is promptly obtained the modified collagen bulk material.
CNA2007100491732A 2007-05-28 2007-05-28 Modification method for animal skin collagen Pending CN101314058A (en)

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Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
ITVI20130233A1 (en) * 2013-09-24 2015-03-25 Gruppo Mastrotto S P A PROCEDURE FOR THE TANNING OF LEATHER WITH TRIAZINE DERIVATIVES
CN104874012A (en) * 2015-05-05 2015-09-02 四川大学 Fluffy type skin collagen hemostatic material and preparation method thereof
CN105497979A (en) * 2015-12-24 2016-04-20 中国科学院遗传与发育生物学研究所 Functional material with controllable degradation rate and nerve regeneration guiding function as well as preparation method and application of functional material
CN109432489A (en) * 2018-12-29 2019-03-08 无锡贝迪生物工程股份有限公司 A kind of collagen hemostasis cellucotton and preparation method thereof

Cited By (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
ITVI20130233A1 (en) * 2013-09-24 2015-03-25 Gruppo Mastrotto S P A PROCEDURE FOR THE TANNING OF LEATHER WITH TRIAZINE DERIVATIVES
WO2015044971A3 (en) * 2013-09-24 2015-07-16 Gruppo Mastrotto S.P.A. Process for tanning leathers with triazine derivatives
CN104874012A (en) * 2015-05-05 2015-09-02 四川大学 Fluffy type skin collagen hemostatic material and preparation method thereof
CN104874012B (en) * 2015-05-05 2017-05-31 四川大学 Fluff type collagen hemostatic material and preparation method thereof
CN105497979A (en) * 2015-12-24 2016-04-20 中国科学院遗传与发育生物学研究所 Functional material with controllable degradation rate and nerve regeneration guiding function as well as preparation method and application of functional material
CN109432489A (en) * 2018-12-29 2019-03-08 无锡贝迪生物工程股份有限公司 A kind of collagen hemostasis cellucotton and preparation method thereof
CN109432489B (en) * 2018-12-29 2021-05-28 无锡贝迪生物工程股份有限公司 Collagen hemostatic cellucotton and preparation method thereof

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Application publication date: 20081203