Influence of crosslinking on the biological and physical properties of collagen
- VernacularTitle:交联对胶原生物学和物理性能的影响
- Author:
Chunrong YANG
- Publication Type:Journal Article
- From:
Chinese Journal of Tissue Engineering Research
2007;0(03):-
- CountryChina
- Language:Chinese
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Abstract:
BACKGROUND:Water-soluble 1-ethyl-3-(3-dimethyl aminopropyl) carbodiimide(EDC) and N-hydroxysuccinimide(NHS) are non-toxic and good biocompatible crosslinking agents which can trigger collagen to crosslink and form amide bond.OBJECTIVE:To analysis the influence of crosslinking on the biological and physical properties of collagen.DESIGN,TIME AND SETTING:A crosslinking experiment of collagen was performed at the Laboratory in Department of Materials Science and Engineering of Fujian University of Technology from September to November 2008.MATERIALS:Ⅰ-type bovine collagen solution was provided by Guangzhou Chuang'er Company.EDC and NHS,as the crosslinking agents,were provided by Shanghai Gill Biochemical Company and Shanghai Bo'ao Biological Technology Limited Company,respectively.2-(N-Morpholino) ethane sulfonic acid(MES),as a buffer,was provided by Shanghai Juyuan Biological Technology Limited Company.METHODS:Collagen solution was freezed at -80 ℃ for 12 hours in refrigerator.After vacuum freeze-drying 24 hours for complete dehydration in freeze-drying equipment,collagen matrices were obtained.The collagen matrices were immersed into different concentration of EDC.NHS was added according to EDC:NHS=4:1.The MES was as the buffer to adjust pH to 3.0.Then the solution was treated as follow:washed by deionized water,vacuum freeze-drying for complete dehydration.MAIN OUTCOME MEASURES:The microstructure,shrinkage temperature,characteristics of swelling dynamics and ability of antidegradation of collagen before and after crosslinking were analyzed.RESULTS:The studies of collagen crosslinking showed that the free -NH2 functional group of collagen molecules changed into N-H functional group after crosslinking,and the amino-link formed between collagen molecules.When the concentration of EDC reached 2 g/L,the crosslinking achieved to the greatest degree.After crosslinking,the microstructure of collagen changed from a state of disorder into the close and orderly structure,and the thermal stability and shape stability enhanced.In addition,the ability to antidegradation also significantly increased after crosslinking.CONCLUSION:Using EDC and NHS as crosslinking agents,crosslinking treatment can effectively improve the biological and physiochemical properties of collagen as bone tissue engineering material.
