A Reviewon Chemical stabilizationmethods of collagen

Collagen is an important biomaterial finding several applications as prosthesis, artificial tissue, drugcarrier and cosmetics [1].Generally, the isolated collagen from skin or tendon exhibits poor thermalstability, mechanical strength and water resistance, due to the destruction of natural cross-linking andassembly structure by neutral salt, acid, alkali, or proteases during the extraction process [2].Therefore,they are often modified for practical uses by various methods. Generally, methods applied to stabilizecollageninclude chemical crosslinking and/or physical treatments (dehydrothermal, radiation). Chemicalreactions are favored by the largenumber of collagen functional side groups [3]. This can be achieved by anumber of different cross-linking agents that react with specific amino acid residues on the collagenmolecule imparting individual biochemical, thermal and mechanical characteristics to thebiomaterial.Actually stabilizationof collagen reduces itsantigenicity and the rate of biodegradation andimproves thethermal and mechanical stability [4].The interaction of these agents may occur with the ε-amino group of lysine residues, the carboxyl groups of glutamic and aspartic acids, or with hydroxylgroups [5].Accordingly, in this paper we review and classify chemical stabilization methods and crosslinkingagents for collagen.

کلیدواژه ها:

Biomaterial ، Collagen ، Amino acid ، Modification ، Stabilisation ، Chemical cross-linking