化学修饰丝素蛋白的生物医学应用。
Biomedical applications of chemically-modified silk fibroin.
作者信息
Murphy Amanda R, Kaplan David L
机构信息
Department of Biomedical Engineering, 4 Colby Street, Tufts University, Medford, MA 02155. Email:
出版信息
J Mater Chem. 2009 Jun 23;19(36):6443-6450. doi: 10.1039/b905802h.
Abstract
Silk proteins belong to a class of unique, high molecular weight, block copolymer-like proteins that have found widespread use in biomaterials and regenerative medicine. The useful features of these proteins, including self-assembly, robust mechanical properties, biocompatibility and biodegradability can be enhanced through a variety of chemical modifications. These modifications provide chemical handles for the attachment of growth factors, cell binding domains and other polymers to silk, expanding the range of cell and tissue engineering applications attainable. This review focuses on the chemical reactions that have been used to modify the amino acids in silk proteins, and describes their utility in biomedical applications.
摘要
丝蛋白属于一类独特的、高分子量的、类似嵌段共聚物的蛋白质，已在生物材料和再生医学中得到广泛应用。这些蛋白质的有用特性，包括自组装、强大的机械性能、生物相容性和生物降解性，可以通过各种化学修饰得到增强。这些修饰为生长因子、细胞结合域和其他聚合物与丝的连接提供了化学手段，扩大了细胞和组织工程应用的范围。本综述重点关注用于修饰丝蛋白中氨基酸的化学反应，并描述它们在生物医学应用中的效用。
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