Jenkins Cara L, Raines Ronald T
Department of Chemistry, University of Wisconsin-Madison, 53706, USA.
Nat Prod Rep. 2002 Feb;19(1):49-59. doi: 10.1039/a903001h.
This review describes work on the conformational stability of the collagen triple helix. In 1994, the structure of collagen was determined at high resolution. Since then, much work has been done on synthetic mimics of collagen that contain host-guest peptides, tethers, peptoid residues, or analogs of the prevalent 4(R)-hydroxy-L-proline residues. This work has revealed much about the chemical basis for collagen stability, and could spawn useful new biomaterials. The literature from 1994 to mid 2001 is reviewed, and 116 references are cited.
本综述描述了关于胶原蛋白三螺旋构象稳定性的研究工作。1994年，胶原蛋白的结构被高分辨率测定。从那时起，人们对包含主客体肽、连接链、类肽残基或普遍存在的4(R)-羟基-L-脯氨酸残基类似物的胶原蛋白合成模拟物开展了大量研究工作。这些研究揭示了许多关于胶原蛋白稳定性的化学基础，并且可能催生出有用的新型生物材料。本文对1994年至2001年年中的文献进行了综述，并引用了116篇参考文献。
