Stabilization of collagen-model, triple-helical peptides for in vitro and in vivo applications.
Stabilization of collagen-model, triple-helical peptides for in vitro and in vivo applications.
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DOI：
10.1007/978-1-62703-652-8_11
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发表时间：
2013
期刊：
影响因子：
--
通讯作者：
Fields, Gregg B
中科院分区：
文献类型：
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作者：
Bhowmick, Manishabrata;Fields, Gregg B
胶原蛋白的三螺旋结构已经在许多化学和重组模型系统中准确地再现。三螺旋肽和蛋白质已被应用于解剖胶原稳定力、分离胶原中的受体和蛋白质结合位点、胶原分解蛋白酶的机械检查以及新型生物材料的开发。将天然样序列引入三螺旋构建体可以将三螺旋的热稳定性降低至低于生理环境的热稳定性。反过来，掺入非天然氨基酸和/或模板可以增强三螺旋稳定性。我们目前描述了可以调节三螺旋结构以在生理或近生理条件下使用的方法。
The triple-helical structure of collagen has been accurately reproduced in numerous chemical and recombinant model systems. Triple-helical peptides and proteins have found application for dissecting collagen-stabilizing forces, isolating receptor- and protein-binding sites in collagen, mechanistic examination of collagenolytic proteases, and development of novel biomaterials. Introduction of native-like sequences into triple-helical constructs can reduce the thermal stability of the triple-helix to below that of the physiological environment. In turn, incorporation of nonnative amino acids and/or templates can enhance triple-helix stability. We presently describe approaches by which triple-helical structure can be modulated for use under physiological or near-physiological conditions.