Investigation of pH-Dependent Collagen Triple-Helix Formation

被引：23
|
作者：
Lee, Song-Gil [1 ]
Lee, Jee Yeon [1 ]
Chmielewski, Jean [1 ]
机构：
[1] Purdue Univ, Dept Chem, W Lafayette, IN 47907 USA
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2008年 / 47卷 / 44期
关键词：
circular dichroism; collagen peptides; helical structures; peptide engineering; pH switches;
D O I：
10.1002/anie.200802224
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
(Figure Presented) Helices on demand: Collagen peptides were engineered to form triple helices under environmental control. The replacement of the hydroxyproline (Hyp) residues in a collagen peptide with carboxylate-modified Hyp residues gave a petide that forms a collagen triple-helical structure at acidic pH values and low temperatures and adopts a monomeric, polyproline II helical conformation under neutral conditions (see scheme). © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码：8429 / 8432
页数：4
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