Investigation of pH-Dependent Collagen Triple-Helix Formation

被引：24

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

页码：8429 / 8432

页数：4

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