Metal-assisted stabilization and probing of collagenous triple helices

被引：63

作者：

Koide, T ^{[1
]}

Yuguchi, M ^{[1
]}

Kawakita, M ^{[1
]}

Konno, H ^{[1
]}

机构：

[1] Univ Tokushima, Fac Engn, Dept Biol Sci & Technol, Tokushima 7708506, Japan

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2002年 / 124卷 / 32期

关键词：

D O I：

10.1021/ja026182+

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Collagen model peptides that contain 2,2′-bipyridyl (bpy) ligands were designed and synthesized. The thermal stability of the collagenous triple helix was increased by forming an FeII(bpy-peptide)3 complex. The chirality of the metal center was shifted to form right-handed Δ-isomers induced by the supercoiling of the peptide moiety. Moreover, the refolding rate of the triple helix was increased in the presence of Fe(II). This metal-coordinating system possesses potential to be used to stabilize the triple-helical conformation as well as to probe the folding status of collagen model peptides. Copyright © 2002 American Chemical Society.

引用

页码：9388 / 9389

页数：2

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