Photocontrolled folding and unfolding of a collagen triple helix

被引：92
|
作者：
Kusebauch, Ulrike
Cadamuro, Sergio A.
Musiol, Hans-Juergen
Lenz, Martin O.
Wachtveitl, Josef
Moroder, Luis
Renner, Christian
机构：
[1] Max Planck Inst Biochem, D-82152 Martinsried, Germany
[2] Goethe Univ Frankfurt, Inst Phys & Theoret Chem, D-60438 Frankfurt, Germany
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2006年 / 45卷 / 42期
关键词：
collagen; folding/unfolding; peptides; photoswitches; triple helix;
D O I：
10.1002/anie.200601432
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
(Figure Presented) At the flick of a switch: Two side chains of a collagen peptide containing (2S,4S)-mercaptoproline at two defined positions are linked with a diiodo azobenzene derivative. With the trans isomer of the azobenzene clamp (orange), the peptide folds into the collagen triple helix (green, blue, gray), which unfolds upon irradiation at 330 nm. The light-controlled folding/unfolding processes are fully reversible, making this system well-suited for ultrafast spectroscopic analysis. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码：7015 / 7018
页数：4
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