ZiCo: A peptide designed to switch folded state upon binding zinc

被引：88

作者：

Cerasoli, E ^{[1
]}

Sharpe, BK ^{[1
]}

Woolfson, DN ^{[1
]}

机构：

[1] Univ Sussex, Sch Life Sci, Dept Biochem, Brighton BN1 9QG, E Sussex, England

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2005年 / 127卷 / 43期

基金：

英国医学研究理事会; 英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1021/ja0543604

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

We describe a novel approach to the design of a metal-triggered conformational switch. Specifically, two distinct protein-folding motifs were merged into one polypeptide sequence. The target structures were an α-helical coiled-coil trimer and zinc-bound monomer. Solution-phase spectroscopic, sedimentation, and binding studies confirmed the key aspects of the design. Both forms of the peptide were cooperatively folded, and the switch between them was reversible. This design process potentially presents a novel route to peptide-based biosensors. Copyright © 2005 American Chemical Society.

引用

页码：15008 / 15009

页数：2

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