Structure-based design of a fluorimetric redox active peptide probe

被引：16

作者：

Cline, DJ ^{[1
]}

Thorpe, C ^{[1
]}

Schneider, JP ^{[1
]}

机构：

[1] Univ Delaware, Dept Chem & Biochem, Newark, DE 19716 USA

来源：

ANALYTICAL BIOCHEMISTRY | 2004年 / 325卷 / 01期

关键词：

D O I：

10.1016/j.ab.2003.10.014

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Structure-based iterative design was used to prepare a disulfide-containing nonapeptide as a fluorimetric probe for chemical and biochemical disulfide forming and breaking reactions. The peptide is composed entirely of natural amino acids and exhibits a marked (42%) change in fluorescence between its oxidized and its reduced states. The probe is easily synthesized and highly water soluble and exhibits well-behaved kinetics on reduction with the reductant tris-carboxyethylphosphine. The reduced peptide is an excellent substrate of the enzyme quiescin-sulfhydryl oxidase and may find utility in the characterization of other disulfide oxidoreductases. (C) 2003 Elsevier Inc. All rights reserved.

引用

页码：144 / 150

页数：7

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