Structure-based design of a fluorimetric redox active peptide probe
Structure-based design of a fluorimetric redox active peptide probe
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DOI：
10.1016/j.ab.2003.10.014
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发表时间：
2004-02-01
影响因子：
2.9
通讯作者：
Schneider, JP
中科院分区：
文献类型：
--
作者：
Cline, DJ;Thorpe, C;Schneider, JP
基于结构的迭代设计被用来制备一个含二硫键的九肽作为化学和生化二硫键形成和断裂反应的荧光探针。该肽完全由天然氨基酸组成，并且在其氧化和还原状态之间表现出显著的荧光变化（42%）。该探针易于合成，水溶性好，在还原剂三羧乙基膦的作用下表现出良好的还原动力学。还原肽是一个很好的底物的酶quiescin-巯基氧化酶，并可能发现其他二硫键氧化还原酶的特性的实用程序。(C)2003年爱思唯尔公司All rights reserved.
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.