Site-specific modification of alpha-helical peptides with electron donors and acceptors

被引：14

作者：

Dahiyat, BI

Meade, TJ

Mayo, SL

机构：

[1] CALTECH, DIV BIOL, PASADENA, CA 91125 USA

[2] CALTECH, BECKMAN INST, PASADENA, CA 91125 USA

[3] CALTECH, DIV CHEM & CHEM ENGN, PASADENA, CA 91125 USA

[4] CALTECH, HOWARD HUGHES MED INST, PASADENA, CA 91125 USA

[5] CALTECH, DIV BIOL, PASADENA, CA 91125 USA

来源：

INORGANICA CHIMICA ACTA | 1996年 / 243卷 / 1-2期

基金：

美国国家卫生研究院;

关键词：

electron transfer; alpha-helical peptides complexes; ruthenium complexes;

D O I：

10.1016/0020-1693(95)04909-6

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

We have prepared a histidine containing monomeric alpha-helical peptide, ETH6 (A(2)KA(4)KA(2)HA(6)HA(4)KA(4)K) in order to study long-range electron transfer (ET). This peptide was site-specifically labeled with a ruthenium (donor) at one histidine and a second ruthenium (acceptor) at a second histidine located on the same peptide. Both the unlabeled peptide and the singly labeled peptide-metal complex, Ru(bpy)(2)(im)(His)-ETH6, were shown to form stable monomeric alpha-helical structures as determined by circular dichroism. Ru(NH3)(4)(py) was coupled to Ru(bpy)(2)(im)(His)-ETH6, forming a Ru(bpy)(2)(im)(His)-ETH6-(His)Ru(NH3)(4)(py) donor-acceptor complex. The synthesis and characterization of these peptides provide an entry into a series of molecules that are ideally suited to evaluate pathway differences such as H-bond mediated versus backbone-coupled long-range ET in protein alpha-helices.

引用

页码：207 / 212

页数：6

共 37 条

[1] CHARGED HISTIDINE AFFECTS ALPHA-HELIX STABILITY AT ALL POSITIONS IN THE HELIX BY INTERACTING WITH THE BACKBONE CHARGES [J].