Inhibition of Escherichia coli RecA by rationally redesigned N-terminal helix

被引：21

作者：

Cline, Daniel J. ^{[1
]}

Holt, Shannon L. ^{[1
]}

Singleton, Scott F. ^{[1
]}

机构：

[1] Univ N Carolina, Sch Pharm, Chapel Hill, NC 27599 USA

来源：

ORGANIC & BIOMOLECULAR CHEMISTRY | 2007年 / 5卷 / 10期

关键词：

D O I：

10.1039/b703159a

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

Bacterial RecA promotes the development and transmission of antibiotic resistance genes by self-assembling into an ATP-hydrolyzing filamentous homopolymer on single-stranded DNA. We report the design of a 29mer peptide based on the RecA N-terminal domain involved in intermonomer contact that inhibits RecA filament assembly with an IC50 of 3 mu M.

引用

页码：1525 / 1528

页数：4

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