Issue 10, 2007
From the journal:

Organic & Biomolecular Chemistry

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

Daniel J. Cline,a   Shannon L. Holta  and  Scott F. Singleton*a  

* Corresponding authors

a School of Pharmacy, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA
E-mail: sfs@email.unc.edu
Fax: +1 919-966-0204
Tel: +1 919-966-7954

Abstract

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 µM.

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

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Article information

DOI
https://doi.org/10.1039/B703159A
Article type
Communication
Submitted
01 Mar 2007
Accepted
10 Apr 2007
First published
18 Apr 2007

Org. Biomol. Chem., 2007,5, 1525-1528

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

D. J. Cline, S. L. Holt and S. F. Singleton, Org. Biomol. Chem., 2007, 5, 1525 DOI: 10.1039/B703159A

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