4.6 Article

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

Journal

ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 5, Issue 10, Pages 1525-1528

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/b703159a

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Funding

  1. NIGMS NIH HHS [GM58114, R01 GM058114] Funding Source: Medline

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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.

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