| Literature DB >> 24428639 |
Thanh Lam1, Mark T Hilgers, Mark L Cunningham, Bryan P Kwan, Kirk J Nelson, Vickie Brown-Driver, Voon Ong, Michael Trzoss, Grayson Hough, Karen Joy Shaw, John Finn.
Abstract
A new series of dihydrofolate reductase (DHFR) inhibitors, the 7-(benzimidazol-1-yl)-2,4-diaminoquinazolines, were designed and optimized for antibacterial potency and enzyme selectivity. The most potent inhibitors in this series contained a five-membered heterocycle at the 2-position of the benzimidazole, leading to highly potent and selective compounds that exploit the differences in the size of a binding pocket adjacent to the NADPH cofactor between the bacterial and human DHFR enzymes. Typical of these compounds is 7-((2-thiazol-2-yl)benzimidazol-1-yl)-2,4 diaminoquinazoline, which is a potent inhibitor of S. aureus DHFR (Ki = 0.002 nM) with 46700-fold selectivity over human DHFR. This compound also has high antibacterial potency on Gram-positive bacteria with an MIC versus wild type S. aureus of 0.0125 μg/mL and a MIC versus trimethoprim-resistant S. aureus of 0.25 μg/mL. In vivo efficacy versus a S. aureus septicemia was demonstrated, highlighting the potential of this new series.Entities:
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Year: 2014 PMID: 24428639 DOI: 10.1021/jm401204g
Source DB: PubMed Journal: J Med Chem ISSN: 0022-2623 Impact factor: 7.446