| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1355962 | Bioorganic Chemistry | 2007 | 7 Pages |
Abstract
A high-throughput screening approach was used to identify new inhibitors of the metallo-protease lethal factor from Bacillus anthracis. A library of ∼14,000 compounds was screened using a fluorescence-based in vitro assay and hits were further characterized enzymatically via measurements of IC50 and Ki values against a small panel of metallo-proteases. This study led to the identification of new scaffolds that inhibit LF and the Botulinum Neurotoxin Type A in the low micromolar range, while sparing the human metallo-proteases MMP-2 and MMP-9. Therefore, these scaffolds could be further exploited for the development of potent and selective anti-toxin agents.
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Sherida L. Johnson, Li-Hsing Chen, Maurizio Pellecchia,