AI Article Synopsis
- The study analyzed the VIM-5 metallo-β-lactamase (MBL) using crystallography to understand how it interacts with isoquinoline inhibitors, which don’t bind to zinc ions.
- Researchers compared this structure with other MBL-inhibitor complexes, leading them to add a thiol that binds zinc, which helped identify effective B1 MBL inhibitors.
- These identified inhibitors enhanced the effectiveness of meropenem (an antibiotic) against bacteria that carry MBLs in clinical settings.
Article Abstract
Crystallographic analyses of the VIM-5 metallo-β-lactamase (MBL) with isoquinoline inhibitors reveal non zinc ion binding modes. Comparison with other MBL-inhibitor structures directed addition of a zinc-binding thiol enabling identification of potent B1 MBL inhibitors. The inhibitors potentiate meropenem activity against clinical isolates harboring MBLs.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5516270 | PMC |
| http://dx.doi.org/10.1039/c7cc02394d | DOI Listing |
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