Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-β-lactamase inhibition.

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.

SUBMITTER: Li GB 

PROVIDER: S-EPMC5516270 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature