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

ABSTRACT: Crystallographic analyses of the VIM-5 metallo-?-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

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

Li Guo-Bo GB   Brem Jürgen J   Lesniak Robert R   Abboud Martine I MI   Lohans Christopher T CT   Clifton Ian J IJ   Yang Sheng-Yong SY   Jiménez-Castellanos Juan-Carlos JC   Avison Matthew B MB   Spencer James J   McDonough Michael A MA   Schofield Christopher J CJ  

Chemical communications (Cambridge, England) 20170501 43

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. ...[more]

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