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

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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.

Graphical abstract: Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-β-lactamase inhibition

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Publication details

The article was received on 28 Mar 2017, accepted on 25 Apr 2017 and first published on 25 Apr 2017


Article type: Communication
DOI: 10.1039/C7CC02394D
Citation: Chem. Commun., 2017, Advance Article
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    Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-β-lactamase inhibition

    G. Li, J. Brem, R. Lesniak, M. I. Abboud, C. T. Lohans, I. J. Clifton, S. Yang, J. Jiménez-Castellanos, M. B. Avison, J. Spencer, M. A. McDonough and C. J. Schofield, Chem. Commun., 2017, Advance Article , DOI: 10.1039/C7CC02394D

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