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Issue 43, 2017
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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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Article information


Submitted
28 Mar 2017
Accepted
25 Apr 2017
First published
25 Apr 2017

Chem. Commun., 2017,53, 5806-5809
Article type
Communication

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, 53, 5806
DOI: 10.1039/C7CC02394D

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