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

DOI: 10.1039/C7CC02394D DOI Help

Authors: Guo-bo Li (University of Oxford; Sichuan University) , Jurgen Brem (University of Oxford) , Robert Lesniak (University of Oxford) , Martine I. Abboud (University of Oxford) , Christopher T. Lohans (University of Oxford) , Ian J. Clifton (University of Oxford) , Sheng-yong Yang (Sichuan University) , Juan-carlos Jiménez-castellanos (University of Bristol) , Matthew B. Avison (University of Bristol) , James Spencer (University of Bristol) , Michael A. Mcdonough (University of Oxford) , Christopher J. Schofield (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Chem. Commun. , VOL 54

State: Published (Approved)
Published: April 2017
Diamond Proposal Number(s): 12346

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.

Subject Areas: Chemistry, Biology and Bio-materials, Medicine


Instruments: I04-Macromolecular Crystallography