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

Guo-Bo Li, Jürgen Brem, Martine I Abboud, Christopher T Lohans, Ian J Clifton, Juan-Carlos Jiménez-Castellanos, Matthew B Avison, James Spencer, Michael A McDonough, Christopher J Schofield

Research output: Contribution to journalArticle (Academic Journal)

17 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)5806-5809
Number of pages4
JournalChemical Communications
Volume53
Issue number43
DOIs
Publication statusPublished - 30 May 2017

Keywords

  • Journal Article

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    Li, G-B., Brem, J., Abboud, M. I., Lohans, C. T., Clifton, I. J., Jiménez-Castellanos, J-C., Avison, M. B., Spencer, J., McDonough, M. A., & Schofield, C. J. (2017). Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-β-lactamase inhibition. Chemical Communications, 53(43), 5806-5809. https://doi.org/10.1039/c7cc02394d