Ebselen as a potent covalent inhibitor of New Delhi metallo-β-lactamase (NDM-1)

Jia-chi Chiou; Shengbiao Wan; Kin Fai Chan; Pui Kin So; Dandan He; Edward Wai Chi Chan; Tak Hang Chan; Kwok Yin Wong; Jiang Tao; Sheng Chen

doi:10.1039/c5cc02594j

Ebselen as a potent covalent inhibitor of New Delhi metallo-β-lactamase (NDM-1)

Jia-chi Chiou, Shengbiao Wan, Kin Fai Chan, Pui Kin So, Dandan He, Edward Wai Chi Chan, Tak Hang Chan, Kwok Yin Wong, Jiang Tao, Sheng Chen

Research output: Journal article publication › Journal article › Academic research › peer-review

110 Citations (Scopus)

Abstract

We report the discovery of a promising NDM-1 inhibitor, ebselen, through a cell-based screening approach. Enzymatic kinetic study and ESI-MS analysis suggested that ebselen could bind to NDM-1 by forming a S-Se bond with the Cys221residue at the active site, thereby exhibiting a new inhibition mechanism with broad spectrum inhibitory potential.

Original language	English
Pages (from-to)	9543-9546
Number of pages	4
Journal	Chemical Communications
Volume	51
Issue number	46
DOIs	https://doi.org/10.1039/c5cc02594j
Publication status	Published - 11 Jun 2015

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Chemistry(all)
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/c5cc02594j

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abstract = "We report the discovery of a promising NDM-1 inhibitor, ebselen, through a cell-based screening approach. Enzymatic kinetic study and ESI-MS analysis suggested that ebselen could bind to NDM-1 by forming a S-Se bond with the Cys221residue at the active site, thereby exhibiting a new inhibition mechanism with broad spectrum inhibitory potential.",

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AU - Chiou, Jia-chi

AU - Wan, Shengbiao

AU - Chan, Kin Fai

AU - So, Pui Kin

AU - He, Dandan

AU - Chan, Edward Wai Chi

AU - Chan, Tak Hang

AU - Wong, Kwok Yin

AU - Tao, Jiang

AU - Chen, Sheng

PY - 2015/6/11

Y1 - 2015/6/11

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AB - We report the discovery of a promising NDM-1 inhibitor, ebselen, through a cell-based screening approach. Enzymatic kinetic study and ESI-MS analysis suggested that ebselen could bind to NDM-1 by forming a S-Se bond with the Cys221residue at the active site, thereby exhibiting a new inhibition mechanism with broad spectrum inhibitory potential.

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U2 - 10.1039/c5cc02594j

DO - 10.1039/c5cc02594j

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JO - Chemical Communications

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Ebselen as a potent covalent inhibitor of New Delhi metallo-β-lactamase (NDM-1)

Abstract

ASJC Scopus subject areas

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