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 Cys(221) residue at the active site, thereby exhibiting a new inhibition mechanism with broad spectrum inhibitory potential.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Ampicillin / pharmacology
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Anti-Bacterial Agents / pharmacology
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Azoles / pharmacology*
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Escherichia coli / drug effects
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Isoindoles
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Meropenem
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Microbial Sensitivity Tests
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Organoselenium Compounds / pharmacology*
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Thienamycins / pharmacology
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beta-Lactamase Inhibitors / pharmacology*
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beta-Lactamases / genetics
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beta-Lactamases / metabolism*
Substances
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Anti-Bacterial Agents
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Azoles
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Isoindoles
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Organoselenium Compounds
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Thienamycins
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beta-Lactamase Inhibitors
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ebselen
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Ampicillin
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beta-Lactamases
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beta-lactamase NDM-1
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Meropenem