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Disulfiram as a potent metallo-β-lactamase inhibitor with dual functional mechanisms

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Abstract

We report a promising NDM-1 inhibitor, disulfiram, which can covalently bind to NDM-1 by forming an S–S bond with the Cys208 residue. Its copper-containing metabolite in vivo, Cu(DTC)2, also inactivated NDM-1 through oxidizing the Zn(II) thiolate site of the enzyme, therefore exhibiting dual functional inhibitory potential against B1 and B2 subclass MβLs.

Graphical abstract: Disulfiram as a potent metallo-β-lactamase inhibitor with dual functional mechanisms

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Article information


Submitted
21 Nov 2019
Accepted
28 Jan 2020
First published
29 Jan 2020

Chem. Commun., 2020, Advance Article
Article type
Communication

Disulfiram as a potent metallo-β-lactamase inhibitor with dual functional mechanisms

C. Chen, K. Yang, L. Wu, J. Li and L. Sun, Chem. Commun., 2020, Advance Article , DOI: 10.1039/C9CC09074F

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