Issue 64, 2021

SARS-CoV-2 Mpro inhibition by a zinc ion: structural features and hints for drug design

Abstract

Structural data on the SARS-CoV-2 main protease in complex with a zinc-containing organic inhibitor are already present in the literature and gave hints on the presence of a zinc binding site involving the catalytically relevant cysteine and histidine residues. In this paper, the structural basis of ionic zinc binding to the SARS-CoV-2 main protease has been elucidated by X-ray crystallography. The zinc binding affinity and its ability to inhibit the SARS-CoV-2 main protease have been investigated. These findings provide solid ground for the design of potent and selective metal-conjugated inhibitors of the SARS-CoV-2 main protease.

Graphical abstract: SARS-CoV-2 Mpro inhibition by a zinc ion: structural features and hints for drug design

Supplementary files

Article information

Article type
Communication
Submitted
04 Jun 2021
Accepted
06 Jul 2021
First published
16 Jul 2021
This article is Open Access
Creative Commons BY-NC license

Chem. Commun., 2021,57, 7910-7913

SARS-CoV-2 Mpro inhibition by a zinc ion: structural features and hints for drug design

D. Grifagni, V. Calderone, S. Giuntini, F. Cantini, M. Fragai and L. Banci, Chem. Commun., 2021, 57, 7910 DOI: 10.1039/D1CC02956H

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