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

被引：13

作者：

Grifagni, Deborah ^{[1
]}

Calderone, Vito ^{[1
,2
,3
]}

Giuntini, Stefano ^{[1
]}

Cantini, Francesca ^{[1
,2
,3
]}

Fragai, Marco ^{[1
,2
,3
]}

Banci, Lucia ^{[1
,2
,3
]}

机构：

[1] Univ Florence, Magnet Resonance Ctr CERM, Via Sacconi 6, I-50019 Sesto Fiorentino, Italy

[2] Univ Florence, Dept Chem Ugo Schiff, Via Lastruccia 3, I-50019 Sesto Fiorentino, Italy

[3] Consorzio Interuniv Risonanze Magnet Met Prot CIR, Via Sacconi 6, I-50019 Sesto Fiorentino, Italy

来源：

CHEMICAL COMMUNICATIONS | 2021年 / 57卷 / 64期

基金：

欧盟地平线“2020”;

关键词：

PROTEASE; SINGLE;

D O I：

10.1039/d1cc02956h

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

页码：7910 / 7913

页数：4

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