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Copper(II) Inhibition of the SARS-CoV-2 Main Protease.

ABSTRACT: In an analysis of the structural stability of the coronavirus main protease (Mpro), we identified regions of the protein that could be disabled by cobalt(III)-cation binding to histidines and cysteines [1]. Here we have extended our work to include copper(II) chelates, which we have docked to HIS 41 and CYS 145 in the Mpro active-site region. We have found stable docked structures where Cu(II) could readily bond to the CYS 145 thiolate, which would be lethal to the enzyme. We also started studying the Spike Protein, PDB ID: 6VXX and the region around the D614G mutant.

SUBMITTER: Garza-Lopez RA

PROVIDER: S-EPMC7668746 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

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Copper(II) Inhibition of the SARS-CoV-2 Main Protease.

Garza-López Roberto A RA Kozak John J JJ Gray Harry B HB

ChemRxiv : the preprint server for chemistry 20200721

In an analysis of the structural stability of the coronavirus main protease (Mpro), we identified regions of the protein that could be disabled by cobalt(III)-cation binding to histidines and cysteines [1]. Here we have extended our work to include copper(II) chelates, which we have docked to HIS 41 and CYS 145 in the Mpro active-site region. We have found stable docked structures where Cu(II) could readily bond to the CYS 145 thiolate, which would be lethal to the enzyme. ...[more]

PMID: 33200118

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