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Mpro_RAGL_JJK_HBG_19July2020_ChemRxiv.pdf (3.27 MB)

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

preprint
submitted on 19.07.2020 and posted on 21.07.2020 by Roberto A. Garza-Lopez, John J. Kozak, Harry B. Gray
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.

Funding

Pomona College, Sontag Research Fellowship Award.

Pomona College, Howard Hughes Medical Institute Research Program

History

Email Address of Submitting Author

ragl4747@pomona.edu

Institution

Chemistry Department. Pomona College

Country

United States of America

ORCID For Submitting Author

0000-0002-9363-1842

Declaration of Conflict of Interest

No conflict of Interest

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