1. Academic Validation
  2. Discovery and Mechanism of SARS-CoV-2 Main Protease Inhibitors

Discovery and Mechanism of SARS-CoV-2 Main Protease Inhibitors

  • J Med Chem. 2022 Feb 24;65(4):2866-2879. doi: 10.1021/acs.jmedchem.1c00566.
Sarah Huff 1 Indrasena Reddy Kummetha 1 Shashi Kant Tiwari 1 Matthew B Huante 2 Alex E Clark 3 Shaobo Wang 1 William Bray 1 Davey Smith 3 Aaron F Carlin 3 Mark Endsley 2 Tariq M Rana 1 3
Affiliations

Affiliations

  • 1 Division of Genetics, Department of Pediatrics, Center for Drug Discovery Innovation, Program in Immunology, Institute for Genomic Medicine, 9500 Gilman Drive MC 0762, La Jolla, California 92093, United States.
  • 2 Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas 77555, United States.
  • 3 Division of Infectious Diseases and Global Public Health, Department of Medicine, University of California San Diego, 9500 Gilman Drive MC 0762, La Jolla, California 92093, United States.
Abstract

The emergence of a new coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), presents an urgent public health crisis. Without available targeted therapies, treatment options remain limited for COVID-19 patients. Using medicinal chemistry and rational drug design strategies, we identify a 2-phenyl-1,2-benzoselenazol-3-one class of compounds targeting the SARS-CoV-2 main protease (Mpro). FRET-based screening against recombinant SARS-CoV-2 Mpro identified six compounds that inhibit proteolysis with nanomolar IC50 values. Preincubation dilution experiments and molecular docking determined that the inhibition of SARS-CoV-2 Mpro can occur by either covalent or noncovalent mechanisms, and lead E04 was determined to inhibit Mpro competitively. Lead E24 inhibited viral replication with a nanomolar EC50 value (844 nM) in SARS-CoV-2-infected Vero E6 cells and was further confirmed to impair SARS-CoV-2 replication in human lung epithelial cells and human-induced pluripotent stem cell-derived 3D lung organoids. Altogether, these studies provide a structural framework and mechanism of Mpro inhibition that should facilitate the design of future COVID-19 treatments.

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