| Literature DB >> 33054210 |
Robert L Hoffman1, Robert S Kania1, Mary A Brothers1, Jay F Davies1, Rose A Ferre1, Ketan S Gajiwala1, Mingying He1, Robert J Hogan2, Kirk Kozminski1, Lilian Y Li1, Jonathan W Lockner1, Jihong Lou1, Michelle T Marra1, Lennert J Mitchell1, Brion W Murray1, James A Nieman1, Stephen Noell1, Simon P Planken1, Thomas Rowe2, Kevin Ryan1, George J Smith1, James E Solowiej1, Claire M Steppan1, Barbara Taggart2.
Abstract
The novel coronavirus disease COVID-19 that emerged in 2019 is caused by the virus SARS CoV-2 and named for its close genetic similarity to SARS CoV-1 that caused severe acute respiratory syndrome (SARS) in 2002. Both SARS coronavirus genomes encode two overlapping large polyproteins, which are cleaved at specific sites by a 3C-like cysteine protease (3CLpro) in a post-translational processing step that is critical for coronavirus replication. The 3CLpro sequences for CoV-1 and CoV-2 viruses are 100% identical in the catalytic domain that carries out protein cleavage. A research effort that focused on the discovery of reversible and irreversible ketone-based inhibitors of SARS CoV-1 3CLpro employing ligand-protease structures solved by X-ray crystallography led to the identification of 3 and 4. Preclinical experiments reveal 4 (PF-00835231) as a potent inhibitor of CoV-2 3CLpro with suitable pharmaceutical properties to warrant further development as an intravenous treatment for COVID-19.Entities:
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Year: 2020 PMID: 33054210 PMCID: PMC7571312 DOI: 10.1021/acs.jmedchem.0c01063
Source DB: PubMed Journal: J Med Chem ISSN: 0022-2623 Impact factor: 7.446