Probing the SARS-CoV-2 main protease active site as a target to inhibit viral replication

Journal Article · Fri Feb 26 04:00:00 EST 2021 · Research Features

DOI:https://doi.org/10.26904/rf-134-6265· OSTI ID:1770639

Kneller, Daniel ^[1]; Coates, Leighton ^[1]; Kovalevskyi, Andrii Y. ^[1]

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1. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)

SARS-CoV-2 replication involves the synthesis of two large proteins, which are inactive and harmless until the viral main protease enzyme (3CL M^pro) uses them as substrates, cleaving them into many smaller, functional products. Dr Andrey Kovalevsky and his team from Oak Ridge National Laboratory propose a design of novel inhibitors and the repurposing of clinical drugs developed to treat other diseases for the treatment of COVID-19. Finally, the team uses room temperature crystallography with X-rays and neutrons to guide structure-based and computer-assisted drug design and to assess the ability of drugs to inhibit the SARS-CoV-2 main protease, causing virus replication to stop.

• Research Organization: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). High Flux Isotope Reactor (HFIR) and Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). High Flux Isotope Reactor (HFIR)
• Sponsoring Organization: USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)
• DOE Contract Number: AC05-00OR22725
• OSTI ID: 1770639
• Journal Information: Research Features, Journal Name: Research Features Journal Issue: 134 Vol. 2021; ISSN 2399-1542
• Publisher: Research Features
• Country of Publication: United States
• Language: English