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000456821 1001_ $$0P:(DE-H253)PIP1082033$$aGünther, Sebastian$$b0$$eCorresponding author
000456821 245__ $$aX-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease
000456821 260__ $$aWashington, DC$$bAssoc.$$c2021
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000456821 520__ $$aThe coronavirus disease (COVID-19) caused by SARS-CoV-2 is creating tremendous human suffering. To date, no effective drug is available to directly treat the disease. In a search for a drug against COVID-19, we have performed a high-throughput X-ray crystallographic screen of two repurposing drug libraries against the SARS-CoV-2 main protease (Mpro), which is essential for viral replication. In contrast to commonly applied X-ray fragment screening experiments with molecules of low complexity, our screen tested already approved drugs and drugs in clinical trials. From the three-dimensional protein structures, we identified 37 compounds that bind to Mpro. In subsequent cell-based viral reduction assays, one peptidomimetic and six non-peptidic compounds showed antiviral activity at non-toxic concentrations. We identified two allosteric binding sites representing attractive targets for drug development against SARS-CoV-2.
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000456821 7870_ $$0PUBDB-2022-04874$$aGünther, Sebastian et.al.$$dWashington, DC : Assoc., 2020$$iIsParent$$r$$tInhibition of SARS-CoV-2 main protease by allosteric drug-binding
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