Mass spectrometry reveals potential of b-lactams as SARS-CoV-2 Mpro inhibitors

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dc.contributor.authorMalla, T.R.
dc.contributor.authorTumber, A.
dc.contributor.authorJohn, T.
dc.contributor.authorBrewitz, L.
dc.contributor.authorStrain-Damerell, C.
dc.contributor.authorDavid Owen, C.
dc.contributor.authorLukacik, P.
dc.contributor.authorHenry Chan, H.T.
dc.contributor.authorPratheesh, M.
dc.contributor.authorZihe Rao
dc.contributor.authorZihe Rao, M.A.
dc.contributor.authorSchofield, C.J.
dc.date.accessioned2025-06-09T08:21:34Z
dc.date.available2025-06-09T08:21:34Z
dc.date.issued2021
dc.description.abstractThe main viral protease (Mpro) of SARS-CoV-2 is a nucleophilic cysteine hydrolase and a current target for anti-viral chemotherapy. We describe a high-throughput solid phase extraction coupled to mass spectrometry Mpro assay. The results reveal some b-lactams, including penicillin esters, are active site reacting Mpro inhibitors, thus highlighting the potential of acylating agents for Mpro inhibition.en_US
dc.identifier.issn1359-7345
dc.identifier.urihttp://repo.lib.jfn.ac.lk/ujrr/handle/123456789/11357
dc.language.isoenen_US
dc.publisherThe Royal Society of Chemistryen_US
dc.titleMass spectrometry reveals potential of b-lactams as SARS-CoV-2 Mpro inhibitorsen_US
dc.typeArticleen_US

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