Please use this identifier to cite or link to this item: http://repo.lib.jfn.ac.lk/ujrr/handle/123456789/11209
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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.authorOwen, C.D.-
dc.contributor.authorLukacik, P.-
dc.contributor.authorHenry Chan, H.T.-
dc.contributor.authorPratheesh, M.-
dc.contributor.authorSalah, E.-
dc.contributor.authorDuarte, F.-
dc.contributor.authorYang, H.-
dc.contributor.authorRao, Z.-
dc.contributor.authorWalsh, M.A.-
dc.contributor.authorSchofield, C.J.-
dc.date.accessioned2025-04-21T03:27:58Z-
dc.date.available2025-04-21T03:27:58Z-
dc.date.issued2021-
dc.identifier.urihttp://repo.lib.jfn.ac.lk/ujrr/handle/123456789/11209-
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.language.isoenen_US
dc.publisherRoyal society of Chemistryen_US
dc.titleMass spectrometry reveals potential of b-lactams as SARS-CoV-2 Mpro inhibitorsen_US
dc.typeArticleen_US
Appears in Collections:Pharmacy

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