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

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dc.contributor.author Malla, T.R.
dc.contributor.author Tumber, A.
dc.contributor.author John, T.
dc.contributor.author Brewitz, L.
dc.contributor.author Strain-Damerell, C.
dc.contributor.author Owen, C.D.
dc.contributor.author Lukacik, P.
dc.contributor.author Henry Chan, H.T.
dc.contributor.author Pratheesh, M.
dc.contributor.author Salah, E.
dc.contributor.author Duarte, F.
dc.contributor.author Yang, H.
dc.contributor.author Rao, Z.
dc.contributor.author Walsh, M.A.
dc.contributor.author Schofield, C.J.
dc.date.accessioned 2025-04-21T03:27:58Z
dc.date.available 2025-04-21T03:27:58Z
dc.date.issued 2021
dc.identifier.uri http://repo.lib.jfn.ac.lk/ujrr/handle/123456789/11209
dc.description.abstract The 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.iso en en_US
dc.publisher Royal society of Chemistry en_US
dc.title Mass spectrometry reveals potential of b-lactams as SARS-CoV-2 Mpro inhibitors en_US
dc.type Article en_US


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