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Mass spectrometry reveals potential of β-lactams as SARS-CoV-2 M pro inhibitors

DOI: 10.1039/D0CC06870E DOI Help

Authors: Tika R. Malla (University of Oxford) , Anthony Tumber (University of Oxford) , Tobias John (University of Oxford) , Lennart Brewitz (University of Oxford) , Claire Strain-damerell (Diamond Light Source; Research Complex at Harwell) , C. David Owen (Diamond Light Source; Research Complex at Harwell) , Petra Lukacik (Diamond Light Source; Research Complex at Harwell) , H. T. Henry Chan (University of Oxford) , Pratheesh Maheswaran (University of Oxford) , Eidarus Salah (University of Oxford) , Fernanda Duarte (University of Oxford) , Haitao Yang (ShanghaiTech University) , Zihe Rao (ShanghaiTech University) , Martin A. Walsh (Diamond Light Source; Research Complex at Harwell) , Christopher J. Schofield (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Chemical Communications , VOL 582

State: Published (Approved)
Published: January 2021

Open Access Open Access

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 β-lactams, including penicillin esters, are active site reacting Mpro inhibitors, thus highlighting the potential of acylating agents for Mpro inhibition.

Subject Areas: Biology and Bio-materials


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