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Structure‐Activity Studies Reveal Scope for Optimisation of Ebselen‐Type Inhibition of SARS‐CoV‐2 Main Protease
Author(s) -
ThunHohenstein Siegfried T. D.,
Suits Timothy F.,
Malla Tika R.,
Tumber Anthony,
Brewitz Lennart,
Choudhry Hani,
Salah Eidarus,
Schofield Christopher J.
Publication year - 2022
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.202100582
Subject(s) - ebselen , protease , chemistry , covid-19 , derivative (finance) , coronavirus , scope (computer science) , biochemistry , combinatorial chemistry , enzyme , medicine , disease , computer science , business , glutathione , glutathione peroxidase , infectious disease (medical specialty) , programming language , finance
The reactive organoselenium compound ebselen is being investigated for treatment of coronavirus disease 2019 (COVID‐19) and other diseases. We report structure‐activity studies on sulfur analogues of ebselen with the Severe Acute Respiratory Syndrome coronavirus 2 (SARS‐CoV‐2) main protease (M pro ), employing turnover and protein‐observed mass spectrometry‐based assays. The results reveal scope for optimisation of ebselen/ebselen derivative‐ mediated inhibition of M pro , particularly with respect to improved selectivity.