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SAR QSAR Environ Res ; 32(1): 51-70, 2021 Jan.
Article in English | MEDLINE | ID: mdl-33401979

ABSTRACT

A Förster resonance energy transfer (FRET)-based assay was used to screen the FDA-approved compound library against the MERS-CoV helicase, an essential enzyme for virus replication within the host cell. Five compounds inhibited the helicase activity with submicromolar potencies (IC50, 0.73-1.65 µM) and ten compounds inhibited the enzyme with micromolar potencies (IC50, 19.6-502 µM). The molecular operating environment (MOE) was used to dock the identified inhibitors on the MERS-CoV helicase nucleotide binding. Strong inhibitors docked well in the nucleotide-binding site and established interactions with some of the essential residues. There was a reasonable correlation between the observed IC50 values and the MOE docking scores of the strong inhibitors (r 2 = 0.74), indicating the ability of the in silico docking model to predict the binding of strong inhibitors. In silico docking could be a useful complementary tool used with the FRET-based assay to predict new MERS-CoV helicase inhibitors. The identified inhibitors could potentially be used in the clinical development of new antiviral treatment for MERS-CoV and other coronavirus related diseases, including coronavirus disease 2019 (COVID-19).


Subject(s)
Antiviral Agents/chemistry , Antiviral Agents/therapeutic use , COVID-19 Drug Treatment , Coronavirus Infections/drug therapy , DNA Helicases/drug effects , Enzyme Inhibitors/pharmacokinetics , Middle East Respiratory Syndrome Coronavirus/drug effects , Humans , Quantitative Structure-Activity Relationship , SARS-CoV-2/drug effects , Virus Replication/drug effects
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