Related Experiment Video
Updated: Jun 7, 2026

High-throughput Antiviral Assays to Screen for Inhibitors of Zika Virus Replication
Published on: October 30, 2021
Analogs of NIH Molecular Probe ML283 Are Potent SARS-CoV-2 Helicase Inhibitors
David N Frick1, Robert V Bavisotto1, Nicholas C Hopper1
1Department of Chemistry & Biochemistry, The University of Wisconsin-Milwaukee, Milwaukee, Wisconsin 53217, United States.
Abstract:
The National Institutes of Health molecular probe ML283 was synthesized as a potent, selective inhibitor of the helicase encoded by the hepatitis C virus. Because modeling with AutoDock Vina predicted that ML283 might bind the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) nonstructural protein 13 (nsp13) helicase, the effects of a collection of ML283 analogs and other hepatitis C virus (HCV) helicase inhibitors on the SARS-CoV-2 helicase were analyzed. Only modest impacts on nsp13-catalyzed ATP hydrolyses were observed with some compounds, most of which were analogs of the drug ebselen, not ML283. In contrast, a new molecular-beacon-based helicase assay revealed that ML283 and many ML283 analogs are potent SARS-CoV-2 helicase inhibitors. Analog potencies correlate with the binding energies predicted by modeling, which suggests that a pocket surrounded by the carboxy-terminal nsp13 RecA-like helicase motor domain might be exploitable for antiviral drug development.
Related Concept Videos
DNA Helicases
Inhibitors of Bacterial DNA Synthesis
Inhibitors of Viral Protein Synthesis
Inhibitors Of Virion Release
Antiviral Nucleoside Inhibitors

