In a new study, researchers found that several hepatitis C drugs can inhibit the COVID-19 virus main protease, a crucial protein enzyme that enables the novel coronavirus to reproduce.
Inhibiting, or blocking, this protease from functioning is vital to stopping the virus from spreading in patients with COVID-19.
The study is part of efforts to quickly develop treatments for COVID-19 by repurposing existing drugs known to effectively treat other diseases.
The research was done by a team at the Department of Energy’s Oak Ridge National Laboratory.
The SARS-CoV-2 coronavirus spreads by expressing long chains of polyproteins that must be cut by the main protease to become functional proteins, making the protease an important drug target for researchers and drug developers.
In the study, the team looked at several well-known drugs for potential repurposing efforts including leupeptin, a naturally occurring protease inhibitor, and three FDA-approved hepatitis C protease inhibitors: telaprevir, narlaprevir and boceprevir.
The team performed room temperature X-ray measurements to build a three-dimensional map that revealed how the atoms were arranged and where chemical bonds formed between the protease and the drug inhibitor molecules.
The experiments showed promising results for certain hepatitis C drugs in their ability to bind and inhibit the SARS-CoV-2 main protease—particularly boceprevir and narlaprevir.
To better understand how well or how tightly the inhibitors bind to the protease, the team examined the protease and the inhibitor in a test tube to measure the inhibitor’s binding affinity, or compatibility, with the protease.
The higher the binding affinity, the more effective the inhibitor is at blocking the protease from functioning.
The research suggests that hepatitis C inhibitors are worth thinking about as potential repurposing drugs for COVID-19.
More research, including clinical trials, is necessary to validate the drugs’ efficacy and safety as a COVID-19 treatment.
One author of the study is Daniel Kneller.
The study is published in the journal Structure.
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