Hepatitis C drugs shown to inhibit coronavirus enzyme
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Researchers looked at several well-known drug molecules for potential repurposing efforts. These included three hepatitis C protease inhibitors: telaprevir, narlaprevir and boceprevir.
- Several Hepatitis C drugs have been found to inhibit a crucial protein enzyme in the novel coronavirus SARS-CoV-2.
- Once it has entered the human cell using its spike protein, the coronavirus uses an enzyme called the main protease to replicate.
- The coronavirus expresses long chains of compounds, which must be cut by the main protease to become functional proteins.
- Inhibiting the functioning of the main protease, therefore, is vital to stopping the virus from spreading in patients with Covid-19.
- The researchers performed room-temperature X-ray measurements to build a three-dimensional map of chemical bonds formed between the protease and the drug molecules.
- The experiments yielded promising results for certain hepatitis C drugs in their ability to bind and inhibit the main protease — particularly boceprevir and narlaprevir.
- The study used a technique called in vitro enzyme kinetics. This enables researchers to study the protease and the inhibitor in a test tube to measure the inhibitor’s binding affinity with the protease.
- The higher the binding affinity, the more effective the inhibitor is at blocking the protease from functioning.
- The study also sheds light on a peculiar behaviour of the protease’s ability to change or adapt its shape according to the size and structure of the inhibitor molecule it binds to.
- Pockets within the protease where a drug molecule would attach are highly flexible, and can either open or close to an extent.