Scientists from the University of New Hampshire found that using an already existing drug compound in a new way, known as drug repurposing, could be successful in blocking the activity of a key enzyme of the COVID-19 virus.
The research is published in the journal Proteins: Structure, Function, and Bioinformatics and was conducted by Harish Vashisth et al.
With the end of the pandemic seemingly nowhere in sight, scientists are still very focused on finding new or alternative drugs to treat and stop the spread of COVID-19.
In the study, the team targeted a key enzyme responsible for COVID-19, called the main protease enzyme Mpro. It is essential for the virus to replicate.
They explored the inhibiting properties of a derivative of the potent chemical compound known as Thiadiazolidinones, or TDZD, which work as a potential treatment for neurological disorders like Parkinson’s Disease.
Using molecular dynamics simulations combined with laboratory experiments, the researchers determined that TDZD compound was able to inhibit the Mpro enzyme.
The team says coronaviruses, like COVID-19, are a notorious group of infectious agents that include a large class of viruses with RNA genomes, similar to the human DNA genome, that depend on well-organized protein structures crucial for viral growth and replication.
These viruses can develop rapid defenses at the cellular level by orchestrating these layers, or folding mechanisms, in viral proteins so the key is to find a way to shut them down.
RNA viruses are known for causing seasonal epidemics, like influenza, and can appear as novel virus strains with high fatality rates (COVID-19, SARS, Zika and Ebola).
Researchers say the need for an alternative drug development pipeline, instead of the intensive process of introducing new drugs to market, is illustrated by the high infection rate of COVID-19 (compared to previous coronaviruses) and is important for a long-term effective response to new and reoccurring outbreaks.
Copyright © 2022 Knowridge Science Report. All rights reserved.