Structure: Crystallological studies have revealed that HCV drugs can help treat COVID-19

November 17, 2020 // -- A recent experiment led by researchers at the U.S. Department of Energy's Oak Ridge National Laboratory has determined that several hepatitis C drugs can inhibit the main protease of SARS-CoV-2, which is critical to the toxic reproduction of new coronary diseases.
inhibit or block the function of this protease is essential to stop the spread of the virus in PATIENT-19 patients.
study, published in the journal Structure, is part of an effort to rapidly develop COVID-19 drugs by reusing existing drugs known to be effective in treating other viral diseases.
, there are no FDA-approved inhibitors for SARS-CoV-2's main proteases," said lead author Daniel Kneller of the U.S. Department of Energy (Photo Source: www.pixabay.com).
we found that hepatitis C drugs bind to and inhibit coronavirus proteases.
this is an important first step in determining whether these drugs should be considered potential candidates for the treatment of COVID-19.
" SARS-CoV-2 coronavirus is transmitted through the expression of polyprotein long chains that must be cut by the primary protease to become a functional protein, making it an important drug target for researchers and drug developers.
In this study, the team looked at several potential drug molecules for drug recombinant use, including the natural protease inhibitor leptide and three FDA-approved hepatitis C protease inhibitors: telaprevir, narlaprevir, and boceprevir.
the team performed room temperature X-ray measurements to create a three-dimensional map that revealed how atoms are arranged and where chemical bonds form between proteases and drug inhibitor molecules.
the ability of certain hepatitis C drugs to bind to and inhibit the main proteases of SARS-CoV-2, in particular bossprevir and narlaprevir, has achieved encouraging results.
Leupeptin showed low binding affinity.
To better understand the degree or tightness of the binding of inhibitors to proteases, they used in-body enzyme dynamics, a technique that allows researchers to study proteases and inhibitors in test tubes to measure the binding affinity or compatible between inhibitors and proteases.
binding affinity, the more effective inhibitors are in preventing proteases from working.
the study also revealed the specific behavior of proteases based on their ability to change or adapt their shape to the size and structure of the inhibitor molecules they bind to.
protease in the drug molecule will adhere to the pocket height can be extended or flexible, and can be based on the size of the drug molecule to a certain extent.
the paper was published, researchers had publicly provided their data to provide information and help to the scientific and medical community.
more research, including clinical trials, is needed to verify the drug's effectiveness and safety as a COVID-19 treatment.
, author of the study, said: "Research has shown that hepatitis C inhibitors are worth considering as potential candidates.
immediately release our data so that the scientific community can begin to study the interaction between these inhibitors and proteases.
Don't know what a drug does at the molecular level, we can't design a drug, and the data we provide is the information that developers need to design stronger, tighter drugs for more effective treatment."
"() Source: X-ray study explores potential for hepatitis C drugs to treat COVID-19 Original source: Daniel W. Kneller et al, Malleability of the SARS-CoV-2 3CL Mpro Active-Site Cavity Assists Of Clinical of Antivirals, Structure (2020). DOI: 10.1016/j.str.2020.10.007