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1- Department of Biophysics, Faculty of biological science, Tarbiat Modarres University, Tehran, Iran
2- Full Professor, Department of Biophysics, Faculty of biological science, Tarbiat Modarres University, Tehran, Iran , parviz@modares.ac.ir
Abstract:   (350 Views)
 Hepatitis C virus (HCV) NS3/4A Serine protease is an important drug target for treating patients with hepatitis C virus. However, its amino acid mutations, particularly A156G, commonly lead to the rapid emergence of drug resistance. Bosiprevir, simiprevir, and viniprevir drugs approved by the FDA show distinct resistance profiles against the HCV NS3/4A protease. In order to show the behavior of each of these drugs in the interaction with the protease in the wild type and A156G mutant, molecular dynamics simulation and binding free energy calculations were performed. MMPBSA-based binding free energy calculations showed that the binding affinity of each of the drugs in the interaction with NS3/4A protease in the wild type is significantly more than the interaction with the protease in the A156G mutant state. Free energy landscape (FEL) calculations revealed that in the presence of each of the drugs, more basins of conformations are formed. We hope that our data can provide useful insights for the design of a new effective inhibitory drug for the treatment of patients with the hepatitis C virus.
 
     
Article Type: Original Research | Subject: Bioinformatics
Received: 2023/01/18 | Accepted: 2024/02/12

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