alexa Identification of Novel Hepatitis C Virus NS3-4A Protease Inhibitors by Virtual Screening Approach
ISSN: 1948-5948

Journal of Microbial & Biochemical Technology
Open Access

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Research Article

Identification of Novel Hepatitis C Virus NS3-4A Protease Inhibitors by Virtual Screening Approach

Anish Kumar1, Rashmi Gupta1, Kanika Verma1, Kshitija Iyer2 Shanthi V1 and K Ramanathan1*

1Industrial Biotechnology Division, School of Bio Sciences and Technology, VIT University, Vellore, Tamil Nadu, India

2M.Sc Biotechnology, VIT University, Vellore, Tamil Nadu, India

*Corresponding Author:
K Ramanathan
Industrial Biotechnology Division
School of Bio Sciences and Technology
VIT University, Vellore- 632014, Tamil Nadu, India
Tel: +91 4162202545
Fax: +91 4162243092
E-mail: [email protected]

Received date: May 23, 2013; Accepted date: June 10, 2013; Published date: June 17, 2013

Citation: Kumar A, Gupta R, Verma K, Iyer K, Shanthi V, et al. (2014) Identification of Novel Hepatitis C Virus NS3-4A Protease Inhibitors by Virtual Screening Approach. J Microb Biochem Technol R1: 005. doi: 10.4172/1948-5948.R1-005

Copyright: © 2014 Kumar A, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited

 

Abstract

Hepatitis C Virus (HCV) is a leading cause of cirrhosis and liver cancer worldwide. The replication and viral polyprotein maturation of HCV crucially depends on the cleavage of the polyprotein precursor into 10 viral proteins. The NS3-4A serine protease cleaves the nonstructural region of the polyprotein at four out of five junctions, thus is a promising target for the development of antiviral inhibitors. There are many inhibitors of HCV NS3/4A protease in the clinical trial and improvement indicating significant reduction in the viral infection rate. However, most PIs develop resistance associated variants while treatment and are restricted to one or two HCV genotypes. The second generation PI, MK-5172, is the only exception, which potently inhibits most variants associated with resistance to first generation PIs and is pan-genotypic. In this study, we investigated the potent lead compound(s) based on similarity search using the most potent proved protease inhibitor, MK-5172. We have performed virtual screening techniques using PubChem database available in NCBI to identify lead like molecules. The database has yielded 32 hits for 95% similarity search and the pharmacokinetic analysis (ADME) was performed for screened compounds. This structure based drug design identified three lead compounds that can work better against NS3/4A protease.

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