Paper Title
Evolutionary Invariant Drug Targets: Insilico Approach for The Identification of Potential Drug Target Sites in Hepatitis C Virus (HCV) Proteins Ns3/4a, Ns5a and Ns5b

Abstract
Hepatitis C virus (HCV) shows a high degree of genetic variability, rapid evolution and adaption which results in the creation of drug resistant mutants. The unceasing and increasing advent of multi-drug resistant requires the identification of potential drug targets sites. Targeting conserved regions of viral proteins has been considered as an effective method to develop drugs therapies that may circumvent the wide genetic variability of HCV. The worldwide relationships between protein drug targets in HCV NS3/4A, NS5A and NS5B remains uncharacterized. Our study presented comprehensive mapping of functional conservation in HCV proteins (NS3/4A, NS5A, NS5B) sequences and strengthened the idea that these evolutionary conserved regions within the viral proteins can be used as potential targets for HCV drug design. We attempted to address the usage of computer-based approaches to predict conserved therapeutic targets and assess the likely success of future HCV treatment against various genotype. Overall, the results revealed that NS3/4A and NS5B proteins possess more conserved hydrophobic drug targets compared to NS5A. The targets identified were further validated by docking studies and analysis. The information derived from this study provides a basis to develop promising universal antiviral targets against HCV which are less likely to become resistant. We hope this perception of considering conserved regions as drug targets will address some of the resistance associated issues surrounding our current information of the complexities of HCV therapeutic action. Keywords- Hepatitis C virus, Intrinsic disorder regions, Drug targets, Drug binding sites