Quantum Chemical Investigation of C12 and C6 Position of Oseltamivir Sialidase Antiviral Inhibitor

Krishnan Chandrasekaran

doi:10.7324/japs.2015.50922

Abstract

In-silico Virtual Screening and ADMET Study to Find Novel Neuraminidase N1 Inhibitors Extended to the 150-CavityAshraf Ahmed Ali Abdalsalam

Highlights

Influenza virus is a RNA virus which contains two surface proteins namely hemaglutinnin (HA) and neuraminidase (Chak et al, 2007)
The ab initio and DFT investigation of C12 & C6 position of oseltamivir sialidase inhibitor reveals that the absence of pyranose oxygen ring in the inhibitor structure drastically increases binding affinity of the inhibitor in relation to the pyranose based inhibitors
The analysis at C6 position of oseltamivir inhibitor discloses that the methyl amine group increases the binding affinity due to their strong hydrogen bonding tendency with the vicinity receptors

Summary

Introduction

Influenza virus is a RNA virus which contains two surface proteins namely hemaglutinnin (HA) and neuraminidase (Chak et al, 2007). Hemagglutinin is the prime target of vaccines and neuraminidase is the main target of anti viral drugs. Vaccines against influenza virus are frequently inactive due to the rapid emergence of mutant viral antigens (Gerdon et al, 2005) and it creates an inevitable need of antiviral drugs. NA is an enzyme protein, the influenza virus cleaves the alpla ketosidic linkage of the neuraminidase active site (sialic acid) and the adjacent arginine amino residue of the host cell receptor (Jarreau et al, 1992) The cleavage process proliferate the viral infection to the other cells and continues its lifecycle. The first two antiviral drugs amantadine and rimantadine which block the M2 protein ion channel function will be effective in blocking

Methods

Results

Conclusion