%0 Journal Article %A J. Tengrang and T. Rungrotmongkol and S. Hannongbua %D 2012 %J International Journal of Biotechnology and Bioengineering %B World Academy of Science, Engineering and Technology %I Open Science Index 66, 2012 %T Source of Oseltamivir Resistance Due to R152K Mutation of Influenza B Virus Neuraminidase: Molecular Modeling %U https://publications.waset.org/pdf/5452 %V 66 %X Every 2-3 years the influenza B virus serves epidemics. Neuraminidase (NA) is an important target for influenza drug design. Although, oseltamivir, an oral neuraminidase drug, has been shown good inhibitory efficiency against wild-type of influenza B virus, the lower susceptibility to the R152K mutation has been reported. Better understanding of oseltamivir efficiency and resistance toward the influenza B NA wild-type and R152K mutant, respectively, could be useful for rational drug design. Here, two complex systems of wild-type and R152K NAs with oseltamivir bound were studied using molecular dynamics (MD) simulations. Based on 5-ns MD simulation, the loss of notable hydrogen bond and decrease in per-residue decomposition energy from the mutated residue K152 contributed to drug compared to those of R152 in wildtype were found to be a primary source of high-level of oseltamivir resistance due to the R152K mutation. %P 326 - 329