A molecular docking study of dehydroevodiamine as an inhibitor of epstein-barr virus protease

Abstract

Abstract Epstein-Barr Virus (EBV) is a type of γ-herpes virus which cause kissing disease. The virus induces cancer and causes latent infection. EBV protease is one of the constituent capsid proteins that play an important role in assembling virions on nucleus and spreading them. Therefore, this enzyme potentially became one of inhibition target which have impact on the termination EBV life cycle. During this time, drugs to inhibit this enzyme had not been studied. This study aimed to examine dehydroevodiamine as a potential inhibitor EBV protease by molecular docking method. The docking was done through both blind and specific docking techniques and the Ki values were calculated using docking approach when RMSD is 0 Å. Molecule visualization was done using PyMol and dehydroevodiamine profile identification was done on Ro5. The results showed that dehydroevodiamine has binding affinity of -9.8 kcal/mol and -7.3 kcal/mol; predicted Ki (STP) of 1,426729x10−8 and 1,431479x10−6 for blind and specific docking, respectively. Dehydroevodiamine profiles does not violate Ro5. These values indicated the potential of dehydroevodiamine as an oral drug candidate for kissing disease. This finding opens possibility to do further work on wet-lab-levels.