Abstract

Influenza panedemic affect 25 to 30% of the world's population. Neuraminidase (NA) is the most important surfase glycoprotein of the virus causing cleavage of the sialic acid moieties and releasing of newly formed viral particles. The active site of NA is highly conserved all subtype of influaenza virus, then Neuraminidase is the target of drug designs. Using molecular dynamic (MD) and Monte Carlo simulatory methods, the NA structure and its stability different dielcteric (vacuum, water and methanol) and different tempeartures (298, 310, 315, 329 and 333K) was assessed. Measurements of potential energy (kcal/mol) of binding sites NA in different dielectrics and in different temperaturesrevealed that at time step size 0 ps, drug binding sites have maximum energy level, and at time step size 100 ps, have minimum energy level and maximum stability.

Key words: Neuraminidase, influenza, molecular dynamic, binding sit, free energy, dielectric