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In this study, molecular docking was performed on the 2009 H1N1 complexed with the well-known
drug, oseltamivir (OTV), andrographolide and derivatives (AGD) from Andrographis paniculata, to investigate
the binding affinity of the inhibitors toward wide type and mutant types at the position of H274Y and R292K
of neuraminidase (NA). The results of OTV revealed that the efficiency of binding is OTV-WT ~ OTV-H274Y
> OTV-R292K in which agree well with IC50 values from experimental data. The calculation revealed that AGD1 and AGD5 are good opportunity for developing as NA inhibitor for WT and H274Y. While AGD2 is a good opportunity for developing as NA inhibitor especially for R292K mutant that has more resistant fold when compare to wide type and H274Y. This is due to the AGD2 binds to NA active site in which the binding energies were -7.95,-8.09 and -7.74 kcal/mol for WT, H274Y and R292K, respectively.