Inhibition of Influenza A Hemagglutinin H1N1 with Andrographolide and Derivatives

Abstract

To investigate the binding affinity of the inhibitors, molecular docking was performed on hemagglutinin H1N1 complexed with andrographolide and derivatives from Andrographis paniculata. The result revealed that the 1,4 – deoxyandrographolide_1 led to the strongest binding to hemagglutinin active site. Therefore, 1,4 – deoxyandrographolide_1 was selected to study H-bond and free energy using molecular dynamics simulation. The result showed that 1,4 - deoxy andrographolide_1 inhibitor can be bound to the key positions of HA amino acid (Y95, H183, D190, E227 and G228) with high percentage of interaction. The binding free energy result founded that this complex can be well bound together of -72.33 kcal/mol. Therefore, 1,4 – deoxyandrographolide_1 is a good choice for developing the inhibitor of hemagglutinin.