MOLECULAR DOCKING STUDY OF HEMAGGLUTININ PROTEIN OF INFLUENZA A VIRUS TO DEVELOP A NOVEL ANTI-INFLUENZA DRUG

The Hemagglutinin (HA) protein of the Influenza virus plays a vital role in viral replication. In this study, numerous small molecules were screened systematically against the HA protein to find a compound that can bind to it selectively. The HA protein’s three-dimensional crystal structure was obtained from RCSB PDB and inputted into the FTMap Web Tool to identify the best possible drug gable hotspot. Over 68 million compounds from the ZINC-15 database were filtered for drug-likeness properties and narrowed down to 250,000 ligands. These chosen molecules were then tested for their binding affinity to the selected hotspot on the HA protein using the CLC Drug Discovery Software. The top 100 molecules with the highest binding affinity were tested for ADMET properties using the admet SAR web tool. Six compounds that satisfied the given conditions were then subjected to a more intensive binding affinity test using the AutoDock Vina program of the PyRx software. The molecule with the highest binding affinity to HA, 6-(4-Methylpiperidin-1-yl) sulfonyl-1-azatricyclo [6.3.1.04, 12]dodeca-4,6,8(12)-trien-2-one, was selected as the lead molecule that could be developed further as a potential drug against the Influenza A virus.