A MOLECULAR DOCKING APPROACH TO STUDY BINDING MOLECULAR INTERACTIONS BETWEEN HERBAL COMPOUND BALANITIN-6 AND PLASMODIUM VIVEX DIHYDROFOLATE REDUCTASE

Abstract

In this paper, herbal compound Balanitin-6 a diosgenyl saponin, found in the bark and seed of Balanites aegyptiaca has been investigated as potential inhibitor of Plasmodium vivex didydrofolate reductase (PvDHFR) activity. Molecular interaction analysis using Ligplot, Chimera, and PyMol of Balanitin-6/PvDHFR complex have revealed three hydrogen bonds with active site residues Ser58, Ser120, Arg131 and ten hydrophobic interactions in Site1 hydrophilic domin. The minimum binding energy was found to be -21.31Kcal/Mol and the inhibition constant (Ki) value of 237.79 aM which is 10¹² times higher than other Food Drug Administration (FDA) approved drugs. The possible molecular interactions in close proximity to FDA approved drugs have been acknowledged and due to close proximity of Site1 active residues, where it forms part of the substrate-binding cleft, it is likely that displacement of Site1 region will interfere with substrate binding. Hence, Balanitin 6 targeted to Site1 might have sufficient profound effect to inhibit malarial protein PvDHFR activity.