The present study elucidates molecular interactions of human acetylcholinesterase (AChE),
butyrylcholinesterase (BuChE) and 5-lipoxygenase (5-LPO) with a novel natural ligand Galangin (GAL); and also with
the well-known ligands Bisnorcymserine (BNC) and Cymserine for comparison. Docking between these ligands and
enzymes were performed using ‘Autodock4.2’. It was found that hydrophobic interactions play an important role in the
correct positioning of BNC within the ‘catalytic site’ of AChE, BuChE and 5-LPO to permit docking while hydrogen
bonds are significant in case of cymserine for the same. However, only polar interactions are significant in the correct
positioning of GAL within the ‘catalytic site’ of AChE, BuChE and 5-LPO to permit docking. Such information may aid
in the design of versatile AChE, BuChE and 5 LPO-inhibitors, and is expected to aid in safe clinical use of above ligands.
Scope still remains in the determination of the three-dimensional structure of AChE-GAL, BuChE-GAL and 5-LPO-GAL
complex by X-ray crystallography to certify the described data. Moreover, the present study confirms that GAL is a more
efficient inhibitor of human brain AChE compared to BNC and cymserine, while in case of 5-LPO and human brain
BuChE, BNC is a more efficient inhibitor compared to GAL and cymserine with reference to ΔG and Ki values.