Abstract
Scaffold varied quaternized quinine and cinchonidine alkaloid derivatives were evaluated for their selective butyrylcholinesterase (BChE) inhibitory potential. K i values were between 0.4–260.5 μM (non-competitive inhibition) while corresponding K ivalues to acetylcholinesterase (AChE) ranged from 7.0–400 μM exhibiting a 250-fold selectivity for BChE. Docking arrangements (GOLD, PLANT) revealed that the extended aromatic moieties and the quaternized nitrogen of the inhibitors were responsible for specific π– π stacking and π–cation interactions with the choline binding site and the peripheral anionic site of BChE’s active site.
Published Version
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