Paper Report for: Nawaz_2011_Biochem.Biophys.Res.Commun_404_935
Reference
Title: Cation-Pi and Pi-Pi stacking interactions allow selective inhibition of butyrylcholinesterase by modified quinine and cinchonidine alkaloids Nawaz SA, Ayaz M, Brandt W, Wessjohann LA, Westermann B Ref: Biochemical & Biophysical Research Communications, 404:935, 2011 : PubMed
Scaffold varied quaternized quinine and cinchonidine alkaloid derivatives were evaluated for their selective butyrylcholinesterase (BChE) inhibitory potential. K(i) values were between 0.4-260.5microM (non-competitive inhibition) while corresponding K(i)values to acetylcholinesterase (AChE) ranged from 7.0-400microM 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 Pi-Pi stacking and Pi-cation interactions with the choline binding site and the peripheral anionic site of BChE's active site.
Nawaz SA, Ayaz M, Brandt W, Wessjohann LA, Westermann B (2011) Cation-Pi and Pi-Pi stacking interactions allow selective inhibition of butyrylcholinesterase by modified quinine and cinchonidine alkaloids Biochemical & Biophysical Research Communications404: 935-40
Nawaz SA, Ayaz M, Brandt W, Wessjohann LA, Westermann B (2011) Biochemical & Biophysical Research Communications404: 935-40
