| Title : Cation-Pi and Pi-Pi stacking interactions allow selective inhibition of butyrylcholinesterase by modified quinine and cinchonidine alkaloids - Nawaz_2011_Biochem.Biophys.Res.Commun_404_935 |
| Author(s) : Nawaz SA , Ayaz M , Brandt W , Wessjohann LA , Westermann B |
| Ref : Biochemical & Biophysical Research Communications , 404 :935 , 2011 |
|
Abstract :
Scaffold varied quaternized quinine and cinchonidine alkaloid derivatives were evaluated for their selective butyrylcholinesterase (BChE) inhibitory potential. K(i) values were between 0.4-260.5microM (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. |
| PubMedSearch : Nawaz_2011_Biochem.Biophys.Res.Commun_404_935 |
| PubMedID: 21185266 |
| Inhibitor | Cinchonidine Cinchonine |
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 Communications
404 :935
Nawaz SA, Ayaz M, Brandt W, Wessjohann LA, Westermann B (2011)
Biochemical & Biophysical Research Communications
404 :935