Molecular modeling and enzymatic studies of the interaction of a choline analogue and acetylcholinesterase.
Pivaloyl-choline iodide 1 interactions with acetylcholinesterase (AChE) have been studied by theoretical and enzymatic methods. An integrated computational approach has clearly shown a substrate rather than inhibitory profile for 1. Enzymatic experiments have also supported the same theoretical conclusion indicating that AChE was able to hydrolyze 1 to choline.
Alcaro
Stefano
S
Dipartimento di Scienze Farmacobiologiche, Università degli Studi Magna Graecia di Catanzaro, Complesso Ninì Barbieri, Roccelletta di Borgia, Italy.
Scipione
Luigi
L
Ortuso
Francesco
F
Posca
Salvatore
S
Rispoli
Vincenzo
V
Rotiroti
Domenicantonio
D
D000110:Acetylcholinesterase / Q000737:chemistry*; D000595:Amino Acid Sequence; D001665:Binding Sites; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002794:Choline / Q000031:analogs & derivatives* / Q000494:pharmacology*; D006868:Hydrolysis; D007700:Kinetics; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation
D008024:Ligands; D000110:Acetylcholinesterase; D002794:Choline