title: Molecular modeling and enzymatic studies of the interaction of a choline analogue and acetylcholinesterase.
abstract: 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.
authors.affiliation: Dipartimento di Scienze Farmacobiologiche, Università degli Studi Magna Graecia di Catanzaro, Complesso Ninì Barbieri, Roccelletta di Borgia, Italy.
authors.forename: Stefano
authors.initials: S
authors.lastname: Alcaro
authors.forename: Luigi
authors.initials: L
authors.lastname: Scipione
authors.forename: Francesco
authors.initials: F
authors.lastname: Ortuso
authors.forename: Salvatore
authors.initials: S
authors.lastname: Posca
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Rispoli
authors.forename: Domenicantonio
authors.initials: D
authors.lastname: Rotiroti
mesh_terms: 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
chemical_list: D008024:Ligands; D000110:Acetylcholinesterase; D002794:Choline