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.
Molecular modeling and enzymatic studies of the interaction of a choline analogue and acetylcholinesterase / Stefano, Alcaro; Scipione, Luigi; Francesco, Ortuso; Salvatore, Posca; Vincenzo, Rispoli; Domenicantonio, Rotiroti. - In: BIOORGANIC & MEDICINAL CHEMISTRY LETTERS. - ISSN 0960-894X. - STAMPA. - 12:20(2002), pp. 2899-2905. [10.1016/s0960-894x(02)00554-1]
Molecular modeling and enzymatic studies of the interaction of a choline analogue and acetylcholinesterase
SCIPIONE, Luigi;
2002
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
