Electrosynthesis, in Silico Ligand-Protein Interaction and Pharmacokinetic Studies of Some Aryl Sulfone Derivatives as Potential Acetylcholinesterase Inhibitors: Synthesis of aryl sulfones as acetylcholinesterase inhibitors

Abstract

Acetylcholinesterase (AChE) is an enzyme that catalyzes the hydrolysis of acetylcholine. Acetylcholine plays an essential role in learning and memory. Since acetylcholine deficiency is related to the pathogenesis of Alzheimer's disease, obtaining acetylcholinesterase inhibitors is of great interest. Here, a group of aryl sulfone derivatives with a catechol ring was synthesized by the electrochemical method. The structure of compounds was confirmed by 1HNMR and ESI-MS. Molecular docking studies of the synthesized compounds with AChE were performed and the results showed that all of the compounds have good theoretical affinities for the target enzyme, AChE. Moreover, the physicochemical properties and ADME parameters of synthesized compounds were predicted, which revealed that they have acceptable features as drug candidates. HIGHLIGHTS Aryl sulfone derivatives with catechol rings were synthesized by electrochemical method. Molecular docking studies of the compounds revealed good binding affinities against acetylcholinesterase. All of the synthesized compounds obey Lipinski’s rule of five which suggests them as good oral drug candidates