An investigation of new designed carbamate drives for acetylcholinesterase (AChE) Inhibitor using molecular docking and molecular dynamic simulation (MD) methods

The physiological role of AChE is to effectively terminate cholinergic signals by hydrolyzingacetylcholine (ACh), in the bottom of a narrow 20 Å deep gorge. Carbamyl moiety in thecarbamylated AChE can be split from the enzyme by spontaneous hydrolysis (in about 30-40min), therefore carbamates are considered reversible AChE inhibitors and this property makethem a good candidate to neurotherapic uses [1]. In the present study, we have designed newcarbamate AChE inhibitors by changing the alkyl substituents, oxygen and sulfur. Thendetails of binding modes and binding energies have been studied using molecular dockingand molecular dynamic simulation methods and upon to the results, good candidates tomedical and pesticide uses are selected among a list of carbamate compounds.