DOCKING STUDIES IN ACETYL CHOLINESTERASE INHIBITORY ACTIVITY OF DIMETHOATEJ. HELAN CHANDRA C, JAYARAMBALAKRISHNAN AND S. SRIDHAR
The objective of present study deals with Insilco acetyl cholinesterase inhibitory analysis of Organo phosphorous pesticide Dimethoate (O, O-dimethyl S-[2-(methyl amino)-2-oxoethyl] phosphorodithioate). To comprehend the mechanism of protein and pesticide binding and interaction, molecular docking was performed for the compounds predicting the probable binding mode of the inhibitors to the protein. Molecular docking studies were carried out using Auto Dock 4.0 and in silicoacetyl cholinesterase inhibitory activity was performed using acetyl cholinesterase as the receptor. Among the active residues identified, the binding conformation confirms that residues TYR337: OH of the acetyl cholinesterase may play an important role in its pesticide interaction. The results revealed that acetyl cholinesterase showed lowest binding energy value about -5.98 kcal/mol. It is concluded that Dimethoate binds strongly with acetyl cholinesterase inhibiting the enzyme that hydrolyzes the neurotransmitter acetylcholine (ACh) at cholinergic synapses in the nervous system.
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