In silico molecular docking of niloticin with acetylcholinesterase 1 (AChE1) of Aedes aegypti L. (Diptera: Culicidae): a promising molecular target

Abstract

Synthetic insecticides used in mosquito control program are harmful to environment and also affect other associated organisms. As a choice, plant-based natural compounds proved to be a good alternative to synthetic insecticides. In a study, we had reported niloticin (C30H48O3) from the plant Limonia acidissima L. was effective and disturbed the larval growth of A. aegypti. The main molecular target for many commercially available synthetic mosquitocides is acetylcholinesterase (AChE), which plays a major role in larval knockdown/resistant mechanisms. AChE1 is a serine protease, which fulfills the physiological function of neurotransmitter hydrolysis at synapses. In the present study, we performed molecular docking studies with acetylcholinesterase 1 (AChE1) of A. aegypti with niloticin (C30H48O3) and compared with commercially available chemical larvicidal compound temephos (C16H20O6P2S3). The docking results revealed that the binding affinities and energy values of niloticin (−8.4 kcal/mol) were found to be significantly higher than temephos (−4.75 kcal/mol). Both niloticin (C30H48O3) and temephos (C16H20O6P2S3) showed the same binding residues (THR’58 and HIS’62) on AChE1. Further, niloticin produced least binding energy (−8.4 kcal/mol), good inhibition constant value (695.18 μM) and high ligand efficiency (0.25) than temephos, suggesting that niloticin (C30H48O3) could be used against the larvae of A. aegypti as an effective AChE1 inhibitor.