Potential Molecular Docking of Four Acetylcholinesterase Inhibitors

Nahd Mohamed Elmaki¹, Inass A Al Sadawi², Anton Hermann³ and Abdul M Gbaj*²

Received:September 04, 2018;   Published: September 10, 2018

DOI: 10.32474/DDIPIJ.2018.02.000136

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Abstract

Molecular modeling attempts to study the function, structure and inhibition of the acetylcholinesterase enzyme due to the fact that the inhibition of this enzyme is importance to medical conditions such as Alzheimer’s disease, myasthenia gravis and Parkinson’s disease, and it is also important in eminent toxicological susceptibility to nerve agents. In this study we present an approach for forecasting the inhibitory activity of acetylcholinesterase (AChE) inhibitors by using docking studies. The docking studies were done on acetylcholinesterase to attain the conformation of the enzyme in water surroundings. The obtained conformation of the enzyme was used for docking with four inhibitors (physostigmine, neostigmine, pyridostigmine and rivastigmine). Docking analysis showed that hydrogen bonds and hydrophobic interactions play important tasks in the acetylcholinesterase -inhibitor complex. Subsequently, all inhibitors that bind at the catalytic site of acetylcholinesterase and their interactions with acetylcholinesterase were studied. In addition, conformation stability of acetylcholinesterase -inhibitors was studied using simulation docking technique. The complex showed that acetylcholinesterase conformation did not change significantly in the presence of the four inhibitors. This paper showed important studies on acetylcholinesterase and assists to illuminate the four inhibitors interdependencies using molecular modeling.

Keywords: Acetylcholinesterase; Molecular docking; Physostigmine; Neostigmine; Pyridostigmine; Rivastigmine

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