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.
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