In Silico Molecular Docking Analysis of Nilotinib-Mediated Inhibition of Alpha-Synuclein Phosphorylation in Parkinson's Disease

This article employs an innovative molecular docking approach to explore alternatives to the palliative treatments historically used for Parkinson's disease management. Specifically, we analyze the interaction between residues 91 and 39 of the $\alpha$-synuclein protein and the drug nilotinib, as opposed to its conventional application targeting cAbl kinase to inhibit phosphorylation-a process frequently associated with Lewy body formation. Our results demonstrate successful docking of nilotinib with $\alpha$-synuclein, with the optimal interaction exhibiting a binding energy of-5.00 kcal/mol and ligand efficiency of-0.17 kcal/mol/atom. This investigation aims to evaluate the potential for significantly mitigating phosphorylation effects in Parkinson's disease, thereby providing a robust foundation for future therapeutic development.