Backgrounds Finding novel therapies that stop a-synuclein oligomerisation and, consequently, the progression of Parkinson's disease (PD) may result from the identification of putative neuroprotective substances that bind to a-synuclein.Thus, in silico methods play a critical role in cutting down on the time and expenses related to testing drugs with negligible or no neuroprotective effect in experiments.
Methods Prior research has examined novel compounds for naturally occurring antioxidant phytochemicals, chosen AI-based compounds, and docked these compounds with the protein α-synuclein (1XQ8) The molecule with the highest binding affinity is used in MD simulation to ensure structural stability.
Results We investigate the regulatory functions of the alpha synuclein protein using computational molecular docking and MD simulations. MD simulations revealed that the primary amino acid residues Lys32, Leu38, Val40, Glu35, Gly36, Lys43, Thr44, Lys45, Glu46, Gly47, and Val48 bind to certain amino acid residues of alpha synuclein, especially the basic residues located in amino acid residues 1–61. These results validate previous experimental studies. This analysis using MD modeling revealed the N-terminal residues. Eight natural and ten artificial intelligence-based ligands were docked with the alpha synuclein protein. Our investigation revealed that the ligand4 would assist to suppress the disease condition of Parkinson's disease, based on prior research on the potential regulatory role of various natural phytochemicals that are significant for Parkinson's disease.
Conclusion Therefore, it is thought that these phytochemicals could be employed as potential bioenhancers in the therapy of Parkinson's disease. The current investigation could be expanded for future experimental validation and would provide light on the identification of natural phytochemicals and AI-based compounds against SNCA as an alternative treatment of Parkinson's disease.
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