Fig. 6

Molecular docking simulation of α-synuclein (α-syn) structures C2 (a), C5 (b), C7 (c), and C8 (d) bound to DPCPX. Below full 3D representations show magnified binding pocket of α-syn and the locations of amino acid residues responsible for each drug binding. Bold black dashed lines and amino acid residues indicate hydrogen bonding, while the grey dashed lines and amino acid residues indicate hydrophobic interactions. Hydrogen bonding of DPCPX with both the N- and C-terminal amino acid residues is observed in C7 α-syn structure (c). DPCPX also forms hydrogen bond with either the N-terminal (C5 α-syn structure in b) or C-terminal amino acids (C8 α-syn structure in d) and also hydrophobic bonds with portions of the NAC region. N-and C-terminal binding of DPCPX is also observed without hydrogen bonding (C2 α-syn structure in a). The molecular docking study was carried out using Autodock Vina module implemented in PyRx tool. Protein and ligand interactions were analyzed and visualized through Pymol and LigPlot +