Figures and display most stable two-and three-dimensional structure alpha synuclein-ligand complex. This research indicates that the majority of the ligand-protein interactions were hydrophobic. Nonetheless, the fibril-ligand interactions were also found to involve hydrogen bonding. The analysis of our predicted inhibitors was performed by applying the PLIP software, Table and Figure . This web server is used to find the chemical interactions between protein and ligand complexes. Based on our analysis of Ligand I had five hydrophobic interactions with The docking results were further verified by carrying out two sets of molecular docking simulations shown in Figure and b. In the first set, molecular docking amid ligand-bound fibril and free fibrils was carried out, Figure . In the second set, molecular docking between free fibril and free fibril was performed, Figure . Because of the ligand existence, two fibrils (Fibril 1 and Fibril 2) were not able to bind properly. However, in the second set, due to the absence of the ligands, the two fibrils formed strong interface binding. Indicating that the fibril interface contact is inhibited by the ligand.