The formation of these fibrils starts with the misfolding of alpha-synuclein creating an abnormal conformation. This abnormal conformation acts as a seed for other alpha-synuclein to clump together. In the next step, elongation of these fibrils to long fibrils takes place. Slowly the fibrils continue to grow and mature forming a stable and resistant form of the insoluble fibril clumps. Therefore, inhibition of this fibril formation is an area of active research. Some effective treatments that can inhibit these fibrils are (a) small molecule inhibitors: these small molecules are suggested to bind alpha-synuclein and can prevent its formation. Another approach is the use of chaperone proteins. These naturally occurring proteins interact with PDrelated proteins and help them to fold correctly. Studies have shown that this chaperone protein can be used to prevent the misfolding of alpha-synuclein. Additionally, immunotherapy involving the usage of antibodies to target and clean alpha-synuclein aggregates can also be used as a solution. In this therapy, the toxic proteins are neutralized which assists in preventing the disease from spreading. Molecular docking is a method that predicts how two or more molecular structures fit together.( ) It plays a crucial role in drug discovery because of its ability to simulate the interaction between small molecules and proteins. It is performed to find the strongest binding model of a ligand with a three-dimensional protein. If this is used properly one would be able to study protein-ligand interactions, helping them to develop effective drugs. In addition to this molecular docking is also able to assist with virtual screening on large libraries of compounds and rank results. Molecular docking is a powerful tool because of its ability to predict molecular interactions and potential drug candidates. The application of molecular docking advances our understanding of the intricate relationships between proteins and ligands allowing us to make incredible steps in the scientific world. Molecular docking simulations have been employed in the present study to determine the chemical compounds that interacts with the alpha-synuclein protein and prevent its clumping. Our hypothesis is that these ligands can interact at the interface of the amyloids and could potentially block the binding and thus preventing the fibril formation.