Alpha-synuclein fibrils have been recently been isolated from dementia body and was used in this research . The formation of these fibrils takes place through the process of nucleation and elongation. The interfaces at the ends of the fibrils are crucial sites for the addition of monomers and elongation of the fibrils and these inhibitors can effectively block the addition of new monomers and prevent fibril growth. Due to a high accessibility and higher binding affinity, these interfaces provided an easier, open, and accessible region for inhibitor binding. Therefore, in this study we have targeted only the interface and have proposed inhibitors that can bind strongly to this surface. On the fibril surface valine, glycine, alanine, lysine, threonine and glutamic acid amino acids are present in a higher concentration within fibrils and can provide insights into potential strategies for fibril formation, Figure . For instance, Val is non-polar and hydrophobic in nature; hence, inhibitors should form hydrophobic interactions to the protein. On the other hand, Lys is positive, Thr is polar, and Glu is negative in nature and these amino acids can form hydrogen bonds with the protein. Gly, Ala, and Thr amino acids are smaller in size and are not properly exposed to the surface for interactions. Other amino acids Lys and Thr are not located at binding region of the protein. From our docking studies we found key amino acids that commonly bind to the predicted ligands are Val40, Val71, Glu73, Val74, and Phe94. In addition, all the predicted ligands formed both hydrogen bonds and hydrophobic interactions with the protein.