Our work represents the conformational change of α-synuclein under a polymer surfactant environment having higher molecular weight. Also, to give aetiology to many neurodegenerative diseases, we have studied interaction with various amphiphiles having different hydrophobic chains and head groups. We have also studied the mechanism involved in interaction with similar amphiphiles if we change the protein. Here we have studied on α-chymotrypsin at its fibrillar condition, since α-chymotrypsin undergo thermally induced disordered state it can give more aspects into molecular insights. We have also studied the behaviour of Regenerated Silk Fibroin in the ionic liquid-aqueous mixture, which showed the delaying of fibrillation at a certain volume percentage of ionic liquid in an aqueous solution of protein.