Recently, amyloid fibrils formation is the subject of many scientific researchers from medicine to foodscience. Amyloid fibrils formation is the base of some diseases such as type II diabetes, Parkinson andAlzheimer. There are some evidences that show some biological molecules inhibited protein fibrillationand aggregation. In this study, the effect of curcumin on protein fibrillation was considered. Using a rangeof techniques including thioflavin T (ThT) and monitoring of the changes in reactive oxygen species(ROS) levels upon incubation of curcumin with some proteins such as beta-lactoglobulin and Humanserum albumin (HSA) have been verified inhibition effects of it. The results imply two assumptionsregarding the inhibition mechanism of amyloid protein fibril formation by this compound; the first is forspecific structural conformation of it that is necessary for b-sheet interaction and stabilization of theinhibition–protein complex; and the second is accused to aromatic interaction between curcumin andaromatic residues in the amyloidogenic sequence that may direct the inhibitor to the amyloidogenic coreand facilitate interaction, but interfere with fibril assembly. So consumption of curcumin may be effectivein preventing and curing the disorders.