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Aim and Background: Amylloid fibrils are filamentus protein aggregates derived from various proteins and peptides. They can be distinguished from other type of features according to their appear shape and electron microscope images, also by dye binding methods, which can indicate induced cross beta structures. Amyloid fibrils are correlated to creating general disease, amyloidosis. Disease such Alzheimer, Parkinson, diabetes type II, and others disease which in each of them, the special kind of protein subjected to form amyloid or amyloid like fibrils. A variety of proteins which they are not converted to amyloid fibrils invivo, can be transform to amyloids in special unstabilizing conditions.
Materials and Methods: Congored spectrophotometric method, ThT fluorescence and CD Data was used for fibril formation assay and Transmission Electron microscopy was used for final affirmation of fibrils.
Results: results shows that maximum amyloid formation was in 5 mg.ml-1 protein concentration, 50 ºC and 7.4 buffer pH.

Conclusion:
With the new approach obtained from the kappa casein, amyloid fibers can be introduced as new nanomaterials, Thus the results, given the diverse applications of nanomaterials, can affirm process optimization of amyloid production from accessible and inexpensive protein in milk.