Protein misfolding and amyloid aggregation cause many human diseases, including Alzheimer's disease (AD), Type II Diabetes (T2D), and Parkinson's disease.1 Despite the morphological variations, amyloid aggregates causing these diseases are rich in highly ordered cross-β-sheet structures.2 Amylin or human Islet Amyloid Polypeptide (hIAPP), co-secreted with insulin from pancreatic β-cell, changes from non-toxic monomers to toxic oligomers at physiological conditions. This evidence concerns the gene INS and Alzheimer disease.