Amylin is a 37 residue peptide with a disulfide bridge between the residues 2 and 7. This hormone co-secreted with insulin by pancreatic islet b-cells. It has been reported that amylin is able to form amyloid fibrils. Although these fibrils are not related with the manifestation of type 2 diabetes, they have a significant role in the aggravation of diabetic condition. In this study, the potential of amyloid formation and stability of amylin has been studied in 10 species with high sequence similarity (80%), with the use of molecular Dynamics simulation. Based on the structure of human amylin (2L86.pdb from Protein Data Bank) homology modeling technique was used to create 10 different species amylin. Simulation was performed using GROMACS version 4.6.1, with a 10 ns duration and 500K. The systems were solvated with SPC water molecules. Secondary structure content was calculated using DSSP. Other analyses such as energy, solvent accessible surface, radius of gyration, RMSD and RMSF were performed, using GROMACS. Human and Rat amylin were selected as non-aggregating peptides respectively. During simulation amylin showed remarkable Structural changes, and in most cases α-helical structures were lost. In some species with aggregating amylin, b -sheets were formed at the end of the simulation. Between the studied species, Pongoabelii peptide, one of the two species of orangutans used in this study, showed more stability alongside with more similarity to human amylin. Based on these results, this amylin specie could be proposed as a potential therapeutic peptide, as an alternative to rat amylin.