IAPP is an amyloid peptide which causes diabetes by killing beta-pancreatic cells. However, its mechanism of cell destruction is still under debate. It is not clear which structural species is responsible of cell disruption, whether it is the final amyloid fibril, a fibrillation-intermediary polymer or a stable oligomer. Here, we intend to characterize the mechanism of IAPP interaction with a model membrane by studying how different fragments of this peptide adsorbs, inserts and possibly desorbs, once in an oligomeric form, in order to map IAPP sequence for membrane disruption capabilities. The results of this functional study will bring direct information about the role of each part of IAPP in the bilayer disruption mechanism that will have tremendous implication in the development of therapeutics against amyloid diseases.