IAPP (Islet Amyloid polypeptide)is involved in the death of pancreatic Beta-cells triggering Type 2 Diabetes mellitus syndrom. Our previous Neutron Reflectometry and small angle scattering experiments were extremely informative and showed that i) it can extract lipids from a POPC bilayer and permeate it thans to its N-terminal half; ii) the amyloid aggregation promoted by its C-terminal half, compete with this process of lipid depletion; iii) a significative amount of lipids can be incorporated in the amyloid aggregates.Together, these results suggest that lipid depletion could be the mechanism of cytotoxicity of this peptide. We propose to use the same techniques to understand cell specificity of IAPP, starting by exploring the role of electrostatic charges in the interaction of IAPP with model memebranes.