It is very likely that type 2 diabetes is caused by the human islet amyloid polypeptide (hIAPP) which is proposed to induce pancreatic â-cell membrane penetration and forms fibrils in the body's pancreas. We studied the structures and kinetics of hIAPP folding in the presence of lipid vesicles using 2DIR spectroscopy. hIAPP accumulates at the water lipid interface through electrostatic interactions and, somehow, the membrane catalyses beta-sheet amyloid formation. Comparison of the spectra with and without membranes shows that the folding pathway of hIAPP is very different when it is membrane catalyzed. Furthermore, we have preliminary evidence of an intermediate state that is not beta-sheet on the folding pathway with membranes. Our results so far point to 2D IR spectroscopy as a powerful tool for studying amyloid fiber formation.