Structural changes of amyloid proteins in lipid membrane system have been studied to further understanding of the effect of protein-lipid interactions on the fibrillation process.We monitor insulin fibrillation in organic-water mixtures, which provides a model system of lipid membrane [1].Careful monitoring reveals that the binary mixture solutions of water with organic solvent enhance the fibrillation kinetics and the abundance, whereas organic solvents without water suppress the fibrillation of insulin.α-Synuclein (α-Syn), which is associated with the pathogenesis of Parkinsons disease, is known to have protein conformation changes and amyloid aggregation under the membranes influence.We have investigated conformation change of □-Syn to helical structures by absorption into large unilamellar veiscles using solution SAXS and electrospray ionization ion mobility mass spectrometry [2].Combining two studies provides the insight of influence of water limited environment to the structures of amyloid proteins related to their fibrillation processes.