Alzheimer's disease (AD) represents one of the most common cause of dementia in the elderly population. One of its characteristic hallmarks is the accumulation of amyloid-beta (Aβ) peptide in neuritic plaques is. Nevertheless, significant evidences suggest that small, prefibrillar oligomers, arising at the beginning of its aggregation process, represent the most toxic species1,2. To better understand the cause of the early impairments in neuronal membrane damage it is important to characterize the seeding and growth of Aβ aggregates onto the lipid bilayer and the interaction of the membrane with different Aβ species. Increasing evidence indicated that ganglioside GM1 in lipid rafts plays a pivotal role in amyloid deposition of Aβ3. Despite many efforts have been recently made to characterize Aβ-lipid interactions, the effect of Aβ aggregation on dynamic properties and organization of lipid membranes is still unclear4. We present a neutron scattering study on the interaction of cell membrane models -large unilamellar liposomes (LUV)- in presence of both monomers and of the early toxic oligomers of Aβ peptide. Small Angle Neutron Scattering and Neutron Spin Echo experiments were performed, allowing to compare the structural effects of Aβ monomers and oligomers on LUVs and the impact on their slow dynamics.
1Selkoe, D.J. (1991) Nature 354, 432-433.
2Kayed, Ret al. (2009) J Biol Chem 284, 4230-4237.
3Hirai, Met al (2013) Eur Phys J E Soft Matter 36, 74.
4W. Gibson Wood et al. (2003) Biochim Biophys Acta 1610 281–290.