Nanoscale electrostatic domains in cholesterol-laden lipid membranes create a target for amyloid binding.

ABSTRACT: Amyloid fibrils are associated with multiple neurodegenerative disorders, such as Alzheimer's disease. Although biological membranes are involved in fibril plaque formation, the role of lipid membrane composition in fibril formation and toxicity is not well understood. We investigated the effect of cholesterol on the interaction of model lipid membranes with amyloid-β peptide (Aβ). With atomic force microscopy we demonstrated that binding of Aβ (1-42) to DOPC bilayer, enriched with 20% cholesterol, resulted in an intriguing formation of small nonuniform islands loaded with Aβ. We attribute this effect to the presence of nanoscale electrostatic domains induced by cholesterol in DOPC bilayers. Using frequency-modulated Kelvin probe force microscopy we were able to resolve these nanoscale ele

SUBMITTER: Drolle E 

PROVIDER: S-EPMC3443788 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature