Interaction of mutated A-beta peptides with single 'raft' model membrane
A-beta oligomers were identified as the main cause of synaptic dysfunction leading to alterations in both neuronal activity and cognitive function in Alzheimer's Disease. A-beta oligomers, are "membrane-active" species that can promote membrane punctuation and increase its permeability. A putative site on the plasma membrane for amyloid-membrane interaction are the lipid "raft", enriched in cholesterol and sphingolipids. We identified a more fibrillogenic analogue of A-beta; carrying Ala-to-Val substitution, that promotes a peculiar pathway of oligomerization, forming a connected system similar to a polymer network. The heterotypic interaction between the mutated and wild-type A-beta affects nucleation-dependent A-beta polymerization, preventing amyloid fibril formation. Aim of this proposal is the study of the structural details of the interaction between the oligomeric species of A-beta amyloid and a raft-mimicking model membrane in the case of the A2V mutant A-beta peptide. Moreover we plan to investigate in detail if the mutated + wild type A-beta mixture displays a different propensity to interact with model membranes.
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RONDELLI Valeria Maria; BROCCA Paola; CANTU Laura; DEL FAVERO Elena; FRAGNETO Giovanna; GUTFREUND Philipp and MOTTA Simona. (2015). Interaction of mutated A-beta peptides with single 'raft' model membrane. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-733
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