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Mechanism of Membrane Interaction and Disruption by α-Synuclein

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Institute of Physical Chemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland
Institute of Physical Chemistry, ETH Zurich, Wolfgang-Pauli Strasse 10, 8093 Zurich, Switzerland
§ Electron Microscopy Center of the ETH Zurich (EMEZ), Schafmattstrasse 18, 8093 Zurich, Switzerland
Cite this: J. Am. Chem. Soc. 2011, 133, 48, 19366–19375
Publication Date (Web):October 6, 2011
Copyright © 2011 American Chemical Society

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    Parkinson's disease is a common progressive neurodegenerative condition, characterized by the deposition of amyloid fibrils as Lewy bodies in the substantia nigra of affected individuals. These insoluble aggregates predominantly consist of the protein α-synuclein. There is increasing evidence suggesting that the aggregation of α-synuclein is influenced by lipid membranes and, vice versa, the membrane integrity is severely affected by the presence of bound aggregates. Here, using the surface-sensitive imaging technique supercritical angle fluorescence microscopy and Förster resonance energy transfer, we report the direct observation of α-synuclein aggregation on supported lipid bilayers. Both the wild-type and the two mutant forms of α-synuclein studied, namely, the familiar variant A53T and the designed highly toxic variant E57K, were found to follow the same mechanism of polymerization and membrane damage. This mechanism involved the extraction of lipids from the bilayer and their clustering around growing α-synuclein aggregates. Despite all three isoforms following the same pathway, the extent of aggregation and their effect on the bilayers was seen to be variant and concentration dependent. Both A53T and E57K formed cross-β-sheet aggregates and damaged the membrane at submicromolar concentrations. The wild-type also formed aggregates in this range; however, the extent of membrane disruption was greatly reduced. The process of membrane damage could resemble part of the yet poorly understood cellular toxicity phenomenon in vivo.

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    Additional methods, SAF microscopy images showing adsorption of WT, A53T, and E57K α-Syn at 200 nM, adsorption of α-Syn to SLBs containing various amounts of fluorophores, adsorption of E57K α-Syn on a 20% DOPS SLB, and OC antibody positive α-Syn aggregates, confocal microscopy images showing p-FTAA staining of α-Syn at 400 nM (A53T) and 3 μM (E57K) and p-FTAA staining of α-Syn fibrils grown in vitro, cryo-SEM image of clean SLBs, and complete refs 13, 15, 38, 47, 55, and 56. This material is available free of charge via the Internet at

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