Membrane interactions and fibrillization of alpha-synuclein play an essential role in membrane disruption

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Title:	Membrane interactions and fibrillization of alpha-synuclein play an essential role in membrane disruption
Author(s):	Chaudhary, H.; Stefanovic, A.N.; Subramaniam, V.; Claessens, M.M.B.
Publication year:	2014
Source:	Febs Letters, vol. 588, iss. 23, (2014), pp. 4457-4463
ISSN:	0014-5793
Related links:	http://www.ncbi.nlm.nih.gov/pubmed/25448986
DOI:	http://dx.doi.org/10.1016/j.febslet.2014.10.016
Publication type:	Article / Letter to editor
Please use this identifier to cite or link to this item : http://hdl.handle.net/2066/140717
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Subject:	Radboudumc 2: Cancer development and immune defence RIMLS: Radboud Institute for Molecular Life Sciences
Organization:	Tumorimmunology
Journal title:	Febs Letters
Volume:	vol. 588
Issue:	iss. 23
Page start:	p. 4457
Page end:	p. 4463
Abstract:	We studied alpha-synuclein (alphaS) aggregation in giant vesicles, and observed dramatic membrane disintegration, as well as lipid incorporation into micrometer-sized suprafibrillar aggregates. In the presence of dye-filled vesicles, dye leakage and fibrillization happen concurrently. However, growing fibrils do not impair the integrity of phospholipid vesicles that have a low affinity for alphaS. Seeding alphaS aggregation accelerates dye leakage, indicating that oligomeric species are not required to explain the observed effect. The evolving picture suggests that fibrils that appear in solution bind membranes and recruit membrane-bound monomers, resulting in lipid extraction, membrane destabilization and the formation of lipid-containing suprafibrillar aggregates.