Journal
FEBS LETTERS
Volume 588, Issue 23, Pages 4457-4463Publisher
WILEY
DOI: 10.1016/j.febslet.2014.10.016
Keywords
Amyloid; Protein aggregation; Vesicle; Oligomer; Fibril; Phospholipid; Suprafibrillar aggregate
Funding
- VIDI grant from the Netherlands Organization for Scientific Research (NWO) [700.59.423]
- Stichting voor Fundamenteel Onderzoek der Materie (FOM), Nederland
- NWO-CW TOP [700.58.3012]
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We studied alpha-synuclein (alpha S) 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 aS. Seeding aS 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. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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