TY - JOUR
T1 - Membrane interactions and fibrillization of alpha-synuclein play an essential role in membrane disruption
AU - Chaudhary, Himanshu
AU - Stefanovic, Anja N.D.
AU - Subramaniam, Vinod
AU - Claessens, Mireille M.A.E.
PY - 2014
Y1 - 2014
N2 - We studied α-synuclein (αS) 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 αS. Seeding αS 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
AB - We studied α-synuclein (αS) 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 αS. Seeding αS 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
KW - 2023 OA procedure
U2 - 10.1016/j.febslet.2014.10.016
DO - 10.1016/j.febslet.2014.10.016
M3 - Article
SN - 0014-5793
VL - 588
SP - 4457
EP - 4463
JO - FEBS letters
JF - FEBS letters
ER -