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

Himanshu Chaudhary; Anja N.D. Stefanovic; Vinod Subramaniam; Mireille M.A.E. Claessens

doi:10.1016/j.febslet.2014.10.016

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

Himanshu Chaudhary, Anja N.D. Stefanovic, Vinod Subramaniam, Mireille M.A.E. Claessens^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

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Abstract

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

Original language	English
Pages (from-to)	4457-4463
Number of pages	7
Journal	FEBS letters
Volume	588
DOIs	https://doi.org/10.1016/j.febslet.2014.10.016
Publication status	Published - 2014

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2023 OA procedure

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title = "Membrane interactions and fibrillization of alpha-synuclein play an essential role in membrane disruption",

abstract = "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",

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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 -

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

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