Alpha-synuclein amyloid oligomers act as multivalent nanoparticles to cause hemifusion in negatively charged vesicles

Anja N.D. Stefanovic; Mireille M.A.E. Claessens; Christian Blum; Vinod Subramaniam

doi:10.1002/smll.201402674

Alpha-synuclein amyloid oligomers act as multivalent nanoparticles to cause hemifusion in negatively charged vesicles

Anja N.D. Stefanovic, Mireille M.A.E. Claessens^*, Christian Blum, Vinod Subramaniam

^*Corresponding author for this work

Nanobiophysics

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

12 Citations (Scopus)

6 Downloads (Pure)

Abstract

Multivalent membrane binding sites on the α-synuclein oligomer result in clustering of vesicles and hemifusion of negatively charged model membranes. These multivalent, biological nanoparticles are reminiscent of inorganic nanoparticles in their interactions with membranes. Alpha-synuclein oligomers induce lipid exchange efficiently, with fewer than 10 oligomers/vesicle required to complete hemifusion. No full fusion or vesicle content mixing is observed.

Original language	English
Pages (from-to)	2257-2262
Number of pages	6
Journal	Small
Volume	11
Issue number	19
DOIs	https://doi.org/10.1002/smll.201402674
Publication status	Published - 20 May 2015

Keywords

Alpha-synuclein
Hemifusion
Multivalent nanoparticles
Oligomers
Parkinson's disease
Vesicles
2023 OA procedure

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10.1002/smll.201402674

ArticleFinal published version, 589 KBLicence: Taverne

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title = "Alpha-synuclein amyloid oligomers act as multivalent nanoparticles to cause hemifusion in negatively charged vesicles",

abstract = "Multivalent membrane binding sites on the α-synuclein oligomer result in clustering of vesicles and hemifusion of negatively charged model membranes. These multivalent, biological nanoparticles are reminiscent of inorganic nanoparticles in their interactions with membranes. Alpha-synuclein oligomers induce lipid exchange efficiently, with fewer than 10 oligomers/vesicle required to complete hemifusion. No full fusion or vesicle content mixing is observed.",

keywords = "Alpha-synuclein, Hemifusion, Multivalent nanoparticles, Oligomers, Parkinson's disease, Vesicles, 2023 OA procedure",

author = "Stefanovic, {Anja N.D.} and Claessens, {Mireille M.A.E.} and Christian Blum and Vinod Subramaniam",

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AU - Stefanovic, Anja N.D.

AU - Claessens, Mireille M.A.E.

AU - Blum, Christian

AU - Subramaniam, Vinod

PY - 2015/5/20

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AB - Multivalent membrane binding sites on the α-synuclein oligomer result in clustering of vesicles and hemifusion of negatively charged model membranes. These multivalent, biological nanoparticles are reminiscent of inorganic nanoparticles in their interactions with membranes. Alpha-synuclein oligomers induce lipid exchange efficiently, with fewer than 10 oligomers/vesicle required to complete hemifusion. No full fusion or vesicle content mixing is observed.

KW - Alpha-synuclein

KW - Hemifusion

KW - Multivalent nanoparticles

KW - Oligomers

KW - Parkinson's disease

KW - Vesicles

KW - 2023 OA procedure

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EP - 2262

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JF - Small

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Alpha-synuclein amyloid oligomers act as multivalent nanoparticles to cause hemifusion in negatively charged vesicles

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Keywords

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