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

14 Citations (Scopus)

41 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",

note = "Publisher Copyright: {\textcopyright} 2015 WILEY-VCH Verlag GmbH \& Co. KGaA, Weinheim.",

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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

Y1 - 2015/5/20

N2 - 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.

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

UR - https://www.scopus.com/pages/publications/84929161789

U2 - 10.1002/smll.201402674

DO - 10.1002/smll.201402674

M3 - Article

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SP - 2257

EP - 2262

JO - Small

JF - Small

IS - 19

ER -

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

Abstract

Keywords

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