Alpha-Synuclein Amyloid Oligomers Act as Multivalent Nanoparticles to Cause Hemifusion in Negatively Charged Vesicles

A. Stefanovic; Mireille Maria Anna Elisabeth 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

A. Stefanovic, Mireille Maria Anna Elisabeth Claessens, Christian Blum, Vinod Subramaniam

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

8 Citations (Scopus)

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	Undefined
Pages (from-to)	2257-2262
Journal	Small
Volume	11
Issue number	19
DOIs	https://doi.org/10.1002/smll.201402674
Publication status	Published - 15 Jan 2015

Keywords

IR-95651
METIS-309191

Access to Document

10.1002/smll.201402674

Cite this

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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",

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AU - Claessens, Mireille Maria Anna Elisabeth

AU - Blum, Christian

AU - Subramaniam, Vinod

PY - 2015/1/15

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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

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KW - METIS-309191

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