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 journalArticleAcademicpeer-review

6 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 languageUndefined
Pages (from-to)2257-2262
JournalSmall
Volume11
Issue number19
DOIs
Publication statusPublished - 15 Jan 2015

Keywords

  • IR-95651
  • METIS-309191

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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author = "A. Stefanovic and Claessens, {Mireille Maria Anna Elisabeth} and Christian Blum and Vinod Subramaniam",
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doi = "10.1002/smll.201402674",
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volume = "11",
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Alpha-Synuclein Amyloid Oligomers Act as Multivalent Nanoparticles to Cause Hemifusion in Negatively Charged Vesicles. / Stefanovic, A.; Claessens, Mireille Maria Anna Elisabeth; Blum, Christian; Subramaniam, Vinod.

In: Small, Vol. 11, No. 19, 15.01.2015, p. 2257-2262.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Alpha-Synuclein Amyloid Oligomers Act as Multivalent Nanoparticles to Cause Hemifusion in Negatively Charged Vesicles

AU - Stefanovic, A.

AU - Claessens, Mireille Maria Anna Elisabeth

AU - Blum, Christian

AU - Subramaniam, Vinod

PY - 2015/1/15

Y1 - 2015/1/15

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 - IR-95651

KW - METIS-309191

U2 - 10.1002/smll.201402674

DO - 10.1002/smll.201402674

M3 - Article

VL - 11

SP - 2257

EP - 2262

JO - Small

JF - Small

SN - 1613-6810

IS - 19

ER -