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Alpha‐Synuclein Amyloid Oligomers Act as Multivalent Nanoparticles to Cause Hemifusion in Negatively Charged Vesicles
Author(s) -
Stefanovic Anja N. D.,
Claessens Mireille M. A. E.,
Blum Christian,
Subramaniam Vinod
Publication year - 2015
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201402674
Subject(s) - vesicle , membrane , oligomer , biophysics , chemistry , nanoparticle , lipid vesicle , amyloid (mycology) , alpha synuclein , lipid bilayer , vesicle fusion , materials science , polymer chemistry , nanotechnology , biochemistry , synaptic vesicle , biology , medicine , pathology , inorganic chemistry , disease , parkinson's disease
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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