Alpha‐Synuclein Amyloid Oligomers Act as Multivalent Nanoparticles to Cause Hemifusion in Negatively Charged Vesicles
Source abstract
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.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Alzheimer's disease research and treatments · Lipid Membrane Structure and Behavior · Parkinson's Disease Mechanisms and Treatments
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Nanobiophysics, MESA+ Institute for Nanotechnology Faculty of Science and Technology University of Twente PO Box 217 7500 AE Enschede The Netherlands
MIRA Institute for Biomedical Technology and Technical Medicine University of Twente PO Box 217 7500 AE Enschede The Netherlands
FOM Institute AMOLF Science Park 104 1098 XG Amsterdam The Netherlands
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