Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing

Bart van Rooijen, Mireille Maria Anna Elisabeth Claessens, Vinod Subramaniam

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Membrane disruption by oligomeric α-synuclein (αS) is considered a likely mechanism of cytotoxicity in Parkinson’s disease (PD). However, the mechanism of oligomer binding and the relation between binding and membrane disruption is not known. We have visualized αS oligomer-lipid binding by fluorescence microscopy and have measured membrane disruption using a dye release assay. The data reveal that oligomeric αS selectively binds to membranes containing anionic lipids and preferentially accumulates into liquid disordered (Ld) domains. Furthermore, we show that binding of oligomers to the membrane and disruption of the membrane require different lipid properties. Thus membrane-bound oligomeric αS does not always cause bilayer disruption.
Original languageUndefined
Pages (from-to)3788-3792
Number of pages5
JournalFEBS letters
Issue number27
Publication statusPublished - 2008


  • IR-78905
  • Synuclein
  • Parkinson’s disease
  • Lipid
  • Amyloid
  • Confocal fluorescence microscopy
  • Pore
  • METIS-250788

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