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

Rooijen van, Bart D. and Claessens, Mireille M.A.E. and Subramaniam, Vinod (2008) Membrane binding of oligomeric α-synuclein depends on bilayer charge and packing. FEBS Letters, 582 (27). pp. 3788-3792. ISSN 0014-5793

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Abstract:	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.
Item Type:	Article
Copyright:	© 2008 Federation of European Biochemical Societies
Faculty:	Science and Technology (TNW)
Research Group:	Nano-Biophysics (NBP)
Link to this item:	http://purl.utwente.nl/publications/78905
Official URL:	http://dx.doi.org/10.1016/j.febslet.2008.10.009
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