Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing
| Autor: | Bart D. van Rooijen, Vinod Subramaniam, Mireille Maria Anna Elisabeth Claessens |
|---|---|
| Přispěvatelé: | Executive board Vrije Universiteit, Faculty of Science and Technology, Nanobiophysics |
| Rok vydání: | 2008 |
| Předmět: |
Amyloid
Lipid Bilayers Biophysics METIS-250788 Research Support Biochemistry Oligomer Fluorescence Permeability chemistry.chemical_compound Structural Biology Journal Article Genetics Fluorescence microscope Non-U.S. Gov't Lipid bilayer Molecular Biology POPC Alpha-synuclein Synuclein Microscopy Microscopy Confocal Pore Research Support Non-U.S. Gov't Bilayer Parkinson Disease Cell Biology Lipid Confocal fluorescence microscopy Membrane Microscopy Fluorescence chemistry IR-78905 Confocal alpha-Synuclein Parkinson’s disease SDG 6 - Clean Water and Sanitation |
| Zdroj: | van Rooijen, B D, Claessens, M M A E & Subramaniam, V 2008, ' Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing ', FEBS Letters, vol. 582, no. 27, pp. 3788-92 . https://doi.org/10.1016/j.febslet.2008.10.009 FEBS Letters, 582(27), 3788-92. Elsevier FEBS letters, 582(27), 3788-3792. Wiley-Blackwell |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2008.10.009 |
| Popis: | Membrane disruption by oligomeric alpha-synuclein (alphaS) 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 alphaS oligomer-lipid binding by fluorescence microscopy and have measured membrane disruption using a dye release assay. The data reveal that oligomeric alphaS 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 alphaS does not always cause bilayer disruption. |
| Databáze: | OpenAIRE |
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