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Simultaneous IR-Spectroscopic Observation of [alpha]-Synuclein, Lipids, and Solvent Reveals an Alternative Membrane-Induced Oligomerization Pathway

The intrinsically disordered protein [alpha]-synuclein ([alpha]S), a known pathogenic factor for Parkinson's disease, can adopt defined secondary structures when interacting with membranes or during fibrillation. The [alpha]S-lipid interaction and the implications of this process for aggregatio...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2017-12, Vol.18 (23), p.2312
Main Authors: Fallah, Mohammad A, Gerding, Hanne R, Scheibe, Christian, Drescher, Malte, Karreman, Christiaan, Schildknecht, Stefan, Leist, Marcel, Hauser, Karin
Format: Article
Language:English
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Summary:The intrinsically disordered protein [alpha]-synuclein ([alpha]S), a known pathogenic factor for Parkinson's disease, can adopt defined secondary structures when interacting with membranes or during fibrillation. The [alpha]S-lipid interaction and the implications of this process for aggregation and damage to membranes are still poorly understood. Therefore, we established a label-free infrared (IR) spectroscopic approach to allow simultaneous monitoring of [alpha]S conformation and membrane integrity. IR showed its unique sensitivity for identifying distinct [beta]-structured aggregates. A comparative study of wild-type [alpha]S and the naturally occurring splicing variant [alpha]S [Delta]exon3 yielded new insights into the membrane's capability for altering aggregation pathways.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.201700355