Publikation: Simultaneous IR-spectroscopic observation of α-synuclein, lipids, and solvent reveals an alternative membrane-induced oligomerization pathway
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The intrinsically disordered protein α-synuclein (αS), a known pathogenic factor for Parkinson's disease, can adopt defined secondary structures when interacting with membranes or during fibrillation. The αS-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 simultaneously monitor αS conformation and membrane integrity. IR showed its unique sensitivity for identifying distinct α-structured aggregates. A comparative study of wildtype αS and the naturally occurring splicing variant αS Δexon3 yielded new insights into the membrane's capability of altering aggregation pathways.
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FALLAH, Mohammad A., Hanne R. GERDING, Christian SCHEIBE, Malte DRESCHER, Christiaan KARREMAN, Stefan SCHILDKNECHT, Marcel LEIST, Karin HAUSER, 2017. Simultaneous IR-spectroscopic observation of α-synuclein, lipids, and solvent reveals an alternative membrane-induced oligomerization pathway. In: ChemBioChem. 2017, 18(23), pp. 2312-2316. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201700355BibTex
@article{Fallah2017-12-05Simul-40331, year={2017}, doi={10.1002/cbic.201700355}, title={Simultaneous IR-spectroscopic observation of α-synuclein, lipids, and solvent reveals an alternative membrane-induced oligomerization pathway}, number={23}, volume={18}, issn={1439-4227}, journal={ChemBioChem}, pages={2312--2316}, author={Fallah, Mohammad A. and Gerding, Hanne R. and Scheibe, Christian and Drescher, Malte and Karreman, Christiaan and Schildknecht, Stefan and Leist, Marcel and Hauser, Karin} }
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