Simultaneous IR-spectroscopic observation of α-synuclein, lipids, and solvent reveals an alternative membrane-induced oligomerization pathway

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ChemBioChem. 2017, 18(23), pp. 2312-2316. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201700355
Zusammenfassung

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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570 Biowissenschaften, Biologie
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ISO 690FALLAH, 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.201700355
BibTex
@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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