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Alpha-Synuclein Binds to the Inner Membrane of Mitochondria in an α-Helical Conformation

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2014

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https://doi.org/10.1002/cbic.201402281
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ChemBioChem. 2014, 15(17), pp. 2499-2502. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201402281

Zusammenfassung

The human alpha-Synuclein (αS) protein is of significant interest because of its association with Parkinson's disease and related neurodegenerative disorders. The intrinsically disordered protein (140 amino acids) is characterized by the absence of a well-defined structure in solution. It displays remarkable conformational flexibility upon macromolecular interactions, and can associate with mitochondrial membranes. Site-directed spin-labeling in combination with electron paramagnetic resonance spectroscopy enabled us to study the local binding properties of αS on artificial membranes (mimicking the inner and outer mitochondrial membranes), and to evaluate the importance of cardiolipin in this interaction. With pulsed, twofrequency, double-electron electron paramagnetic resonance (DEER) approaches, we examined, to the best of our knowledge for the first time, the conformation of αS bound to isolated mitochondria.

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540 Chemie

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alpha-synuclein; DEER; helical structures; membranes; mitochondria; site-directed spin labeling

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ISO 690ROBOTTA, Marta, Hanne R. GERDING, Antonia VOGEL, Karin HAUSER, Stefan SCHILDKNECHT, Christiaan KARREMAN, Marcel LEIST, Vinod SUBRAMANIAM, Malte DRESCHER, 2014. Alpha-Synuclein Binds to the Inner Membrane of Mitochondria in an α-Helical Conformation. In: ChemBioChem. 2014, 15(17), pp. 2499-2502. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201402281
BibTex
@article{Robotta2014Alpha-29387,
  year={2014},
  doi={10.1002/cbic.201402281},
  title={Alpha-Synuclein Binds to the Inner Membrane of Mitochondria in an α-Helical Conformation},
  number={17},
  volume={15},
  issn={1439-4227},
  journal={ChemBioChem},
  pages={2499--2502},
  author={Robotta, Marta and Gerding, Hanne R. and Vogel, Antonia and Hauser, Karin and Schildknecht, Stefan and Karreman, Christiaan and Leist, Marcel and Subramaniam, Vinod and Drescher, Malte}
}
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