Alpha-synuclein binds to the inner membrane of mitochondria in an a-helical conformation

Marta Robotta, Hanne R. Gerding, Antonia Vogel, Karin Hauser, Stefan Schildknecht, Christiaan Karreman, Marcel Leist, Vinod Subramaniam, Malte Drescher*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

73 Citations (Scopus)
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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.

Original languageEnglish
Pages (from-to)2499-2502
Number of pages4
Issue number17
Publication statusPublished - 24 Nov 2014


  • Alpha-synuclein
  • DEER
  • Helical structures
  • Membranes
  • Mitochondria
  • Site-directed spin labeling


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