Alpha-Synuclein Binds to the Inner Membrane of Mitochondria in an alpha-Helical Conformation
Publication year
2014Source
ChemBioChem, 15, 17, (2014), pp. 2499-502ISSN
Publication type
Article / Letter to editor
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Organization
Tumorimmunology
Journal title
ChemBioChem
Volume
vol. 15
Issue
iss. 17
Page start
p. 2499
Page end
p. 502
Subject
Radboudumc 2: Cancer development and immune defence RIMLS: Radboud Institute for Molecular Life SciencesAbstract
The human alpha-Synuclein (alphaS) 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 alphaS 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 alphaS bound to isolated mitochondria.
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- Faculty of Medical Sciences [93208]
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