Locally resolved membrane binding affinity of the N-terminus of α-synuclein

Marta Robotta, Christian Hintze, Stefan Schildknecht, Niels Zijlstra, Christian Jüngst, Christiaan Karreman, Martina Huber, Marcel Leist, Vinod Subramaniam, Malte Drescher

    Research output: Contribution to JournalArticleAcademicpeer-review


    α-Synuclein is abundantly present in Lewy bodies, characteristic of Parkinson's disease. Its exact physiological role has yet to be determined, but mitochondrial membrane binding is suspected to be a key aspect of its function. Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling allowed for a locally resolved analysis of the protein-membrane binding affinity for artificial phospholipid membranes, supported by a study of binding to isolated mitochondria. The data reveal that the binding affinity of the N-terminus is nonuniform.

    Original languageEnglish
    Pages (from-to)3960-2
    Number of pages3
    Issue number19
    Publication statusPublished - 2012


    • Cell Membrane
    • Electron Spin Resonance Spectroscopy
    • Humans
    • Lewy Bodies
    • Membranes, Artificial
    • Mutation
    • Phosphatidylcholines
    • Phosphatidylglycerols
    • Phospholipids
    • alpha-Synuclein
    • Journal Article
    • Research Support, Non-U.S. Gov't


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