Antiparallel arrangement of the helices of vesicle-bound alpha-synuclein

Malte Drescher, Gertjan Veldhuis, Bart D van Rooijen, Sergey Milikisyants, Vinod Subramaniam, Martina Huber

    Research output: Contribution to JournalArticleAcademicpeer-review


    alpha-Synuclein (alphaS) is the main component of Lewy bodies from Parkinson's disease. That alphaS binds to membranes is known, but the conformation it adopts is still unclear. Pulsed EPR on doubly spin-labeled variants of alphaS sheds light on the most likely structure. For alphaS bound to vesicles large enough to accommodate also the extended conformation, an antiparallel helix conformation is found. This suggests that the bent structure shown is the preferred conformation of alphaS on membranes.

    Original languageEnglish
    Pages (from-to)7796-7
    Number of pages2
    JournalJournal of the American Chemical Society
    Issue number25
    Publication statusPublished - 25 Jun 2008


    • Magnetic Resonance Spectroscopy
    • Models, Molecular
    • Protein Binding
    • Protein Structure, Secondary
    • Transport Vesicles
    • alpha-Synuclein
    • Journal Article
    • Research Support, Non-U.S. Gov't


    Dive into the research topics of 'Antiparallel arrangement of the helices of vesicle-bound alpha-synuclein'. Together they form a unique fingerprint.

    Cite this