Alpha-Synuclein Disease Mutations Are Structurally Defective and Locally Affect Membrane Binding

Marta Robotta, Julia Cattani, Juliana Cristina Martins, Vinod Subramaniam, Malte Drescher

    Research output: Contribution to JournalArticle


    The intrinsically disordered human protein alpha-Synuclein (αS) has a prominent role in Parkinson's disease (PD) pathology. Several familial variants of αS are correlated with inherited PD. Disease mutations have been shown to have an impact on lipid membrane binding. Here, using electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling, we show that familial PD-associated variants are structurally defective in membrane binding and alter the local binding properties of the protein.

    Original languageEnglish
    Pages (from-to)4254-4257
    Number of pages4
    JournalJournal of the American Chemical Society
    Issue number12
    Publication statusE-pub ahead of print - 20 Mar 2017



    • Journal Article

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