Room-temperature in-cell EPR spectroscopy: Alpha-Synuclein disease variants remain intrinsically disordered in the cell

Julia Cattani, Vinod Subramaniam, Malte Drescher*

*Corresponding author for this work

    Research output: Contribution to JournalArticleAcademicpeer-review


    Human alpha-Synuclein (aS), implicated in Parkinson's disease, adopts a rich variety of different conformations depending on the macromolecular context. In order to unravel its pathophysiological role, monitoring its intracellular conformational state and identifying differences for the disease variants is crucial. Here, we present an intracellular spectroscopy approach based on a systematic spin-labeling site-scan in combination with intracellular electron paramagnetic resonance spectroscopy determining conformations on a molecular scale. A quantitative and model-based data analysis revealed that the vast majority of aS, be it wild-type or disease variants A30P or A53T, exists in the monomeric intrinsically disordered form in the cell.

    Original languageEnglish
    Pages (from-to)18147-18151
    Number of pages5
    JournalPhysical Chemistry Chemical Physics
    Issue number28
    Publication statusPublished - 2017


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