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Single-Molecule FRET Detection of Early-Stage Conformations in α-Synuclein Aggregation

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Alpha-Synuclein

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1948))

Abstract

Misfolding and aggregation of α-synuclein are linked to many neurodegenerative disorders, including Parkinson’s and Alzheimer’s disease. Despite intense research efforts, detailed structural characterization of early conformational transitions that initiate and drive α-synuclein aggregation remains elusive often due to the low sensitivity and ensemble averaging of commonly used techniques. Single-molecule Förster resonance energy transfer (smFRET) provides unique advantages in detecting minor conformations that initiate protein pathologic aggregation. In this chapter, we describe an smFRET-based method for characterizing early conformational conversions that are responsible for α-synuclein self-assembly and aggregation.

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Acknowledgments

This work was supported by laboratory startup funds from the Baylor College of Medicine (A.C.M.F. and J.C.F.). The authors declare no competing financial interests.

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Authors and Affiliations

  1. Department of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, TX, USA

    Mahdi Muhammad Moosa, Josephine C. Ferreon & Allan Chris M. Ferreon

Authors
  1. Mahdi Muhammad Moosa
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  2. Josephine C. Ferreon
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  3. Allan Chris M. Ferreon
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Corresponding author

Correspondence to Allan Chris M. Ferreon .

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Editors and Affiliations

  1. Dementia Research Institute, University College London, London, UK

    Tim Bartels

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Moosa, M.M., Ferreon, J.C., Ferreon, A.C.M. (2019). Single-Molecule FRET Detection of Early-Stage Conformations in α-Synuclein Aggregation. In: Bartels, T. (eds) Alpha-Synuclein. Methods in Molecular Biology, vol 1948. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-9124-2_17

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  • DOI: https://doi.org/10.1007/978-1-4939-9124-2_17

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-9123-5

  • Online ISBN: 978-1-4939-9124-2

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