Abstract
In vitro time-resolved characterization of protein aggregation into amyloid fibers and the effects of other proteins on the aggregation process are fundamentally important measurements to obtain a better understanding of the mechanisms contributing to neurodegeneration, as well as other diseases involving amyloid formation. Here, we describe how to perform in vitro aggregation experiments with α-synuclein, the amyloidogenic protein involved in Parkinson’s disease, including how to assess the starting material, useful experimental/instrumental conditions, as well as how to set up cross-seeding and co-aggregation experiments. The high variability of data reported for in vitro α-synuclein amyloid formation may in part be explained by experimental differences.
Dedicated to the memory of Juris Kiskis.
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Acknowledgments
Support is acknowledged from the Knut and Alice Wallenberg foundation, the Swedish Research Council, the Chalmers Foundation, and the Olle Engkvist foundation.
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Horvath, I., Rocha, S., Wittung-Stafshede, P. (2018). In Vitro Analysis of α-Synuclein Amyloid Formation and Cross-Reactivity. In: Sigurdsson, E., Calero, M., Gasset, M. (eds) Amyloid Proteins. Methods in Molecular Biology, vol 1779. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7816-8_6
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DOI: https://doi.org/10.1007/978-1-4939-7816-8_6
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