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Preparation and Investigation of Crucial Oligomers in the Early Stages of Aβ40 and Aβ42 Aggregation

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Protein Aggregation

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2551))

Abstract

Amyloid aggregation is a hallmark in many neuropathologies and other diseases of tremendous impact. It is increasingly evident that neuronal death associated with Alzheimer’s disease (AD) is mainly produced by oligomers of the amyloid-β (Aβ) peptide. Yet little is known about the detailed structural and biophysical mechanisms of their formation. This lack of complete understanding comes from the labile nature and handling complexity of the oligomers. Consequently, providing reproducible and robust protocols for oligomer preparation is of particular importance.

In this study, we describe detailed methods for the preparation and isolation of micellar oligomers of Aβ that evolve towards larger and more stable oligomers enriched in beta-sheet structure and able to acquire a higher capacity to fibrillate. We also describe briefly some biophysical experiments allowing oligomer characterization.

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Acknowledgments

Research on amyloid beta was funded by Grant BIO2013-40697-R from the Spanish Ministry of Economy and Competitiveness and by the European Regional Development Fund of the European Union.

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Correspondence to Bertrand Morel or Francisco Conejero-Lara .

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Morel, B., Conejero-Lara, F. (2023). Preparation and Investigation of Crucial Oligomers in the Early Stages of Aβ40 and Aβ42 Aggregation. In: Cieplak, A.S. (eds) Protein Aggregation. Methods in Molecular Biology, vol 2551. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2597-2_2

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  • DOI: https://doi.org/10.1007/978-1-0716-2597-2_2

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-2596-5

  • Online ISBN: 978-1-0716-2597-2

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