Abstract
Alzheimer’s disease (AD) is a progressive neurodegenerative disease affecting cognitive and memory abilities and is believed to be linked to the formation and accumulation of neurotoxic aggregates of the Amyloid-β peptide (Aβ). In particular, it is the formation of soluble pre-fibrillar oligomers within the early stage of Aβ aggregation which is thought to represent a key step in the development of AD, thus underlining the interest in characterizing the aggregation process and the nature of these aggregates. In this context, fluorescence correlation spectroscopy (FCS) has emerged as a valuable alternative for the study of these systems in solution. Indeed, the use of FCS to study terminally labelled Aβ provides a means to detect changes in the size and concentration of initially monomeric Aβ samples by monitoring these fluorescently labelled species freely diffusing in solution with single-molecule resolution. Herein, we show how to employ FCS to study the early aggregation process of Aβ(1–42) and how this can be used to estimate the critical concentration for oligomer formation and to characterize the aggregates formed.
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Acknowledgments
We thank the Ministerio de Ciencia e Innovacion, the Ministerio de Economia y Competitividad, and the Xunta de Galicia for their financial support (CTQ2010-21369, CTQ2014-59020-R, GPC2013-052, R2014/051, ED431B 2016/024, ED431D R2016/007, ED431B 2019/18). S.F. thanks the Xunta de Galicia for her research scholarship.
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Novo, M., Pérez-González, C., Freire, S., Al-Soufi, W. (2023). Early Aggregation of Amyloid-β(1–42) Studied by Fluorescence Correlation Spectroscopy. 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_1
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DOI: https://doi.org/10.1007/978-1-0716-2597-2_1
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