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Preparation of Stable Amyloid-β Oligomers Without Perturbative Methods

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Peptide Self-Assembly

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1777))

Abstract

Soluble amyloid-β (Aβ) oligomers have become a focal point in the study of Alzheimer’s disease due to their ability to elicit cytotoxicity. A number of recent studies have concentrated on the structural characterization of soluble Aβ oligomers to gain insight into their mechanism of toxicity. Consequently, providing reproducible protocols for the preparation of such oligomers is of utmost importance. The method presented in this chapter details a protocol for preparing an Aβ oligomer, with a primarily disordered secondary structure, without the need for chemical modification or amino acid substitution. Due to the stability of these disordered Aβ oligomers and the reproducibility with which they form, they are amenable for biophysical and high-resolution structural characterization.

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Acknowledgments

Research on amyloid-beta is supported by funds from the National Institutes of Health (AG048934 to A.R.).

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Correspondence to Ayyalusamy Ramamoorthy .

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Kotler, S.A., Ramamoorthy, A. (2018). Preparation of Stable Amyloid-β Oligomers Without Perturbative Methods. In: Nilsson, B., Doran, T. (eds) Peptide Self-Assembly. Methods in Molecular Biology, vol 1777. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7811-3_21

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  • DOI: https://doi.org/10.1007/978-1-4939-7811-3_21

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-7809-0

  • Online ISBN: 978-1-4939-7811-3

  • eBook Packages: Springer Protocols

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