Abstract
α-Synuclein (α-syn) is a major component of abnormal protein deposits observed in the brains of patients with synucleinopathies, including Parkinson’s disease, dementia with Lewy bodies, and multiple system atrophy (MSA). The synaptic protein α-syn is water-soluble under normal physiological conditions, but in these patients’ brains, we see accumulation of insoluble amyloid-like α-syn fibrils with prion-like properties. Intracerebral accumulation of these fibrils is correlated with disease onset and progression. Recombinant α-syn protein also forms amyloid-like fibrils that are structurally akin to those extracted from patients’ brains. Recent cryo-electron microscopic studies have identified the core structures of synthetic α-syn fibrils and α-syn fibrils extracted from the brains of patients with MSA at the atomic level. In this chapter, we describe negative staining and immunoelectron microscopy protocols for ultrastructural characterization of synthetic α-syn fibrils and pathological α-syn fibrils.
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Tarutani, A., Hasegawa, M. (2021). Electron Microscopic Analysis of α-Synuclein Fibrils. In: Imai, Y. (eds) Experimental Models of Parkinson’s Disease. Methods in Molecular Biology, vol 2322. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-1495-2_2
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DOI: https://doi.org/10.1007/978-1-0716-1495-2_2
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