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Updated: Nov 4, 2025
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Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
Published on: June 2, 2019
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Electron Microscopic Analysis of α-Synuclein Fibrils
Airi Tarutani1,2, Masato Hasegawa3
1Department of Brain and Neurosciences, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Methods in Molecular Biology (Clifton, N.J.)
|May 27, 2021
Summary
Alpha-synuclein (α-syn) forms insoluble fibrils in neurodegenerative diseases like Parkinson's. This study details methods to characterize these pathological α-syn fibrils using electron microscopy.
Area of Science:
- Neuroscience
- Biochemistry
- Structural Biology
Background:
- Alpha-synuclein (α-syn) aggregates into amyloid fibrils in synucleinopathies, such as Parkinson's disease and multiple system atrophy (MSA).
- These insoluble α-syn fibrils exhibit prion-like properties and their accumulation correlates with disease progression.
- Atomic-level structures of both synthetic and patient-derived α-syn fibrils have been recently elucidated.
Purpose of the Study:
- To describe protocols for the ultrastructural characterization of α-syn fibrils.
- To enable detailed analysis of both synthetic and pathological α-syn aggregates.
Main Methods:
- Negative staining electron microscopy.
- Immunoelectron microscopy.
- Cryo-electron microscopy for structural determination.
Main Results:
- Established protocols for visualizing α-syn fibril ultrastructure.
- Enabled comparison between synthetic and pathological fibril structures.
- Provided detailed insights into the atomic-level architecture of α-syn fibrils.
Conclusions:
- Negative staining and immunoelectron microscopy are crucial for characterizing α-syn fibril morphology.
- These methods facilitate the study of α-syn aggregation in neurodegenerative diseases.
- Understanding fibril structure aids in developing therapeutic strategies for synucleinopathies.
Keywords:
Amyloid-like fibrilsDementia with Lewy bodiesImmunoelectron microscopyMultiple system atrophyNegative stainingParkinson’s diseaseα-SynucleinMore Related Videos
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