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Updated: Aug 9, 2026

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
Published on: June 2, 2019
Study of the disassembly-assembly process of alpha-synuclein fibrils by in situ atomic force microscopy
Lin Tang1, Hong-Tao Li, Hai-Ning Du
1Shanghai Institute of Applied Physics, Chinese Academy of Sciences, 2019 Baojia Road, Shanghai 201800, China. tanglin@sinap.ac.cn
Abstract:
In this report, we applied in situ atomic force microscopy (AFM) to study the dynamic process of disassembly-assembly of alpha-synuclein (alpha-Syn) fibrils in different solutions. Most of the mica-adsorbed alpha-Syn fibrils disassemble into small particles step-by-step on the mica surface in diluted solutions, yet a few short fibrils still extend to form longer fibrils. This process usually started randomly at the center of the long fibrils, which progressively disassemble into short fragments and small protein particles of varying size. Compared to disassembly, assembly happened infrequently when the protein concentration was low. It was observed directly by AFM that the chaotropic agent guanidinium chloride rapidly breaks the long alpha-Syn fibrils.
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