Study of the disassembly-assembly process of alpha-synuclein fibrils by in situ atomic force microscopy

Micron : the International Research and Review Journal for Microscopy
Lin TangHong-Yu Hu

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.

References

Dec 20, 1994·Proceedings of the National Academy of Sciences of the United States of America·M GutholdC Bustamante
Dec 1, 1993·Proceedings of the National Academy of Sciences of the United States of America·K UédaT Saitoh
Sep 13, 2000·Nucleic Acids Research·L S ShlyakhtenkoY L Lyubchenko

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Citations

May 1, 2008·Journal of Microscopy·S KunzeW Bodemer
Jan 31, 2008·Biochemical and Biophysical Research Communications·Feng ZhangHong-Yu Hu
Apr 30, 2016·The Journal of Biological Chemistry·Jing L GuoVirginia M Y Lee
Jan 14, 2022·Chemical Reviews·Ruiheng WuJonathan Rivnay

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