Single molecule sensing of amyloid-β aggregation by confined glass nanopores

We have developed a glass nanopore based single molecule tool to investigate the dynamic oligomerization and aggregation process of Aβ1-42 peptides. The intrinsic differences in the molecular size and surface charge of amyloid aggregated states could be distinguished through single molecule induced...

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Bibliographic Details
Published in:Chemical science (Cambridge) 2019-12, Vol.10 (46), p.10728-10732
Main Authors: Yu, Ru-Jia, Lu, Si-Min, Xu, Su-Wen, Li, Yuan-Jie, Xu, Qun, Ying, Yi-Lun, Long, Yi-Tao
Format: Article
Language:English
Subjects:
Agglomeration
Chemistry
Glass
Neurotoxicity
Oligomerization
Peptides
Porosity
Solid surfaces
Surface charge
Variations
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Summary:We have developed a glass nanopore based single molecule tool to investigate the dynamic oligomerization and aggregation process of Aβ1-42 peptides. The intrinsic differences in the molecular size and surface charge of amyloid aggregated states could be distinguished through single molecule induced characteristic current fluctuation. More importantly, our results reveal that the neurotoxic Aβ1-42 oligomer tends to adsorb onto the solid surface of nanopores, which may explain its instability and highly neurotoxic features.
ISSN:2041-6520
2041-6539
DOI:10.1039/c9sc03260f