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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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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cited_by cdi_FETCH-LOGICAL-c447t-4c593b52db0f3b407a5a678a248684b571e2563e0b3621e617be9bfdb68442893
cites cdi_FETCH-LOGICAL-c447t-4c593b52db0f3b407a5a678a248684b571e2563e0b3621e617be9bfdb68442893
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container_issue 46
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container_title Chemical science (Cambridge)
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creator Yu, Ru-Jia
Lu, Si-Min
Xu, Su-Wen
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Long, Yi-Tao
description 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.
doi_str_mv 10.1039/c9sc03260f
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subjects Agglomeration
Chemistry
Glass
Neurotoxicity
Oligomerization
Peptides
Porosity
Solid surfaces
Surface charge
Variations
title Single molecule sensing of amyloid-β aggregation by confined glass nanopores
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