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

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Abstract

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.

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

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Publication details

The article was received on 02 Jul 2019, accepted on 04 Oct 2019 and first published on 08 Oct 2019


Article type: Edge Article
DOI: 10.1039/C9SC03260F
Chem. Sci., 2019, Advance Article
  • Open access: Creative Commons BY-NC license
    All publication charges for this article have been paid for by the Royal Society of Chemistry

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

    R. Yu, S. Lu, S. Xu, Y. Li, Q. Xu, Y. Ying and Y. Long, Chem. Sci., 2019, Advance Article , DOI: 10.1039/C9SC03260F

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