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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Royal Society of Chemistry
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7020925/ https://www.ncbi.nlm.nih.gov/pubmed/32153747 http://dx.doi.org/10.1039/c9sc03260f |
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author | Yu, Ru-Jia Lu, Si-Min Xu, Su-Wen Li, Yuan-Jie Xu, Qun Ying, Yi-Lun Long, Yi-Tao |
author_facet | Yu, Ru-Jia Lu, Si-Min Xu, Su-Wen Li, Yuan-Jie Xu, Qun Ying, Yi-Lun Long, Yi-Tao |
author_sort | Yu, Ru-Jia |
collection | PubMed |
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. |
format | Online Article Text |
id | pubmed-7020925 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-70209252020-03-09 Single molecule sensing of amyloid-β aggregation by confined glass nanopores Yu, Ru-Jia Lu, Si-Min Xu, Su-Wen Li, Yuan-Jie Xu, Qun Ying, Yi-Lun Long, Yi-Tao Chem Sci Chemistry 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. Royal Society of Chemistry 2019-10-08 /pmc/articles/PMC7020925/ /pubmed/32153747 http://dx.doi.org/10.1039/c9sc03260f Text en This journal is © The Royal Society of Chemistry 2019 http://creativecommons.org/licenses/by-nc/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution Non Commercial 3.0 Unported Licence (CC BY-NC 3.0) |
spellingShingle | Chemistry Yu, Ru-Jia Lu, Si-Min Xu, Su-Wen Li, Yuan-Jie Xu, Qun Ying, Yi-Lun Long, Yi-Tao Single molecule sensing of amyloid-β aggregation by confined glass nanopores |
title | Single molecule sensing of amyloid-β aggregation by confined glass nanopores
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title_full | Single molecule sensing of amyloid-β aggregation by confined glass nanopores
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title_fullStr | Single molecule sensing of amyloid-β aggregation by confined glass nanopores
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title_full_unstemmed | Single molecule sensing of amyloid-β aggregation by confined glass nanopores
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title_short | Single molecule sensing of amyloid-β aggregation by confined glass nanopores
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title_sort | single molecule sensing of amyloid-β aggregation by confined glass nanopores |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7020925/ https://www.ncbi.nlm.nih.gov/pubmed/32153747 http://dx.doi.org/10.1039/c9sc03260f |
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