Unknown

Dataset Information

0

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


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.

SUBMITTER: Yu RJ 

PROVIDER: S-EPMC7020925 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Yu Ru-Jia RJ   Lu Si-Min SM   Xu Su-Wen SW   Li Yuan-Jie YJ   Xu Qun Q   Ying Yi-Lun YL   Long Yi-Tao YT  

Chemical science 20191008 46


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  ...[more]

Similar Datasets

| S-EPMC9036133 | biostudies-literature
| S-EPMC9014393 | biostudies-literature
| S-EPMC10214486 | biostudies-literature
| S-EPMC4543996 | biostudies-literature
| S-EPMC6820719 | biostudies-literature
| S-EPMC8944908 | biostudies-literature
| S-EPMC5662926 | biostudies-literature
| S-EPMC3073859 | biostudies-literature
| S-EPMC8336786 | biostudies-literature
| S-EPMC11492064 | biostudies-literature