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

Abstract

We have employed glass nanopore as a single molecule technique for direct sensing amyloidosis process of Aβ1–42 peptide, which of great significance in Alzheimer's disease.

Single-molecule studies of amyloid proteins: from biophysical properties to diagnostic perspectives

“…Yu et al . (2019) applied the glass nanopore to study the dynamic amyloidosis process of A β 42 peptides. In addition to A β peptides, Zhao’s group identified four types of α -syn oligomers as intermediates during the aggregation process and found the aggregation rate of α -syn has been dramatically accelerated by the presence of negatively charged lipids (Hu et al ., 2016).…”

“…Due to the robustness of these solidstate nanopores over a period of 24 h, tracking the development of protein aggregation over a longer time period becomes possible (Martyushenko et al, 2015). Yu et al (2019) applied the glass nanopore to study the dynamic amyloidosis process of Aβ42 peptides. In addition to Aβ peptides, Zhao's group identified four types of α-syn oligomers as intermediates during the aggregation process and found the aggregation rate of α-syn has been dramatically accelerated by the presence of negatively charged lipids .…”

Dynamic interaction of fluoroquinolones with magnesium ions monitored using bacterial outer membrane nanopores

“…A nanopore provides a connement effect to amplify the amperometric response of single molecules. 31,32 Outer membrane nanopores achieved already dened inter-molecular competition of different antimicrobial agents inside the pore lumen. 33 To this end, one can titrate antibiotic molecules on one side and the subsequent permeation of individual antibiotic molecules into the channel constriction transiently interrupts the ionic current.…”

Single-molecule nanopore sensing of actin dynamics and drug binding

“…20 Both biological and solid-state nanopores have been used to study protein folding at the single-molecule level, revealing the conformational change and dynamics during protein unfolding, [21][22][23][24] and have also been used to observe macromolecular changes of proteins. 25,26 Quartz nanopipettes, a sub-class of solid-state nanopores, are low-cost and straightforward to fabricate, circumventing the technical barrier of using conventional and expensive solid-state nanopores or biological nanopores.…”