Single molecule study of initial structural features on the amyloidosis process

Abstract

We employed an α-hemolysin (α-HL) nanopore as a single-molecule tool to investigate the effects of initial structure on the amyloidosis process. The differences in the initial structure of two β-amyloid (Aβ) peptides (Aβ25-35 and Aβ35-25) could be distinguished in real-time due to their characteristic blockades. More importantly, the distinct aggregate dynamics for these two kinds of Aβ fragments can be readily analyzed by monitoring the blockade frequency over time.