Investigation of the Dissociation Mechanism of Single-Walled Carbon Nanotube on Mature Amyloid-β Fibrils at Single Nanotube Level.

Amyloid fibrils originating from the fibrillogenesis of misfolded amyloid proteins are associated with the pathogenesis of many neurodegenerative diseases, such as Alzheimer's, Parkinson's, and Huntington's diseases. Carbon nanotubes have been extensively applied in our life and industry due to their unique chemical and physical properties. Nonetheless, the details between carbon nanotubes and mature amyloid fibrils remain elusive. In this study, we explored the interplay between single-walled carbon nanotubes (SWCNTs) and preformed amyloid-β (Aβ) fibrils by atomic force microscopy at the single SWCNT level, together with ThT fluorescence, cellular viability assays, infrared spectroscopy, and molecular dynamics (MD) simulations. The results demonstrated that SWCNTs could partially destroy the preformed Aβ fibrils and form the Aβ-surrounded-SWCNTs conjugates, as well as reduce the β-sheet structures. Peak force quantitative nanomechanical measurements revealed that the conjugates have lower Young's modulus than fibrils. Furthermore, our MD simulation demonstrated that the dissociation ability was dependent on the binding sites of Aβ fibrils. Overall, this study provides an insight into the dissociation mechanism between SWCNT and Aβ fibrils, which could be beneficial for the study of bionanomaterials and the development of other potential drug candidates for amyloidosis.