Jump to main content
Jump to site search

Issue 12, 2014
Previous Article Next Article

The Aβ peptide forms non-amyloid fibrils in the presence of carbon nanotubes

Author affiliations

Abstract

Carbon nanotubes have specific properties that make them potentially useful in biomedicine and biotechnology. However, carbon nanotubes may themselves be toxic, making it imperative to understand how carbon nanotubes interact with biomolecules such as proteins. Here, we used NMR, CD, and ThT/fluorescence spectroscopy together with AFM imaging to study pH-dependent molecular interactions between single walled carbon nanotubes (SWNTs) and the amyloid-beta (Aβ) peptide. The aggregation of the Aβ peptide, first into oligomers and later into amyloid fibrils, is considered to be the toxic mechanism behind Alzheimer's disease. We found that SWNTs direct the Aβ peptides to form a new class of β-sheet-rich yet non-amyloid fibrils.

Graphical abstract: The Aβ peptide forms non-amyloid fibrils in the presence of carbon nanotubes

Back to tab navigation

Supplementary files

Publication details

The article was received on 16 Jan 2014, accepted on 11 Apr 2014 and first published on 13 May 2014


Article type: Paper
DOI: 10.1039/C4NR00291A
Author version available: Download Author version (PDF)
Citation: Nanoscale, 2014,6, 6720-6726
  •   Request permissions

    The Aβ peptide forms non-amyloid fibrils in the presence of carbon nanotubes

    J. Luo, S. K. T. S. Wärmländer, C. Yu, K. Muhammad, A. Gräslund and J. Pieter Abrahams, Nanoscale, 2014, 6, 6720
    DOI: 10.1039/C4NR00291A

Search articles by author

Spotlight

Advertisements