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

Jinghui Luo, Sebastian K.T.S. Wärmländer, Chien Hung Yu, Kamran Muhammad, Astrid Gräslund, Jan Pieter Abrahams

Research output: Contribution to journalArticle

26 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)6720-6726
Number of pages7
JournalNanoscale
Volume6
Issue number12
DOIs
Publication statusPublished - 2014 Jun 21

All Science Journal Classification (ASJC) codes

  • Materials Science(all)

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    Luo, J., Wärmländer, S. K. T. S., Yu, C. H., Muhammad, K., Gräslund, A., & Pieter Abrahams, J. (2014). The Aβ peptide forms non-amyloid fibrils in the presence of carbon nanotubes. Nanoscale, 6(12), 6720-6726. https://doi.org/10.1039/c4nr00291a