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The A beta peptide forms non-amyloid fibrils in the presence of carbon nanotubes
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2014 (English)In: Nanoscale, ISSN 2040-3364, Vol. 6, no 12, 6720-6726 p.Article in journal (Refereed) Published
Abstract [en]

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 (A beta) peptide. The aggregation of the A beta 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 A beta peptides to form a new class of beta-sheet-rich yet non-amyloid fibrils.

Place, publisher, year, edition, pages
2014. Vol. 6, no 12, 6720-6726 p.
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Biochemistry and Molecular Biology
URN: urn:nbn:se:su:diva-105946DOI: 10.1039/c4nr00291aISI: 000337143900060OAI: diva2:733156


Available from: 2014-07-08 Created: 2014-07-08 Last updated: 2014-07-08Bibliographically approved

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Wärmlander, Sebastian K. T. S.Gräslund, Astrid
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