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The A beta peptide ...
The A beta peptide forms non-amyloid fibrils in the presence of carbon nanotubes
- Article/chapterEnglish2014
Publisher, publication year, extent ...
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2014
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Royal Society of Chemistry (RSC),2014
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printrdacarrier
Numbers
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LIBRIS-ID:oai:DiVA.org:su-105946
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https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-105946URI
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https://doi.org/10.1039/c4nr00291aDOI
Supplementary language notes
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Language:English
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Summary in:English
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Classification
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
Notes
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AuthorCount:6;
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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.
Subject headings and genre
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Wärmlander, Sebastian K. T. S.Stockholms universitet,Institutionen för biokemi och biofysik(Swepub:su)seb
(author)
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Yu, Chien-Hung
(author)
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Muhammad, Kamran
(author)
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Gräslund, AstridStockholms universitet,Institutionen för biokemi och biofysik(Swepub:su)astrid
(author)
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Abrahams, Jan Pieter
(author)
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Stockholms universitetInstitutionen för biokemi och biofysik
(creator_code:org_t)
Related titles
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In:Nanoscale: Royal Society of Chemistry (RSC)6:12, s. 6720-67262040-33642040-3372
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