A comparative analysis of the aggregation behavior of amyloid-β peptide variants

Annelies Vandersteen, Ellen Hubin, Rabia Sarroukh, Greet De Baets, Joost Schymkowitz, Frederic Rousseau, Vinod Subramaniam, Vincent Raussens, Holger Wenschuh, Dirk Wildemann, Kerensa Broersen

    Research output: Contribution to JournalArticleAcademicpeer-review

    Abstract

    Aggregated forms of the amyloid-β peptide are hypothesized to act as the prime toxic agents in Alzheimer disease (AD). The in vivo amyloid-β peptide pool consists of both C- and N-terminally truncated or mutated peptides, and the composition thereof significantly determines AD risk. Other variations, such as biotinylation, are introduced as molecular tools to aid the understanding of disease mechanisms. Since these modifications have the potential to alter key aggregation properties of the amyloid-β peptide, we present a comparative study of the aggregation of a substantial set of the most common in vivo identified and in vitro produced amyloid-β peptides.

    Original languageEnglish
    Pages (from-to)4088-93
    Number of pages6
    JournalFEBS Letters
    Volume586
    Issue number23
    DOIs
    Publication statusPublished - 30 Nov 2012

    Keywords

    • Amyloid beta-Peptides
    • Biotinylation
    • Microscopy, Electron, Transmission
    • Spectroscopy, Fourier Transform Infrared
    • Journal Article
    • Research Support, Non-U.S. Gov't

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  • Cite this

    Vandersteen, A., Hubin, E., Sarroukh, R., De Baets, G., Schymkowitz, J., Rousseau, F., ... Broersen, K. (2012). A comparative analysis of the aggregation behavior of amyloid-β peptide variants. FEBS Letters, 586(23), 4088-93. https://doi.org/10.1016/j.febslet.2012.10.022