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

A. Vandersteen, E. Hubin, R. Sarroukh, G. de Baets, J. Schymkowitz, F. Rousseau, Vinod Subramaniam, V. Raussens, H. Wenschuh, D. Wildemann, Kerensa Broersen

Research output: Contribution to journalArticleAcademicpeer-review

46 Citations (Scopus)

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)4088-4093
JournalFEBS letters
Volume586
Issue number23
DOIs
Publication statusPublished - 24 Oct 2012

Keywords

  • IR-81969
  • METIS-288676

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