title: A comparative analysis of the aggregation behavior of amyloid-β peptide variants.
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.
authors.affiliation: Nanobiophysics Group, MIRA Institute for Biomedical Technology and Technical Medicine, Faculty of Science and Technology, University of Twente, 7500 AE Enschede, The Netherlands.
authors.forename: Annelies
authors.initials: A
authors.lastname: Vandersteen
authors.forename: Ellen
authors.initials: E
authors.lastname: Hubin
authors.forename: Rabia
authors.initials: R
authors.lastname: Sarroukh
authors.forename: Greet
authors.initials: G
authors.lastname: De Baets
authors.forename: Joost
authors.initials: J
authors.lastname: Schymkowitz
authors.forename: Frederic
authors.initials: F
authors.lastname: Rousseau
authors.forename: Vinod
authors.initials: V
authors.lastname: Subramaniam
authors.forename: Vincent
authors.initials: V
authors.lastname: Raussens
authors.forename: Holger
authors.initials: H
authors.lastname: Wenschuh
authors.forename: Dirk
authors.initials: D
authors.lastname: Wildemann
authors.forename: Kerensa
authors.initials: K
authors.lastname: Broersen
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000648:ultrastructure; D019921:Biotinylation; D046529:Microscopy, Electron, Transmission; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D016229:Amyloid beta-Peptides