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

作者：Vandersteen Annelies; Hubin Ellen; Sarroukh Rabia; De Baets Greet; Schymkowitz Joost; Rousseau Frederic; Subramaniam Vinod; Raussens Vincent; Wenschuh Holger; Wildemann Dirk; Broersen Kerensa^*

来源：FEBS LETTERS, 2012, 586(23): 4088-4093.

DOI：10.1016/j.febslet.2012.10.022

• Thioflavin T fluorescence
• Alzheimer%26apos
• s disease
• FAD mutation
• Biotinylation
• p3 Peptide
• Biophysics

Aggregated forms of the amyloid-beta peptide are hypothesized to act as the prime toxic agents in Alzheimer disease (AD). The in vivo amyloid-beta 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-beta 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-beta peptides.

• 出版日期2012-11-30