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

Vandersteen, A. and Hubin, E. and Sarroukh, R. and Baets, G. and Schymkowitz, J. and Rousseau, F. and Subramaniam, V. and Raussens, V. and Wenschuh, H. and Wildemann, D. and Broersen, K. (2012) A comparative analysis of the aggregation behavior of amyloid-beta peptide variants. FEBS letters, 586 . 4088 - 4093. ISSN 0014-5793

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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
Item Type:	Article
Copyright:	© Elsevier
Faculty:	Science and Technology (TNW)
Research Group:	Nano-Biophysics (NBP)
Link to this item:	http://purl.utwente.nl/publications/81969
Official URL:	http://dx.doi.org/10.1016/j.febslet.2012.10.022
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