Abstract
The aggregation of amyloid beta (A beta) peptide is important in Alzheimer's disease. Shorter A beta fragments may reduce A beta's cytotoxicity and are used in diagnostics. The aggregation of A beta 16 is controversial; Liu et al. (J. Neurosci. Res. 75:162-171, 2004) and Liao et al. (FEBS Lett. 581:1161-1165, 2007) find that A beta 16 does not aggregate and reduces A beta's cytotoxicity, Du et al. (J. Alzheimer's Dis. 27:401-413, 2011) reports that A beta 16 aggregates and that A beta 16 oligomers are toxic to cells. Here the aggregation potential of two shorter fragments, A beta 15 and A beta 16, and their influence on A beta 40 is measured by electron paramagnetic resonance (EPR) spectroscopy and the ThioT fluorescence assay (ThioT). Continuous-wave, 9 GHz EPR measurements and ThioT results reveal that neither A beta 15 nor A beta 16 aggregate by themselves and that they do not affect A beta 40 aggregation
Original language | English |
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Pages (from-to) | 1167-1179 |
Journal | Applied Magnetic Resonance |
Volume | 44 |
Issue number | 10 |
DOIs | |
Publication status | Published - 2013 |