The Aggregation Potential of the 1-15-and 1-16-Fragments of the Amyloid beta Peptide and Their Influence on the Aggregation of A beta 40

Autor: T. Plug, Martina Huber, J. C. M. Meijers, Nico J. Meeuwenoord, Dmitri V. Filippov, M. M. Motazacker, Maryam Hashemi Shabestari
Přispěvatelé: Amsterdam Cardiovascular Sciences, Vascular Medicine, Graduate School, Human Genetics, Experimental Vascular Medicine
Jazyk: angličtina
Rok vydání: 2013
Předmět:
Zdroj: Applied magnetic resonance, 44(10), 1167-1179. Springer Wien
ISSN: 0937-9347
Popis: 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
Databáze: OpenAIRE
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