Alzheimer's Disease (AD) is a complex multifactorial neurodegenerative disease in which many genetic and environmental factors are involved. The aggregation of the amyloid-� peptide (A�), possibly promoted by metal ions, to form amyloid plaques has been considered to be a central process and a relatively early event in the cascade leading to AD. Reactive oxygen species (ROS) and free radicals formed during aggregation appear to play a role in neuronal toxicity. To improve our understanding of amyloid peptide dynamics and the aggregation process, we synthesized a probe constituted of a benzothiazole derivative as the recognition moiety for A� -peptide and a ESR-active nitroxyl radical moiety as �spin label�. This probe will supply information regarding environmental changes during binding to fibrils, and is expected to allow us to monitor the aggregation process and identify the area of interaction between the benzothiazole moiety and the A� peptide.

Synthesis of nitroxyl radical TEMPO for ESR studies of amyloid-beta aggregation linked to Alzheimer's disease

245th National Meeting (2013)

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