Alzheimer's disease (AD), the most common cause of dementia, is characterized by the presence of senile plaques and neurofibrillary tangles, surrounded by damaged neurons. Beta-Amyloid (Aß) peptides, Aß40 (1-40) and Aß42 (1-42), were found to be a major component of the above plaques. Many studies suggest that these peptides can form toxic oligomers and fibrils under physiological conditions and rapidly aggregate. Since Aß aggregation is evidently an essential event in the pathogenesis of AD, a reliable assay is important to study Aß fibrillation kinetics and for screening Aß aggregation inhibitors.
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