Abstract
Oligomeric amyloid-beta (Aβ) peptides are considered as the most toxic species in Alzheimer's disease (AD). Monitoring of the Aβ aggregation profiles is critical for elucidating the oligomer toxicity and may serve as a therapeutic target for AD. By immobilizing the capture antibodies of A11 and OC that are specific to the oligomers and fibrils, respectively, in separate fluidic channels, a novel surface plasmon resonance (SPR) biosensor was designed for monitoring the oligomeric and fibrillar species of Aβ(1-42) simultaneously. The influence of curcumin, Cu(2+) and methylene blue on the amount of toxic oligomers and fibrils was evaluated. The half maximal inhibitory concentration (IC50) of curcumin and methylene blue was determined. The formation of Aβ fibrils was also validated by the thioflavin T (ThT) fluorescence assay. The results demonstrate the utility of SPR as an analytical tool for rapid and comprehensive monitoring of Aβ aggregation and screening of Aβ modulators.
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