(381f) Design of a Peptide Probe for Rapid and Specific Detection of Amyloid Oligomers

Determination of population profiles of different aggregate species is strongly required to understand the molecular causes of beta-amyloid (Abeta) aggregation as well as toxic processes in Alzheimer's disease (AD). A quantitative measurement of aggregate species must be done rapidly in situ for high level accuracy, as aggregates including soluble oligomers are likely to undergo further structural changes during the additional sample preparation and incubation steps. Here, we repot development of peptide probes for rapid in situ amyloid detection. Our peptide probes generated novel fluorescence signals upon coincubation with Abeta oligomers, but not monomeric/dimeric species. Our results suggested that the generation of novel fluorescence signals is due to the conformational change of peptide probes. The detection could occur within an hour without any additional sample incubation steps. We believe that our molecular probe can serve as an elegant molecular tool to enhance our understanding of the molecular causes of Abeta aggregation and their relevance to toxic effects in AD through rapid in situ determination of aggregation profiles.