KCS

Alzheimer’s disease(AD) is caused by amyloid aggregation in neuron. There have been tremendous efforts to explore a new efficient inhibitor for amyloid aggregates as a curing agent of AD. In this work, we have used fluorescence lifetime imaging microscopy (FLIM) for screening amyloid aggregation inhibitors. First, we designed a new FRET amyloid aggregation probe which consists of Alexa 488 for an energy donor, amyloid11-25 and azulene for an energy acceptor. The amyloid conformation probe exhibits different fluorescence lifetimes as in monomers and in micellar structures. The amyloid micellar structures were prepared on a cover glass and the probe lifetime distribution was mapped by FLIM. The inhibitor screening was accomplished by monitoring the FLIM images and bimodal fluorescence lifetime distributions. It appeared that our method is much more powerful than the conventional Th T binding assay.