Alzheimer’s disease is one of the leading causes of death in the US. This disease has been consistently associated with misfolding and aggregation of the amyloid-b (Ab) peptide in neurons. Ab is a mostly unstructured peptide of 39 to 42 amino acids in length, which can form soluble amyloid monomer and oligomers, and insoluble fibrils aggregates. We recently reported the use of [Ru(bpy)2(dpqp)]2+ (bpy = 2,2’-bipyridine; dpqp=pyrazino[2',3':5,6]pyrazino[2,3-f][1,10]phenanthroline) to detect the formation of Ab oligomers in real-time. This metal complex was also found to change its photoluminescence lifetime in response to the aggregation state of Ab. [Ru(bpy)2(dpqp)]2+ possesses a different lifetime when free in solution or bound to Ab fibrils. The deconvolution of these lifetimes from the time-decay curve allows determining the amount of the complex bound to fibrils. Using biophysics techniques we determined the binding stoichiometry, dissociation constant, and unambiguously monitored the formation of Ab fibrils. The use of lifetime present an interesting prospect for studying Ab aggregation in a variety of environments.

Photoluminescence lifetime for the detection of amyloid-beta aggregates

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.