Dual-probe fluorescence spectroscopy for sensitive quantitation of Alzheimer's amyloid pathology.

ABSTRACT: Protein misfolding is a prominent pathological hallmark of neurodegenerative disorders, including Alzheimer's disease (AD). Studies have shown that the diversity of β sheet-rich protein deposits (such as amyloid β plaques and neurofibrillary tangles), present across different brain regions, might underlie different disease phenotypes and only certain types of aggregates might be associated with cognitive decline. Conformationally sensitive fluorescent amyloid probes have the ability to report different structures of protein aggregates by virtue of their shifting emission spectra. Here we defined the binding affinity of the fluorescent amyloid probes BSB and MCAAD to disease-relevant protein aggregates, and combined the two probes to examine formalin-fixed paraffin-embedded mouse and human

SUBMITTER: Stepanchuk AA 

PROVIDER: S-EPMC9615372 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature