Novel assay with fluorescence-labelled PrP peptides for differentiating L-type atypical and classical BSEs, and scrapie.

Characteristic differences of prions may account for the conformational diversity of the pathogenic isoform of prion protein (PrP(Sc)). Here, we applied a protein detection procedure by using fluorescent-labelled peptides for detecting PrP(Sc). Five prion protein (PrP) related peptides were found to change significantly their fluorescent intensities with prion-affected animal samples. Their reactivity was different among atypical L-BSE, classical BSE and scrapie. The pull-down assay revealed that they precipitated PrP(Sc) specifically. These findings suggest that fluorescent intensity changes depend on peptide-PrP(Sc) binding. This novel approach may distinguish the fine structural differences in PrP(Sc), which were not detected by the pull-down assay.