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 (PrPSc). Here, we applied a protein detection procedure by using fluorescent-labelled peptides for detecting PrPSc. 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 PrPSc specifically. These findings suggest that fluorescent intensity changes depend on peptide–PrPSc binding. This novel approach may distinguish the fine structural differences in PrPSc, which were not detected by the pull-down assay.Structured summary of protein interactionsPrP-peptides HPP01, 02, 03, 06, 11 physically interact with PrPSc of L-type atypical and classical BSEs, and scrapie by pull down

► Fluorescence-labelled peptides were used for detecting PrPSc.
► Five PrP peptides changed fluorescence intensities with prion-affected animal samples.
► Reactivity was different among atypical L-BSE, classical BSE and scrapie.
► These peptides bound to PrPSc specifically.
► This procedure may distinguish the fine structural differences in PrPSc.