[摘要]：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 interactions: PrP-peptides HPP01, 02, 03, 06, 11 physically interact with PrPSc of L-type atypical and classical BSEs, and scrapie by pull down (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
