[HTML][HTML] Inhibition of interactions and interconversions of prion protein isoforms by peptide fragments from the C-terminal folded domain

M Horiuchi, GS Baron, LW Xiong, B Caughey - Journal of Biological …, 2001 - ASBMB
The formation of protease-resistant prion protein (PrP-res or PrP Sc) involves selective
interactions between PrP-res and its normal protease-sensitive counterpart, PrP-sen or PrP
C. Previous studies have shown that synthetic peptide fragments of the PrP sequence
corresponding to residues 119–136 of hamster PrP (Ha119–136) can selectively block PrP-
res formation in cell-free systems and scrapie-infected tissue culture cells. Here we show
that two other peptides corresponding to residues 166–179 (Ha166–179) and 200–223 …