Abstract
Prion diseases share a common feature in that the normal cellular prion protein (PrP(C)) converts to a protease-resistant isoform PrP(C). The α-helix-rich C-terminal half of PrP(C) is partly converted into β-sheet in PrP(Sc). We have examined by Raman spectroscopy the structure of an octapeptide PHGGGWGQ that appears in the N-terminal region of PrP(C) and a longer peptide containing the octapeptide region. The peptides do not assume any regular structure without divalent metal ions, whereas Cu(II) binding to the HGGG segment induces formation of α-helical structure on the C-terminal side of the peptide chain. The N-terminal octapeptide of prion protein may be a novel structural motif that acts as a promoter of α-helix formation.
Original language | English |
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Pages (from-to) | 248-252 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 396 |
Issue number | 2-3 |
DOIs | |
Publication status | Published - 1996 Nov 4 |
Externally published | Yes |
Keywords
- Metal coordination
- Prion protein
- Raman spectroscopy
- Secondary structure
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology