Metal‐dependent α‐helix formation promoted by the glycine‐rich octapeptide region of prion protein
- 4 November 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 396 (2-3) , 248-252
- https://doi.org/10.1016/0014-5793(96)01104-0
Abstract
Prion diseases share a common feature in that the normal cellular prion protein (PrPC) converts to a proteaseresistant isoform PrPSc. The α-helix-rich C-terminal half of PrPC is partly converted into β-sheet in PrPSc. We have examined by Raman spectroscopy the structure of an octapeptide PHGGGWGQ that appears in the N-terminal region of PrPC 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.Keywords
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