Publication:

Copper-binding to the n-terminal tandem repeat region of mammalian and avian prion protein - structural studies using synthetic peptides (1995)

Author(s): M. P. Hornshaw;J. R. Mcdermott;J. M. Candy;J. H. Lakey

  • : Copper-binding to the n-terminal tandem repeat region of mammalian and avian prion protein - structural studies using synthetic peptides

Abstract: Using CD spectroscopy we have investigated the effect of Cu2+ on the secondary structure of synthetic peptides Octa(4) and Hexa(4) corresponding to tetra-repeats of the octapeptide of mammalian PrP and the hexapeptide of chicken PrP. in addition, fluorescence spectroscopy was used to estimate the dissociation constants (Kd), of Cu2+ binding by both peptides. Both peptides exhibited unusual CD spectra, complicated by the high proportion of aromatic residues, revealing little secondary structure in aqueous solution. Addition of Cu2+ to Hexa(4) induced an increase in random coil to resemble Octa(4). The fluorescence of both peptides was quenched by Cu2+ and this was used to calculate Kd's of 6.7 mu M for Octa(4) and 4.5 mu M for Hexa(4). Other divalent cations showed lesser effects on the fluorescence of the peptides. (C) 1995 Academic Press, Inc.

  • Short Title: Copper-binding to the n-terminal tandem repeat region of mammalian and avian prion protein - structural studies using synthetic peptides
  • Journal: Biochemical And Biophysical Research Communications
  • Volume: 214
  • Issue: 3
  • Pages: 993-999
  • Publication type: Article
  • Bibliographic status: Published
    Staff

    Professor Jeremy Lakey
    Professor of Struct. Biochemistry