Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: speciation, stability constants and binding details.

@article{Osz2007CopperIIIW,
  title={Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: speciation, stability constants and binding details.},
  author={Katalin Osz and Zolt{\'a}n Nagy and Giuseppe Pappalardo and Giuseppe Di Natale and Daniele Sanna and Giovanni Micera and Enrico Rizzarelli and Imre S{\'o}v{\'a}g{\'o}},
  journal={Chemistry},
  year={2007},
  volume={13 25},
  pages={7129-43}
}
A 31-mer polypeptide, which encompasses residues 84-114 of human prion protein HuPrP(84-114) and contains three histidyl residues, namely one from the octarepeat (His85) and two histidyl residues from outside the octarepeat region (His96 and His111), and its mutants with two histidyl residues HuPrP(84-114)His85Ala, HuPrP(84-114) His96Ala, HuPrP(84-114)His111Ala and HuPrP(91-115) have been synthesised and their Cu2+ complexes studied by potentiometric and spectroscopic (UV/Vis, CD, EPR, ESI-MS… CONTINUE READING