European Biophysics Journal

, Volume 40, Issue 11, pp 1259–1270 | Cite as

Zinc modulates copper coordination mode in prion protein octa-repeat subdomains

  • Francesco Stellato
  • Ann Spevacek
  • Olivier Proux
  • Velia Minicozzi
  • Glenn Millhauser
  • Silvia MoranteEmail author
Original Paper


In this work we present and analyse XAS measurements carried out on various portions of Prion-protein tetra-octa-repeat peptides in complexes with Cu(II) ions, both in the presence and in the absence of Zn(II). Because of the ability of the XAS technique to provide detailed local structural information, we are able to demonstrate that Zn acts by directly interacting with the peptide, in this way competing with Cu for binding with histidine. This finding suggests that metal binding competition can be important in the more general context of metal homeostasis.


Prion protein Zinc Copper XAS spectroscopy Metal homeostasis 



We are very grateful to G.C. Rossi for useful discussions and for reading the manuscript. Partial financial support from PRIN08 is acknowledged. We thank the anonymous referees for their useful suggestions.

Supplementary material

249_2011_713_MOESM1_ESM.doc (138 kb)
Supplementary material 1 (DOC 138 kb)


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Copyright information

© European Biophysical Societies' Association 2011

Authors and Affiliations

  • Francesco Stellato
    • 1
    • 2
  • Ann Spevacek
    • 3
  • Olivier Proux
    • 4
  • Velia Minicozzi
    • 1
  • Glenn Millhauser
    • 3
  • Silvia Morante
    • 1
    Email author
  1. 1.Dipartimento di FisicaUniversità di Roma ‘Tor Vergata’RomeItaly
  2. 2.Centre for Free-Electron Laser Science, DESYHamburgGermany
  3. 3.Department of Chemistry and BiochemistryUniversity of CaliforniaSanta CruzUSA
  4. 4.Observatoire des Sciences de l’Univers de Grenoble, CNRS and Université Joseph FourierGrenoble Cedex 9France

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