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