Zoroddu, Maria Antonietta and Peana, Massimiliano Francesco and Medici, Serenella (2007) Structural model of a Ni(II) complex with a 30-amino acid peptide through an NMR study. In: ISMEC 2007: 18. Italian-Spanish congress on thermodynamics of metal complexes, 5-9 giugno 2007, Santa Margherita di Pula, Italia. [S.l.], [s.n.]. O12-O12. Conference or Workshop Item.
Multidimensional NMR spectroscopy is a useful tool for the calculation of structures or structural models of metal-peptide complexes in solution. We applied bidimensional
NMR techniques to study the interactions of Ni(II) ions with a 30-aminoacid peptide, a fragment of the C-terminal tail of Cap 43 protein. This protein is strictly connected to nickel exposure in cells, since it seems to be specifically expressed as a response to the presence of this metal in the cellular medium and it is also related to cancer development; an abnormal level of Cap43 protein has been detected in a number of tumour tissues. The striking feature of Cap 43 is a three-repeated decapeptide
sequence at its C-terminus; each 10-aminoacid fragment (TRSRSHTSEG) bearing a histidinic residue, which has been indicated as an anchoring site for metal binding in
numerous cases. We previously reported that each fragment is able to coordinate a Ni(II) ion in a very effective way.
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