Complex formation processes and metal ion catalyzed oxidation of model peptides related to the metal binding site of the human prion protein

Csire, Gizella and Turi, Ildikó and Sóvágó, Imre and Kárpáti, Eszter and Kállay, Csilla (2020) Complex formation processes and metal ion catalyzed oxidation of model peptides related to the metal binding site of the human prion protein. JOURNAL OF INORGANIC BIOCHEMISTRY. ISSN 0162-0134

Preview

Text 32Csire_Trideka_Eszter.pdf Available under License Creative Commons Attribution. Download (1MB) | Preview

Abstract

Interaction of copper(II) and nickel(II) ions with the Ac-PHAAAGTHSMKHM-NH2 tridecapeptide containing the His85, His96 and His111 binding sites of human prion protein has been studied by various techniques. pH-potentiometry, UV-Vis and circular dichroism spectroscopy were applied to study the stoichiometry, stability and structure of the copper(II) and nickel(II) complexes, while HPLC-MS and MS/MS were used for identifying the products of copper(II) catalyzed oxidation. The copper binding ability of shorter fragments, namely the nonapeptide Ac-PHAAAGTHS-NH2 and pentapeptide Ac-PHAAA-NH2 have also been studied. The tridecapeptide is able to bind three equivalent of copper(II) ion, since the histidine residues behave as independent metal binding sites. Nevertheless, the metal binding ability of histidine residue mimicking the octarepeat domain (His85) is decreased, while the other parts of the peptide mimicking the histidines outside the octarepeat domain bind the copper ions in comparable concentration. On the other hand, this peptide is able to coordinate only two equivalents of nickel ion on the domains outside the octarepeat region. Furthermore the His96 binding site is more effective for the nickel ions. Both histidine and methionine residues are sensitive for oxidation, the oxidation of these residues are proved, and in the case of the histidine residues follows the order His96 >His85 >> His111.

Actions (login required)

Edit Item