Nickel (ii) And Mixed Metal Complexes Of Amyloid-B N-Terminus. Results Of Potentiometric And Spectroscopic Studies On The Binary Nickel (ii) And Mixed Metal Nickel (ii)-Copper (ii) And Nickel (ii)-Copper (ii)-Zinc (ii) Complexes Of Peptide Fragments
Nickel (ii) And Mixed Metal Complexes Of Amyloid-B N-Terminus. Results Of Potentiometric And Spectroscopic Studies On The Binary Nickel (ii) And Mixed Metal Nickel (ii)-Copper (ii) And Nickel (ii)-Copper (ii)-Zinc (ii) Complexes Of Peptide Fragments(489 views) Jozsa E, Hosz K, Kallay C, De Bona P, Damante CA, Pappalardo G, Rizzarelli E, Sovago I
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2010; 39(30): 7046-7053.
University of Debrecen, Department of Inorganic and Analytical Chemistry, H-4010 Debrecen, Hungary
University of Catania, Department of Chemical Sciences, 95125 Catania, Italy
CNR, Institute of Biostructures and Bioimaging, Catania 95125, Italy
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Nickel (ii) And Mixed Metal Complexes Of Amyloid-B N-Terminus. Results Of Potentiometric And Spectroscopic Studies On The Binary Nickel (ii) And Mixed Metal Nickel (ii)-Copper (ii) And Nickel (ii)-Copper (ii)-Zinc (ii) Complexes Of Peptide Fragments
Nickel (ii) complexes of A (1-16) Y10A and its smaller fragments including A (1-4), A (1-6), Ac-A (1-6) and Ac-A (8-16) Y10A have been studied by potentiometric, UV-Vis and circular dichroism spectroscopic measurements. The formation of mixed metal complexes and the distribution of metal ions among the possible coordination sites in the Cu (ii) -Ni (ii) -A (1- 16) Y10A and Cu (ii) -Ni (ii) -Zn (ii) -A (1-16) Y10A systems have also been evaluated. It was found that the hexadecapeptide and its fragments are effective nickel (ii) binding ligands and complex formation processes of nickel (ii) ions are quite similar to those of copper (ii). Formation of mono- and di-nuclear complexes was detected in the nickel (ii) -A (1-16) Y10A system suggesting the existence of two separated metal binding motifs: the N-terminus and internal histidyl residues. The preference for the coordination at the N-terminus was supported by the spectroscopic measurements but in equilibrium with the metal binding at the internal histidyl sites. Neither zinc (ii) nor nickel (ii) can, however, substitute copper (ii) in the mixed metal complexes of A (1-16) Y10A, but both metal ions are able to alter the distribution of copper (ii) ions among the various binding sites. Both N-terminus (amino and His6) and internal histidyl residues (His13 and His14) can work as dinuclear binding motifs, preferably accommodating copper (II) and zinc (II), respectively, while nickel (ii) can occupy the remaining free coordination sites. The Royal Society of Chemistry 2010
Nickel (ii) And Mixed Metal Complexes Of Amyloid-B N-Terminus. Results Of Potentiometric And Spectroscopic Studies On The Binary Nickel (ii) And Mixed Metal Nickel (ii)-Copper (ii) And Nickel (ii)-Copper (ii)-Zinc (ii) Complexes Of Peptide Fragments
Nickel (ii) And Mixed Metal Complexes Of Amyloid-B N-Terminus. Results Of Potentiometric And Spectroscopic Studies On The Binary Nickel (ii) And Mixed Metal Nickel (ii)-Copper (ii) And Nickel (ii)-Copper (ii)-Zinc (ii) Complexes Of Peptide Fragments
Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I * Copper(II) complexes of rat amylin fragments(360 views) Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721. Impact Factor:3.838 ViewExport to BibTeXExport to EndNote