Copper(II) complexes with an avian prion N-terminal region and their potential SOD-like activity(509 views) La Mendola D, Bonomo RP, Caminati S, Di Natale G, Emmi SS, Hansson O, Maccarrone G, Pappalardo G, Pietropaolo A, Rizzarelli E
Istituto di Biostrutture e Bioimmagini-CNR-Catania, Viale A. Doria 6, 95125 Catania, Italy.
Dipartimento di Scienze Chimiche, Università di Catania, Viale A. Doria 6, 95125 Catania, Italy
Istituto per la Sintesi Organica e la Fotoreattività, CNR (ISOF-CNR), Via P. Gobetti 101, 40129 Bologna, Italy
Department of Chemistry, University of Gothenburg, P.O. Box 462, SE-405 30 Gothenburg, Sweden
References: Not available.
Copper(II) complexes with an avian prion N-terminal region and their potential SOD-like activity
Potentiometric and spectroscopic (UV-Vis, CD and EPR) studies were carried out on copper(II) complexes with chicken prion protein N-terminal fragments, Ac-(PHNPGY)(4)-NH(2), and the mutated residue, Ac-(PHNPGF)(4)-NH(2), to assess the role of tyrosine in the copper coordination. Both thermodynamic and spectroscopic results indicate that chicken prion fragments are not able to bind more than two copper ions and only with the involvement of side chain tyrosine groups. The prevailing complex shows one copper ion bound to four imidazole nitrogen atoms in the 1:1 metal to ligand ratio systems. The superoxide dismutase (SOD)-like activity of copper(II) complexes with the avian peptides and mammal analogue, Ac-(PHGGGWGQ)(4)-NH(2), was also investigated by means of Pulse radiolysis. The copper(II) complexes with avian peptides do not display SOD-like activity, while very low activity has been detected for the copper(II) complexes with mammalian tetraoctarepeat.
Copper(II) complexes with an avian prion N-terminal region and their potential SOD-like activity
No results.
Copper(II) complexes with an avian prion N-terminal region and their potential SOD-like activity
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(569 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