Copper(II) complexes with an avian prion N-terminal region and their potential SOD-like activity (Articolo in rivista)

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Label
  • Copper(II) complexes with an avian prion N-terminal region and their potential SOD-like activity (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.jinorgbio.2008.10.002 (literal)
Alternative label
  • Diego La Mendola; Raffaele P. Bonomo; Serena Caminati; Giuseppe Di Natale; Salvatore S. Emmi; Örjan Hansson; Giuseppe Maccarrone; Giuseppe Pappalardo; Adriana Pietropaolo; Enrico Rizzarelli (2009)
    Copper(II) complexes with an avian prion N-terminal region and their potential SOD-like activity
    in Journal of inorganic biochemistry
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Diego La Mendola; Raffaele P. Bonomo; Serena Caminati; Giuseppe Di Natale; Salvatore S. Emmi; Örjan Hansson; Giuseppe Maccarrone; Giuseppe Pappalardo; Adriana Pietropaolo; Enrico Rizzarelli (literal)
Pagina inizio
  • 195 (literal)
Pagina fine
  • 204 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 103 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Raffaele P. Bonomo, Dipartimento di Scienze Chimiche, Università di Catania, Italy Giuseppe Di Natale, Dipartimento di Scienze Chimiche, Università di Catania, Italy Giuseppe Maccarrone, Dipartimento di Scienze Chimiche, Università di Catania, Italy Adriana Pietropaolo, Dipartimento di Scienze Chimiche, Università di Catania, Italy Enrico Rizzarelli, Dipartimento di Scienze Chimiche, Università di Catania, Italy Serena Caminati, Salvatore S. Emmi, Örjan Hansson, (literal)
Titolo
  • Copper(II) complexes with an avian prion N-terminal region and their potential SOD-like activity (literal)
Abstract
  • 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 indicare 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. (literal)
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