Copper(II) complexes with an avian prion N-terminal region and their potential SOD-like activity
| Autor: | Giuseppe Di Natale, Enrico Rizzarelli, Giuseppe Maccarrone, Giuseppe Pappalardo, Serena Caminati, Adriana Pietropaolo, Örjan Hansson, Salvatore S. Emmi, Diego La Mendola, Raffaele P. Bonomo |
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| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Stereochemistry
Prions chicken Potentiometric titration Inorganic chemistry chemistry.chemical_element Biochemistry Inorganic Chemistry Metal Superoxide dismutase Residue (chemistry) chemistry.chemical_compound Mice Hexarepeat Imidazole Animals Amino Acid Sequence Tyrosine biology Chemistry Ligand Superoxide Dismutase Spectrum Analysis pulse radiolysis octareapeat Copper Peptide Fragments peptide visual_art copper visual_art.visual_art_medium biology.protein Thermodynamics Chickens octarepeat |
| Zdroj: | Journal of inorganic biochemistry 103 (2009): 195–204. doi:10.1016/j.jinorgbio.2008.10.002 info:cnr-pdr/source/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/titolo:Copper(II) complexes with an avian prion N-terminal region and their potential SOD-like activity/doi:10.1016%2Fj.jinorgbio.2008.10.002/rivista:Journal of inorganic biochemistry/anno:2009/pagina_da:195/pagina_a:204/intervallo_pagine:195–204/volume:103 Journal of inorganic biochemistry 103 (2009): 195–204. info:cnr-pdr/source/autori:D. La Mendola, R. P. Bonomo, S. Caminati, G. Di Natale, S. S. Emmi, Ö. Hansson, G. Maccarrone, G. Pappalardo, A. Pietropaolo, E. Rizzarelli/titolo:Copper(II) complexes with an avian prion N-terminal region and their potential SOD-like activity/doi:/rivista:Journal of inorganic biochemistry/anno:2009/pagina_da:195/pagina_a:204/intervallo_pagine:195–204/volume:103 |
| DOI: | 10.1016/j.jinorgbio.2008.10.002 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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