Copper(II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region (Articolo in rivista)

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Label
  • Copper(II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region (Articolo in rivista) (literal)
Anno
  • 2004-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.jinorgbio.2003.09.006 (literal)
Alternative label
  • David R Brown1; Valeria Guantieri2; Giulia Grasso3; Giuseppe Impellizzeri4; Giuseppe Pappalardo3; Enrico Rizzarelli3,4 (2004)
    Copper(II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region
    in Journal of inorganic biochemistry
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • David R Brown1; Valeria Guantieri2; Giulia Grasso3; Giuseppe Impellizzeri4; Giuseppe Pappalardo3; Enrico Rizzarelli3,4 (literal)
Pagina inizio
  • 133 (literal)
Pagina fine
  • 143 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 98 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1 Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, UK 2 Dipartimento di Chimica Inorganica, Metallorganica ed Analitica, Università di Padova, via Marzolo 1, 35131 Padova, Italy 3 Istituto CNR di Biostrutture e Bioimmagini, Sezione di Catania, V.le A. Doria 6, 95125 Catania, Italy 4 Dipartimento di Scienze Chimiche, Università di Catania, V.le A. Doria 6, 95125 Catania, Italy (literal)
Titolo
  • Copper(II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region (literal)
Abstract
  • In this paper, we report the characterization of copper(II) complexes with two prion (PrP) protein peptide fragment analogues (VNITKQHTVTTTT), one with the N-terminus acetylated and the C-terminus amidated (PrP Ac180-193NH2) and the other with both the C- and N-termini free (PrP 180-193). Such peptide sequence almost entirely encompasses the PrPC?s helix 2 in the Cterminal region. The stoichiometry, the binding modes and the conformational features of the copper(II) complexes with the above mentioned two peptides were investigated by electrospray ionization-mass spectrometry (ESI-MS), UV-visible (UV-Vis) spectrometry and electron paramagnetic resonance (EPR) spectrometry as well as by circular dichroism (CD) measurements. The binding site location of copper(II) in the structured region of the protein can be here suggested on the basis of our findings that show the involvement of His 187 residue. The similarity of the EPR parameters suggests that the anchoring imidazole residue drives the copper(II) coordination environment towards a common binding motif in different regions of the prion protein. (literal)
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