Copper(II) complexes with peptide fragments encompassing the sequence 122-130 of human doppel protein (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Copper(II) complexes with peptide fragments encompassing the sequence 122-130 of human doppel protein (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.2009.01.017 (literal)

Alternative label

• D. La Mendola; A. Magrì; Ö. Hansson; R. P. Bonomo; E. Rizzarelli (2009)
  Copper(II) complexes with peptide fragments encompassing the sequence 122-130 of human doppel protein
  in Journal of inorganic biochemistry
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• D. La Mendola; A. Magrì; Ö. Hansson; R. P. Bonomo; E. Rizzarelli (literal)

Pagina inizio

• 758 (literal)

Pagina fine

• 765 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 103 (literal)

Rivista

• Journal of inorganic biochemistry (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Ö. Hansson Department of Chemistry, University of Gothenburg, PO Box 462, SE-405 30 Gothenburg, Sweden R. P. Bonomo Dipartimento di Scienze Chimiche, Università di Catania, Viale A. Doria 6, 95125 Catania, Italy (literal)

Titolo

• Copper(II) complexes with peptide fragments encompassing the sequence 122-130 of human doppel protein (literal)

Abstract

• Copper(II) complexes of the peptide fragment (Dpl122-130) encompassing the sequence 122-130 of human doppel protein were characterized by potentiometric, UV-Visible, CD and EPR spectroscopic methods. An analogous peptide, in which the aspartate residue was substituted by an asparagine amino acid, was synthesized in order to provide evidence on the possible role of carboxylate group in copper(II) coordination. It was found that the carboxylic group is directly involved in copper(II) coordination at acidic pH, forming the CuLH(2) species with Dpl122-130. This copper(II) complex displayed EPR parameters very similar to those of the analogous complex with the whole doppel protein. At pH higher than 7, the complexes showed magnetic parameters similar to those of the major species of protein formed in the pH range 7-8, with the metal coordination environment consisting of one imidazole and three amide nitrogen atoms. The comparison of Cu-Dpl122-130 binding constant values with those of the prion peptide fragments (PrP106-114), showed that doppel peptide had a higher metal binding affinity at acidic pH whereas the prion peptide fragment binds the metal tightly at physiological pH. (C) 2009 Elsevier Inc. All rights reserved. (literal)

Prodotto di

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Studio degli effetti di ioni metallici e membrane sulle proprietà conformazionali di sistemi amiloidogenici. (PM.P01.004.001) (Modulo)

Autore CNR

• ENRICO RIZZARELLI (Unità di personale esterno)
• ANTONIO MAGRI' (Persona)
• DIEGO LA MENDOLA (Unità di personale interno)

Incoming links:

Autore CNR di

• DIEGO LA MENDOLA (Unità di personale interno)
• ANTONIO MAGRI' (Persona)
• ENRICO RIZZARELLI (Unità di personale esterno)

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Studio degli effetti di ioni metallici e membrane sulle proprietà conformazionali di sistemi amiloidogenici. (PM.P01.004.001) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Journal of inorganic biochemistry (Rivista)