Copper(II) binding to two novel histidine-containing model hexapeptides: Evidence for a metal ion driven turn conformation. (Articolo in rivista)

Type

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

Label

• Copper(II) binding to two novel histidine-containing model hexapeptides: Evidence for a metal ion driven turn conformation. (Articolo in rivista) (literal)

Anno

• 2008-01-01T00:00:00+01:00 (literal)

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

• 10.1016/j.jinorgbio.2008.07.017 (literal)

Alternative label

• Giuseppe Di Natale1; Chiara A. Damante1; Zoltán Nagy2; Katalin Osz2, Giuseppe Pappalardo3; Enrico Rizzarelli1,3; Imre Sóvágó 2 (2008)
  Copper(II) binding to two novel histidine-containing model hexapeptides: Evidence for a metal ion driven turn conformation.
  in Journal of inorganic biochemistry
  (literal)

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

• Giuseppe Di Natale1; Chiara A. Damante1; Zoltán Nagy2; Katalin Osz2, Giuseppe Pappalardo3; Enrico Rizzarelli1,3; Imre Sóvágó 2 (literal)

Pagina inizio

• 2012 (literal)

Pagina fine

• 2019 (literal)

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

• 102 (literal)

Rivista

• Journal of inorganic biochemistry (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• 1 Department of Chemical Sciences, University of Catania V.le A. Doria 6, 95125 Catania, Italy 2 Department of Inorganic and Analytical Chemistry, University of Debrecen, 4010 Debrecen, Hungary 3 CNR Institute of Biostructures and Bioimaging V.le A. Doria, 95125 Catania, Italy (literal)

Titolo

• Copper(II) binding to two novel histidine-containing model hexapeptides: Evidence for a metal ion driven turn conformation. (literal)

Abstract

• The solution conformation and the copper(II) binding properties have comparatively been investigated for the two novel hexapeptides Ac-HPSGHA-NH2 (P2) and Ac-HGSPHA-NH2 (P4). The study has been carried out by means of CD, NMR, EPR and UV-Vis spectroscopic techniques in addition to potentiometric measurements to determine the stability constants of the different copper(II) complex species formed in the pH range 3-11. The peptides contain two histidine residues as anchor sites for the metal ion and differ only for the exchanged position of the proline residue with glycine. CD and NMR results for the uncomplexed peptide ligands suggest a predominantly unstructured peptide chain in aqueous solution. Potentiometric and spectroscopic data (UV-Vis, CD and EPR) show that both peptides strongly interact with copper(II) ions by forming complexes with identical stoichiometries but different structures. Furthermore, Far-UV CD experiments indicate that the conformation of the peptides is dramatically affected following copper(II) complexation with the P4 peptide adopting a b-turn-like conformation. (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

• GIUSEPPE PAPPALARDO (Unità di personale interno)
• ENRICO RIZZARELLI (Unità di personale esterno)
• GIUSEPPE DI NATALE (Unità di personale interno)

Insieme di parole chiave

• Keywords of "Copper(II) binding to two novel histidine-containing model hexapeptides: Evidence for a metal ion driven turn conformation." (Insieme di parole chiave)

Incoming links:

Autore CNR di

• GIUSEPPE PAPPALARDO (Unità di personale interno)
• ENRICO RIZZARELLI (Unità di personale esterno)
• GIUSEPPE DI NATALE (Unità di personale interno)

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)

Insieme di parole chiave di

• Keywords of "Copper(II) binding to two novel histidine-containing model hexapeptides: Evidence for a metal ion driven turn conformation." (Insieme di parole chiave)