Environmental Effects on a Prion’s Helix II Domain: Copper(II) and Membrane Interactions with PrP180–193 and Its Analogues. (Articolo in rivista)

Type

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

Label

• Environmental Effects on a Prion’s Helix II Domain: Copper(II) and Membrane Interactions with PrP180–193 and Its Analogues. (Articolo in rivista) (literal)

Anno

• 2006-01-01T00:00:00+01:00 (literal)

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

• 10.1002/chem.200500534 (literal)

Alternative label

• D. Grasso, G. Grasso, V. Guantieri, G. Impellizzeri, C. La Rosa, D. Milardi, G. Micera, K. Ösz, G. Pappalardo, E. Rizzarelli, D. Sanna and I. Sóvágó (2006)
  Environmental Effects on a Prion’s Helix II Domain: Copper(II) and Membrane Interactions with PrP180–193 and Its Analogues.
  in Chemistry - A European Journal
  (literal)

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

• D. Grasso, G. Grasso, V. Guantieri, G. Impellizzeri, C. La Rosa, D. Milardi, G. Micera, K. Ösz, G. Pappalardo, E. Rizzarelli, D. Sanna and I. Sóvágó (literal)

Pagina inizio

• 537 (literal)

Pagina fine

• 547 (literal)

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

• http://onlinelibrary.wiley.com/doi/10.1002/chem.200500534/abstract (literal)

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

• 12 (literal)

Rivista

• Chemistry - A European Journal (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• Università di Catania, Dipartimento di Scienze Chimiche, Viale Andrea Doria 6, 95125 Catania, Italy Istituto CNR di Biostrutture e Bioimmagini - Sezione di Catania, Viale Andrea Doria 6, 95125 Catania, Italy Università di Padova, Dipartimento di Chimica Inorganica, Metallorganica ed Analitica, Via F. Marzolo 1, 35131 Padova, Italy Università di Sassari, Dipartimento di Chimica via Vienna 2, 07100 Sassari, Italy University of Debrecen, Department of Inorganic and Analytical Chemistry, 4010 Debrecen, Hungary, Fax: (+36) 52-489-667 Istituto CNR di Chimica Biomolecolare-Sezione di Sassari, Traversa La Crucca 3, Regione Baldinca, 07040 Li Punti (SS), Italy (literal)

Titolo

• Environmental Effects on a Prion’s Helix II Domain: Copper(II) and Membrane Interactions with PrP180–193 and Its Analogues. (literal)

Abstract

• An abnormal interaction between copper and the prion protein is believed to play a pivotal role in the pathogenesis of prion diseases. Copper binding has been mainly attributed to the N-terminal domain of the prion protein, but this hypothesis has recently been challenged in some papers which suggest that the C-terminal domain might also compete for metal anchoring. In particular, the segment corresponding to the helix II region of the prion protein, namely PrP180–193, has been shown both to bind copper and to exhibit a copper-enhanced cytotoxicity, as well as to interact with artificial membranes. The present work is aimed at extending these results by choosing the most representative model of this domain and by determining its copper affinity. With this aim, the different role played by the electrostatic properties of the C- and N-termini of PrP180–193 (VNITIKQHTVTTTT) in determining its conformational behaviour, copper coordination and ability to perturb model membranes was investigated. Owing to the low solubility of PrP180–193, its copper affinity was evaluated by using the shorter PrPAc184–188NH2 (IKQHT) analogueas a model. ESI-MS, ESR, UV/Vis, and CD measurements were carried out on the copper(ii)/PrPAc184–188NH2 and copper(ii)/PrP180–193NH2 systems, and showed that PrPAc184–188NH2 is a reliable model for the metal interaction with the helix II domain. The affinity of copper(ii) for the helix II fragment is higher than that for the octarepeat and PrP106–126 peptides. Finally, the different ability of PrP180–193 analogues to perturb the DPPC model membrane was assessed by DSC measurements. The possible biological consequences of these findings are also discussed briefly. (literal)

Prodotto di

• Istituto di chimica biomolecolare (ICB) (Istituto)
• Caratterizzazione di complessi metallici formati da proteine coinvolte in patologie correlate al disordine conformazionale proteico. (PM.P01.004.002) (Modulo)

Autore CNR

• ENRICO RIZZARELLI (Unità di personale esterno)
• GIUSEPPE PAPPALARDO (Unità di personale interno)
• GIULIA GRASSO (Persona)
• DANILO MILARDI (Persona)
• DANIELE SANNA (Persona)

Insieme di parole chiave

• Parole chiave di "Environmental Effects on a Prion’s Helix II Domain: Copper(II) and Membrane Interactions with PrP180–193 and Its Analogues." (Insieme di parole chiave)

Incoming links:

Autore CNR di

• GIUSEPPE PAPPALARDO (Unità di personale interno)
• DANIELE SANNA (Persona)
• DANILO MILARDI (Persona)
• GIULIA GRASSO (Persona)
• ENRICO RIZZARELLI (Unità di personale esterno)

Prodotto

• Istituto di chimica biomolecolare (ICB) (Istituto)
• Caratterizzazione di complessi metallici formati da proteine coinvolte in patologie correlate al disordine conformazionale proteico. (PM.P01.004.002) (Modulo)

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

• Chemistry - A European Journal (Rivista)

Insieme di parole chiave di

• Parole chiave di "Environmental Effects on a Prion’s Helix II Domain: Copper(II) and Membrane Interactions with PrP180–193 and Its Analogues." (Insieme di parole chiave)