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

• 2005-01-01T00:00:00+01:00 (literal)

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

• 10.1002/chem.200500534 (literal)

Alternative label

• Domenico Grasso; Giulia Grasso; Valeria Guantieri; Giuseppe Impellizzeri; Carmelo La Rosa; Danilo Milardi; Giovanni Micera; Katalin Osz; Giuseppe Pappalardo; enrico Rizzarelli; Daniele Sanna; Imre Sovago (2005)
  Environmental effects on a prion's helix II domain: Copper(II) and membrane interactions with PrP180-193 and its analogues
  in Chemistry (Weinh., Print); Wiley-VCH Verlag Gmbh, Weinheim (Germania)
  (literal)

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

• Domenico Grasso; Giulia Grasso; Valeria Guantieri; Giuseppe Impellizzeri; Carmelo La Rosa; Danilo Milardi; Giovanni Micera; Katalin Osz; Giuseppe Pappalardo; enrico Rizzarelli; Daniele Sanna; Imre Sovago (literal)

Pagina inizio

• 537 (literal)

Pagina fine

• 547 (literal)

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

• 12 (literal)

Rivista

• Chemistry (Rivista)

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

• 2 (literal)

Note

• ISI Web of Science (WOS) (literal)

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

• Univ Catania, Dipartimento Sci Chim, I-95125 Catania, Italy CNR, Ist Biostrutture & Bioimagini, Sez Catania, I-95125 Catania, Italy Univ Padua, Dipartimento Chim Inorgan Met Organ & Analit, I-35131 Padua, Italy Univ Sassari, Dipartimento Chim, I-07100 Sassari, Italy Debrecen Univ Med, Dept Inorgan & Analyt Chem, H-4010 Debrecen, Hungary CNR, Ist Chim Biomol, Sez Cassari, I-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 11 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 PrPAc184-188NH(2) (IKQHT) analogue 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 PrPAc184-188NH(2) (IKQHT) analogue as a model. ESI-MS, ESR, UV/Vis, and CD measurements were carried out on the copper(II)/PrPAc184-188NH(2) and copper(II)/PrP180-193NH(2) systems, and showed that PrPAc184-188NH(2) is a reliable model for the metal interaction with the helix 11 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)

Editore

• Wiley-VCH Verlag Gmbh (Editore)

Prodotto di

• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

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

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• 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)
• DANILO MILARDI (Persona)
• GIULIA GRASSO (Persona)
• ENRICO RIZZARELLI (Unità di personale esterno)

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)

Editore di

• Wiley-VCH Verlag Gmbh (Editore)

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

• Chemistry (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)