Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study (Articolo in rivista)

Type

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

Label

• Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

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

• 10.1039/b407928k (literal)

Alternative label

• Giuseppe Di Natale1 ; Giuseppe Impellizzeri1; Giuseppe Pappalardo2 (2005)
  Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study
  in Organic & biomolecular chemistry
  (literal)

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

• Giuseppe Di Natale1 ; Giuseppe Impellizzeri1; Giuseppe Pappalardo2 (literal)

Pagina inizio

• 490 (literal)

Pagina fine

• 497 (literal)

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

• 3 (literal)

Rivista

• Organic & biomolecular chemistry (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• 1 Dipartimento di Scienze Chimiche, Universit`a di Catania, V.le A. Doria 6, 95125, Catania 2 Istituto di Biostrutture e Bioimmagini-Sezione di Catania, CNR, V.le A. Doria 6, 95125, Catania. (literal)

Titolo

• Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study (literal)

Abstract

• Two peptide fragments, corresponding to the amino acid residues 106-126 (PrP[Ac-106-126-NH2]) and 106-114 (PrP[Ac-106-114-NH2]) of the human prion protein have been synthesised in the acetylated and amide form at their N- and C-termini, respectively. The conformational preferences of PrP[Ac-106-126-NH2] and PrP[Ac-106-114-NH2] were investigated using CD and NMR spectroscopy. CD results showed that PrP[Ac-106-126-NH2] mainly adopts an a-helical conformation in TFE-water mixture and in SDS micelles, while a predominantly random structure is observed in aqueous solution. The shorter PrP[Ac-106-114-NH2] fragment showed similar propensities when investigated under the same experimental conditions as those employed for PrP[Ac-106-126-NH2]. From CD experiments at different SDS concentrations, an a-helix/b-sheet conformational transition was only observed in the blocked PrP[Ac-106-126-NH2] sequence. The NMR analysis confirmed the helical nature of PrP[Ac-106-126-NH2] in the presence of SDS micelles. The shorter PrP[Ac-106-114-NH2] manifested a similar behaviour. The results as a whole suggest that both hydrophobic effects and electrostatic interactions play a significant role in the formation and stabilisation of ordered secondary structures in PrP[Ac-106-126-NH2]. (literal)

Prodotto di

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

Autore CNR

• GIUSEPPE PAPPALARDO (Unità di personale interno)
• GIUSEPPE DI NATALE (Unità di personale interno)

Insieme di parole chiave

• Parole chiave di "Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• GIUSEPPE PAPPALARDO (Unità di personale interno)
• 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

• Organic & biomolecular chemistry (Rivista)

Insieme di parole chiave di

• Parole chiave di "Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study" (Insieme di parole chiave)