Does tetracycline bind helix 2 of prion? An integrated spectroscopical and computational study of the interaction between the antibiotic and alpha helix 2 human prion protein fragments (Articolo in rivista)

Type

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

Label

• Does tetracycline bind helix 2 of prion? An integrated spectroscopical and computational study of the interaction between the antibiotic and alpha helix 2 human prion protein fragments (Articolo in rivista) (literal)

Anno

• 2007-01-01T00:00:00+01:00 (literal)

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

• 10.1002/prot.21204 (literal)

Alternative label

• Ronga L., Langella E., Palladino P., Marasco D., Tizzano B., Saviano M., Pedone C., Improta R. and Ruvo M (2007)
  Does tetracycline bind helix 2 of prion? An integrated spectroscopical and computational study of the interaction between the antibiotic and alpha helix 2 human prion protein fragments
  in Proteins (Print)
  (literal)

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

• Ronga L., Langella E., Palladino P., Marasco D., Tizzano B., Saviano M., Pedone C., Improta R. and Ruvo M (literal)

Pagina inizio

• 707 (literal)

Pagina fine

• 715 (literal)

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

• 66 (literal)

Rivista

• Proteins (Rivista)

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

• Pubblicazione su rivista scientifica (literal)

Note

• ISI Web of Science (WOS) (literal)

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

• CNR, Ist Biostrutture & Bioimmagini, Sez Biostrutture, I-80134 Naples, Italy Univ Naples Federico II, Dipartimento Sci Biol, Sez Biostrutture, I-80134 Naples, Italy (literal)

Titolo

• Does tetracycline bind helix 2 of prion? An integrated spectroscopical and computational study of the interaction between the antibiotic and alpha helix 2 human prion protein fragments (literal)

Abstract

• We demonstrate here that tetracycline (TC) can strongly interact (K-D = 189 +/- 7 nM) with model peptides derived from the C-terminal globular domain of the prion protein, hPrP [173-195], and that interaction concerns residues within the C-terminal half of the helix 2, a short region previously indicated as endowed with ambivalent conformational behavior and implicated in PrP conversion to the P-sheet-rich, infective scrapie variant. Data have been confirmed by binding studies with the N-terminal truncated 180-195 variant that displays a dissociation constant of 483 +/- 30 nM. Remarkably, TC does not influence the structure of the N-terminally fluoresceinated peptides that both show alpha-helical conformations. Docking calculations and molecular dynamics simulations suggest a direct, strong interaction of the antibiotic with exposed side chain functional groups of threonines 190-193 on the solvent-exposed surface of helix 2. (literal)

Prodotto di

• Modelli molecolari per lo studio di malattie conformazionali (PM.P01.004.003) (Modulo)
• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• CARLO PEDONE (Persona)
• MICHELE SAVIANO (Persona)
• MENOTTI RUVO (Unità di personale interno)

Incoming links:

Autore CNR di

• MICHELE SAVIANO (Persona)
• CARLO PEDONE (Persona)
• MENOTTI RUVO (Unità di personale interno)

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Modelli molecolari per lo studio di malattie conformazionali (PM.P01.004.003) (Modulo)

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

• Proteins (Rivista)