Modeling the Zn+2 binding in the 1-16 region of the amyloid-beta peptide involved in Alzheimer's disease (Articolo in rivista)

Type

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

Label

• Modeling the Zn+2 binding in the 1-16 region of the amyloid-beta peptide involved in Alzheimer's disease (Articolo in rivista) (literal)

Anno

• 2009-01-01T00:00:00+01:00 (literal)

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

• 10.1039/b822771c (literal)

Alternative label

• Furlan S.; La Penna G. (2009)
  Modeling the Zn+2 binding in the 1-16 region of the amyloid-beta peptide involved in Alzheimer's disease
  in PCCP. Physical chemistry chemical physics (Print)
  (literal)

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

• Furlan S.; La Penna G. (literal)

Pagina inizio

• 6468 (literal)

Pagina fine

• 6481 (literal)

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

• http://dx.doi.org/10.1039/b822771c (literal)

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

• 11 (literal)

Rivista

• PCCP. Physical chemistry chemical physics (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• CNR-ICCOM, Firenze (literal)

Titolo

• Modeling the Zn+2 binding in the 1-16 region of the amyloid-beta peptide involved in Alzheimer's disease (literal)

Abstract

• Zinc ions are found at mM concentration in amyloid plaques of Alzheimer's disease and the role of zinc in protein oligomerization is the object of intense investigations. As an in vitro model for studying interactions between Zn2+ and the A beta peptide, that is the main component of plaques, the N- and C-termini protected A beta(1-16) fragment has been chosen because reliable spectroscopic studies in water solution are possible due to the low propensity for oligomerization at pH similar to 6.5, and because all the Zn binding sites of A beta have been identified in the 1-16 region. In this work we present the results of first principle simulations of several initial models of Zn-A beta(1-16) complexes. The NMR results about the same system, where His 6, 13, 14 and Glu 11 side-chains coordinate the Zn ion, are strongly supported by these models. Coordination of Asp 1 to Zn drives the complex towards the expulsion of one of initially bonded His side-chains. Coordination of Tyr 10 to Zn is possible only when Tyr 10 is deprotonated. The interplay between physico-chemical properties of the A beta ligand and the Zn coordination is discussed. (literal)

Prodotto di

• Istituto di chimica dei composti organo metallici (ICCOM) (Istituto)
• Aggregazione di proteine e struttura della cromatina (SV.P14.001.002) (Modulo)

Autore CNR

• GIOVANNI LA PENNA (Unità di personale interno)
• SARA FURLAN (Persona)

Insieme di parole chiave

• Parole chiave di "Modeling the Zn+2 binding in the 1-16 region of the amyloid-beta peptide involved in Alzheimer's disease" (Insieme di parole chiave)

Incoming links:

Prodotto

• Istituto di chimica dei composti organo metallici (ICCOM) (Istituto)
• Aggregazione di proteine e struttura della cromatina (SV.P14.001.002) (Modulo)

Autore CNR di

• GIOVANNI LA PENNA (Unità di personale interno)
• SARA FURLAN (Persona)

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

• PCCP. Physical chemistry chemical physics (Rivista)

Insieme di parole chiave di

• Parole chiave di "Modeling the Zn+2 binding in the 1-16 region of the amyloid-beta peptide involved in Alzheimer's disease" (Insieme di parole chiave)