Stability of single sheet GNNQQNY aggregates analyzed by replica exchange molecular dynamics: antiparallel versus parallel association (Articolo in rivista)

Type

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

Label

• Stability of single sheet GNNQQNY aggregates analyzed by replica exchange molecular dynamics: antiparallel versus parallel association (Articolo in rivista) (literal)

Anno

• 2008-01-01T00:00:00+01:00 (literal)

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

• 10.1016/j.bbrc.2008.10.039 (literal)

Alternative label

• Vitagliano L.; Esposito L.; Pedone C.; De Simone A. (2008)
  Stability of single sheet GNNQQNY aggregates analyzed by replica exchange molecular dynamics: antiparallel versus parallel association
  in Biochemical and biophysical research communications (Print)
  (literal)

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

• Vitagliano L.; Esposito L.; Pedone C.; De Simone A. (literal)

Pagina inizio

• 1036 (literal)

Pagina fine

• 1041 (literal)

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

• 377 (literal)

Rivista

• Biochemical and biophysical research communications (Rivista)

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

• Pubblicazione su rivista internazionale (literal)

Note

• ISI Web of Science (WOS) (literal)

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

• Istituto di Biostrutture e Bioimmagini, CNR via Mezzocannone 16, I-80134 Napoli, Italy Department of Chemistry, University of Cambridge, Lensfield Road CB2 1EW, Cambridge, UK (literal)

Titolo

• Stability of single sheet GNNQQNY aggregates analyzed by replica exchange molecular dynamics: antiparallel versus parallel association (literal)

Abstract

• Protein and peptide aggregation into amyloid plaques is associated with a large variety of neurodegenerative diseases. The definition of the molecular bases of these pathologies is hampered by the transient nature of pre-fibrillar small-oligomers that are considered the toxic species. The ability of the peptide GNNQQNY to form amyloid-like structures makes it a good model to investigate the complex processes involved into amyloid fiber formation. By employing full atomistic replica exchange molecular dynamics simulations, we constructed the free energy surface of small assemblies of GNNQQNY to gain novel insights into the fiber formation process. The calculations suggest that the peptide exhibits a remarkable tendency to form both parallel and antiparallel b-sheets. The data show that GNNQQNY preference for parallel or antiparallel b-sheets is governed by a subtle balance of factors including assemblies' size, sidechain- sidechain interactions and pH. The samplings analysis provides a rationale to the observed trends. (literal)

Prodotto di

• Modelli molecolari per lo studio di malattie conformazionali (PM.P01.004.003) (Modulo)
• Institute of biostructure and bioimaging (IBB) (Istituto)
• Caratterizzazione strutturale di biomolecole di interesse terapeutico mediante metodologie computazionali (PM.P01.022.002) (Modulo)

Autore CNR

• CARLO PEDONE (Persona)
• LUCIANA ESPOSITO (Persona)
• LUIGI VITAGLIANO (Persona)

Incoming links:

Autore CNR di

• LUIGI VITAGLIANO (Persona)
• CARLO PEDONE (Persona)
• LUCIANA ESPOSITO (Persona)

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Caratterizzazione strutturale di biomolecole di interesse terapeutico mediante metodologie computazionali (PM.P01.022.002) (Modulo)
• Modelli molecolari per lo studio di malattie conformazionali (PM.P01.004.003) (Modulo)

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

• Biochemical and biophysical research communications (Rivista)