A Multiscale Approach to Characterize the Early Aggregation Steps of the Amyloid-Forming Peptide GNNQQNY from the Yeast Prion Sup-35 (Articolo in rivista)

Type

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

Label

• A Multiscale Approach to Characterize the Early Aggregation Steps of the Amyloid-Forming Peptide GNNQQNY from the Yeast Prion Sup-35 (Articolo in rivista) (literal)

Anno

• 2011-01-01T00:00:00+01:00 (literal)

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

• 10.1371/journal.pcbi.1002051 (literal)

Alternative label

• Nasica-Labouze, Jessica; Meli, Massimiliano; Derreumaux, Philippe; Colombo, Giorgio; Mousseau, Normand (2011)
  A Multiscale Approach to Characterize the Early Aggregation Steps of the Amyloid-Forming Peptide GNNQQNY from the Yeast Prion Sup-35
  in PLoS computational biology
  (literal)

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

• Nasica-Labouze, Jessica; Meli, Massimiliano; Derreumaux, Philippe; Colombo, Giorgio; Mousseau, Normand (literal)

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

• 7 (literal)

Rivista

• PLoS computational biology (Rivista)

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

• 18 (literal)

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

• 5 (literal)

Note

• ISI Web of Science (WoS) (literal)
• ISI Web of Science (WOS) (literal)

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

• University of Montreal; University of Montreal; Consiglio Nazionale delle Ricerche (CNR); Centre National de la Recherche Scientifique (CNRS); Observatoire de Paris (literal)

Titolo

• A Multiscale Approach to Characterize the Early Aggregation Steps of the Amyloid-Forming Peptide GNNQQNY from the Yeast Prion Sup-35 (literal)

Abstract

• The self-organization of peptides into amyloidogenic oligomers is one of the key events for a wide range of molecular and degenerative diseases. Atomic-resolution characterization of the mechanisms responsible for the aggregation process and the resulting structures is thus a necessary step to improve our understanding of the determinants of these pathologies. To address this issue, we combine the accelerated sampling properties of replica exchange molecular dynamics simulations based on the OPEP coarse-grained potential with the atomic resolution description of interactions provided by all-atom MD simulations, and investigate the oligomerization process of the GNNQQNY for three system sizes: 3-mers, 12-mers and 20-mers. Results for our integrated simulations show a rich variety of structural arrangements for aggregates of all sizes. Elongated fibril-like structures can form transiently in the 20-mer case, but they are not stable and easily interconvert in more globular and disordered forms. Our extensive characterization of the intermediate structures and their physicochemical determinants points to a high degree of polymorphism for the GNNQQNY sequence that can be reflected at the macroscopic scale. Detailed mechanisms and structures that underlie amyloid aggregation are also provided. (literal)

Prodotto di

• simulazioni molecolari di sistemi biologici (INT.P02.001.001) (Modulo)
• Istituto di chimica del riconoscimento molecolare (ICRM) (Istituto)

Autore CNR

• MASSIMILIANO MELI (Persona)
• GIORGIO COLOMBO (Unità di personale interno)

Incoming links:

Prodotto

• Istituto di chimica del riconoscimento molecolare (ICRM) (Istituto)
• simulazioni molecolari di sistemi biologici (INT.P02.001.001) (Modulo)

Autore CNR di

• GIORGIO COLOMBO (Unità di personale interno)
• MASSIMILIANO MELI (Persona)

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

• PLoS computational biology (Rivista)