Aggregation processes in beta-amyloid peptides: effects of molecular chaperons (Abstract/Poster in atti di convegno)

Type

• Prodotto della ricerca (Classe)
• Abstract/Poster in atti di convegno (Classe)

Label

• Aggregation processes in beta-amyloid peptides: effects of molecular chaperons (Abstract/Poster in atti di convegno) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

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

• 10.1007/s00249-005-0504-x (literal)

Alternative label

• A. Sgarbossa; D. Buselli; F. Lenci (2005)
  Aggregation processes in beta-amyloid peptides: effects of molecular chaperons
  in 5th European Biophysics Congress and 15th IUPAB joint Congress, Montpellier, France, 27 August-1 September 2005
  (literal)

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

• A. Sgarbossa; D. Buselli; F. Lenci (literal)

Pagina inizio

• 795 (literal)

Pagina fine

• 795 (literal)

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

• http://www.springerlink.com/content/kl77472l41047061/fulltext.pdf (literal)

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

• 34 (literal)

Rivista

• European biophysics journal (Rivista)

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

• 1 (literal)

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

• 6 (literal)

Note

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

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

• CNR, Istituto di BioFisica, Pisa, Italy (literal)

Titolo

• Aggregation processes in beta-amyloid peptides: effects of molecular chaperons (literal)

Abstract

• Several neurodegenerative pathologies, like Parkinson's, Hungtington's and Alzheimer's diseases, are related to the formation of small peptides aggregates, which amyloid fibrils originate from. Understanding the molecular mechanisms responsible for these processes can, therefore, contribute to clarify the origin and, hopefully, to control the development of the afore mentioned diseases. Here we report the results of an in vitro study aiming to affect the aggregation kinetic of 1-42 and 1-40 beta-amyloid peptides by means of an endogenous chaperone-like protein (alpha-crystallin) and an exogenous polycyclic aromatic pigment (hypericin) that can perturb the aggregation process through stacking interactions with the peptides aromatic residues. Because of the well known problems in getting reproducible and reliable results, particular attention has been devoted to carefully check the preparation procedures of the samples. The effects of both alpha-crystallin and hypericin on the self-assembly process have been examined at different times of the aggregation kinetics. The results are discussed in relation with the involvement of different molecular structures in the amyloid fibrillation phenomenon. (literal)

Editore

• Springer (Editore)

Prodotto di

• Istituto di biofisica (IBF) (Istituto)
• Processi Fotoindotti in Biomolecole e Cellule (MD.P01.003.001) (Modulo)

Autore CNR

• FRANCESCO LENCI (Unità di personale esterno)
• ANTONELLA SGARBOSSA (Unità di personale interno)

Incoming links:

Prodotto

• Istituto di biofisica (IBF) (Istituto)
• Processi Fotoindotti in Biomolecole e Cellule (MD.P01.003.001) (Modulo)

Autore CNR di

• ANTONELLA SGARBOSSA (Unità di personale interno)
• FRANCESCO LENCI (Unità di personale esterno)

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

• European biophysics journal (Rivista)

Editore di

• Springer (Editore)