alpha-Casein Inhibits Insulin Amyloid Formation by Preventing the Onset of Secondary Nucleation Processes (Articolo in rivista)

Type

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

Label

• alpha-Casein Inhibits Insulin Amyloid Formation by Preventing the Onset of Secondary Nucleation Processes (Articolo in rivista) (literal)

Anno

• 2014-01-01T00:00:00+01:00 (literal)

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

• 10.1021/jz501570m (literal)

Alternative label

• Librizzi, Fabio; Carrotta, Rita; Spigolon, Dario; Bulone, Donatella; San Biagio, Pier Luigi (2014)
  alpha-Casein Inhibits Insulin Amyloid Formation by Preventing the Onset of Secondary Nucleation Processes
  in The journal of physical chemistry letters
  (literal)

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

• Librizzi, Fabio; Carrotta, Rita; Spigolon, Dario; Bulone, Donatella; San Biagio, Pier Luigi (literal)

Pagina inizio

• 3043 (literal)

Pagina fine

• 3048 (literal)

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

• 5 (literal)

Rivista

• ?The ?journal of physical chemistry letters (Rivista)

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

• 6 (literal)

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

• 17 (literal)

Note

• ISI Web of Science (WOS) (literal)

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

• Consiglio Nazionale delle Ricerche (CNR) (literal)

Titolo

• alpha-Casein Inhibits Insulin Amyloid Formation by Preventing the Onset of Secondary Nucleation Processes (literal)

Abstract

• alpha-Casein is known to inhibit the aggregation of several proteins, including the amyloid beta-peptide, by mechanisms that are not yet completely clear. We studied its effects on insulin, a system extensively used to investigate the properties of amyloids, many of which are common to all proteins and peptides. In particular, as for other proteins, insulin aggregation is affected by secondary nucleation pathways. We found that alpha-casein strongly delays insulin amyloid formation, even at extremely low doses, when the aggregation process is characterized by secondary nucleation. At difference, it has a vanishing inhibitory effect on the initial oligomer formation, which is observed at high concentration and does not involve any secondary nucleation pathway. These results indicate that an efficient inhibition of amyloid formation can be achieved by chaperone-like systems, by sequestering the early aggregates, before they can trigger the exponential proliferation brought about by secondary nucleation mechanisms. (literal)

Prodotto di

• Processi di aggregazione biomolecolare (MD.P01.002.001) (Modulo)
• Istituto di biofisica (IBF) (Istituto)

Autore CNR

• RITA CARROTTA (Unità di personale interno)
• PIER LUIGI SAN BIAGIO (Unità di personale interno)
• FABIO LIBRIZZI (Unità di personale interno)
• DARIO SPIGOLON (Unità di personale esterno)
• DONATELLA BULONE (Unità di personale interno)

Incoming links:

Prodotto

• Istituto di biofisica (IBF) (Istituto)
• Processi di aggregazione biomolecolare (MD.P01.002.001) (Modulo)

Autore CNR di

• PIER LUIGI SAN BIAGIO (Unità di personale interno)
• DONATELLA BULONE (Unità di personale interno)
• DARIO SPIGOLON (Unità di personale esterno)
• RITA CARROTTA (Unità di personale interno)
• FABIO LIBRIZZI (Unità di personale interno)

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

• ?The ?journal of physical chemistry letters (Rivista)