Anno2014
AutoriLibrizzi, Fabio; Carrotta, Rita; Spigolon, Dario; Bulone, Donatella; San Biagio, Pier Luigi
Abstractalpha-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.
RivistaThe Journal Of Physical Chemistry Letters
ISSN1948-7185
Impact factor0
Volume5
Pagina inizio3043
Pagina fine3048
Autori IBFDonatella BULONE, Pier Luigi SAN BIAGIO, Rita CARROTTA, Fabio LIBRIZZI, Dario SPIGOLON
Linee di Ricerca IBFMD.P01.002.001
Sedi IBFIBF.PA