Anno2012
AutoriCarrotta R; Vilasi S; Librizzi F; Martorana V; Bulone D; San Biagio PL
AbstractThe inhibition of the aggregation in protein solutions is currently a subject of great interest in many research fields, from the study of protein-misfolding related diseases to pharmaceutics, biotechnology, and food science. ?s1-Casein, one of the four types of caseins, which are the largest protein component of bovine milk, has been found to hinder the aggregation process of several proteins, including the amyloid ?-peptide, involved in Alzheimer's disease. To shed light into the mechanisms by which casein exerts this chaperon-like protective action, we studied its effect on the different steps of the aggregation process of concanavalin A, by means of both static and dynamic light scattering, thioflavin T and ANS fluorescence, circular dichroism, and atomic force microscopy. Our results show that casein has a poor effect on the first step of the process leading to the formation of amyloid-like structures. On the contrary, it has a marked effect on the second step of the process, ascribable to clusters condensation and compaction, up to the formation of very large aggregates. Such an effect requires a molar ratio of casein larger than that necessary to inhibit the fibrillogenesis of the amyloid ?-peptide, thus, suggesting a different mechanism of interaction of casein, depending on both conformational properties and relative size of the aggregating molecules.
RivistaThe Journal Of Physical Chemistry. B
ISSN1520-6106
Impact factor
Volume116
Pagina inizio14707
Pagina fine14700
Autori IBFDonatella BULONE, Pier Luigi SAN BIAGIO, Vincenzo MARTORANA, Rita CARROTTA, Silvia VILASI, Fabio LIBRIZZI
Linee di Ricerca IBFMD.P01.002.001
Sedi IBFIBF.PA