alpha-Casein Inhibition Mechanism in Concanavalin A Aggregation Process (Articolo in rivista)

Type
Label
  • alpha-Casein Inhibition Mechanism in Concanavalin A Aggregation Process (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/jp307417x (literal)
Alternative label
  • Carrotta R; Vilasi S; Librizzi F; Martorana V; Bulone D; San Biagio PL (2012)
    alpha-Casein Inhibition Mechanism in Concanavalin A Aggregation Process
    in The journal of physical chemistry. B
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Carrotta R; Vilasi S; Librizzi F; Martorana V; Bulone D; San Biagio PL (literal)
Pagina inizio
  • 14700 (literal)
Pagina fine
  • 14707 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://pubs.acs.org/doi/abs/10.1021/jp307417x (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 116 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 50 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • CNR, Inst Biophys, I-90146 Palermo, Italy (literal)
Titolo
  • alpha-Casein Inhibition Mechanism in Concanavalin A Aggregation Process (literal)
Abstract
  • The 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. (literal)
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