http://www.cnr.it/ontology/cnr/individuo/prodotto/ID201879
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
- 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
- Pagina fine
- 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
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- 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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- Autore CNR
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