Early events in insulin fibrillization studied by time-lapse atomic force microscopy (Articolo in rivista)

Type
Label
  • Early events in insulin fibrillization studied by time-lapse atomic force microscopy (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1529/biophysj.105.068833 (literal)
Alternative label
  • Podestà A.; G.Tiana; P. Milani; M. Manno. (2006)
    Early events in insulin fibrillization studied by time-lapse atomic force microscopy
    in Biophysical journal (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Podestà A.; G.Tiana; P. Milani; M. Manno. (literal)
Pagina inizio
  • 589 (literal)
Pagina fine
  • 597 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 90 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Italian Natl Res Council, Inst Biophys Palermo, I-90146 Palermo, Italy; Univ Milan, Ist Nazl Fis Mat, Dipartimento Fis, Milan, Italy; Univ Milan, Cimaina, Milan, Italy; Ist Nazl Fis Nucl, I-20133 Milan, Italy (literal)
Titolo
  • Early events in insulin fibrillization studied by time-lapse atomic force microscopy (literal)
Abstract
  • The importance of understanding the mechanism of protein aggregation into insoluble amyloid fibrils lies not only in its medical consequences, but also in its more basic properties of self-organization. The discovery that a large number of uncorrelated proteins can form, under proper conditions, structurally similar fibrils has suggested that the underlying mechanism is a general feature of polypeptide chains. In this work, we address the early events preceding amyloid fibril formation in solutions of zinc-free human insulin incubated at low pH and high temperature. Here, we show by time-lapse atomic force microscopy that a steady-state distribution of protein oligomers with a quasiexponential tail is reached within a few minutes after heating. This metastable phase lasts for a few hours, until fibrillar aggregates are observable. Although for such complex systems different aggregation mechanisms can occur simultaneously, our results indicate that the pre fibrillar phase is mainly controlled by a simple coagulation-evaporation kinetic mechanism, in which concentration acts as a critical parameter. These experimental facts, along with the kinetic model used, suggest a critical role for thermal concentration fluctuations in the process of fibril nucleation. (literal)
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