Secondary nucleation and accessible surface in insulin amyloid fibril formation.

Maurizio Leone, Minna Groenning, Vito Foderà, Marco Van De Weert, Maurizio Leone, Fabio Librizzi

Risultato della ricerca: Article

102 Citazioni (Scopus)

Abstract

At low pH insulin is highly prone to self-assembly into amyloid fibrils. The process has been proposed to beaffected by the existence of secondary nucleation pathways, in which already formed fibrils are able to catalyzethe formation of new fibrils. In this work, we studied the fibrillation process of human insulin in a widerange of protein concentrations. Thioflavin T fluorescence was used for its ability to selectively detect amyloidfibrils, by mechanisms that involve the interaction between the dye and the accessible surface of the fibrils.Our results show that the rate of fibrillation and the Thioflavin T fluorescence intensity saturate at highprotein concentration and that, surprisingly, the two parameters are proportional to each other. BecauseThioflavin T fluorescence is likely to depend on the accessible surface of the fibrils, we suggest that theoverall fibrillation kinetics is mainly governed by the accessible surface, through secondary nucleationmechanisms. Moreover, a statistical study of the fibrillation kinetics suggests that the early stages of theprocess are affected by stochastic nucleation events.
Lingua originaleEnglish
pagine (da-a)3853-3858
Numero di pagine6
RivistaJOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL
Volume112
Stato di pubblicazionePublished - 2008

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

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