Abstract
| Lingua originale | English |
|---|---|
| pagine (da-a) | 10830-10837 |
| Numero di pagine | 8 |
| Rivista | JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL |
| Volume | 113 |
| Stato di pubblicazione | Published - 2009 |
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All Science Journal Classification (ASJC) codes
- Physical and Theoretical Chemistry
- Materials Chemistry
- Surfaces, Coatings and Films
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Self-Organization Pathways and Spatial Heterogeneity in Insulin Amyloid Fibril Formation. / Leone, Maurizio; Pignataro, Bruno Giuseppe; Librizzi, Fabio; Cataldo, Sebastiano; Foderà, Vito.
In: JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL, Vol. 113, 2009, pag. 10830-10837.Risultato della ricerca: Article
}
TY - JOUR
T1 - Self-Organization Pathways and Spatial Heterogeneity in Insulin Amyloid Fibril Formation
AU - Leone, Maurizio
AU - Pignataro, Bruno Giuseppe
AU - Librizzi, Fabio
AU - Cataldo, Sebastiano
AU - Foderà, Vito
PY - 2009
Y1 - 2009
N2 - At high temperature and low pH, the protein hormone insulin is highly prone to form amyloid fibrils, and for this reason it is widely used as a model system to study fibril formation mechanisms. In this work, we focused on insulin aggregation mechanisms occurring in HCl solutions (pH 1.6) at 60 °C. By means of in situ Thioflavin T (ThT) staining, the kinetics profiles were characterized as a function of the protein concentration, and two concurrent aggregation pathways were pointed out, being concentration dependent. In correspondence to these pathways, different morphologies of self-assembled protein molecules were detected by atomic force microscopy images also evidencing the presence of secondary nucleation processes as a peculiar mechanism for insulin fibrillation. Moreover, combining ThT fluorescence and light scattering, the early stages of the process were analyzed in the low concentration regime, pointing out a pronounced spatial heterogeneity in the formation of the first stable fibrils in solution and the onset of the secondary nucleation pathways.
AB - At high temperature and low pH, the protein hormone insulin is highly prone to form amyloid fibrils, and for this reason it is widely used as a model system to study fibril formation mechanisms. In this work, we focused on insulin aggregation mechanisms occurring in HCl solutions (pH 1.6) at 60 °C. By means of in situ Thioflavin T (ThT) staining, the kinetics profiles were characterized as a function of the protein concentration, and two concurrent aggregation pathways were pointed out, being concentration dependent. In correspondence to these pathways, different morphologies of self-assembled protein molecules were detected by atomic force microscopy images also evidencing the presence of secondary nucleation processes as a peculiar mechanism for insulin fibrillation. Moreover, combining ThT fluorescence and light scattering, the early stages of the process were analyzed in the low concentration regime, pointing out a pronounced spatial heterogeneity in the formation of the first stable fibrils in solution and the onset of the secondary nucleation pathways.
UR - http://hdl.handle.net/10447/36316
M3 - Article
VL - 113
SP - 10830
EP - 10837
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
SN - 1520-6106
ER -