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1 Dipartimento di Scienze Fisiche e Astronomiche dellUniversità di Palermo, 90123 Palermo, Italy
2 Consiglio Nazionale delle RicercheIstituto Nazionale per la Fisica della Materia
3 Niels Bohr Institute, 2100 Copenhagen, Denmark
(RECEIVED July 11, 2005; FINAL REVISION September 21, 2005; ACCEPTED September 27, 2005)
When subjected to acidic conditions and high temperature, insulin is known to produce fibrils that display the common properties of disease amyloids. Thus, clarifying the mechanisms of insulin fibrillation can help the general understanding of amyloidal aggregation. Insulin fibrillation exhibits a very sharp time dependence, with a pronounced lag phase and subsequent explosive growth of amyloidal aggregates. Here we show that the initial stages of this process can be well described by exponential growth of the fibrillated proteins. This indicates that the process is mainly controlled by a secondary nucleation pathway.
Keywords: insulin; protein aggregation; amyloids; nucleation; Thioflavin T; fluorescence
Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051692305.
Reprint requests to: Fabio Librizzi, Dipartimento di Scienze Fisiche e Astronomiche, Via Archirafi 36, 90123 Palermo, Italy; e-mail: librizzi{at}fisica.unipa.it; fax: +39-091-6234281.
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M. Manno, E. F. Craparo, V. Martorana, D. Bulone, and P. L. San Biagio Kinetics of Insulin Aggregation: Disentanglement of Amyloid Fibrillation from Large-Size Cluster Formation Biophys. J., June 15, 2006; 90(12): 4585 - 4591. [Abstract] [Full Text] [PDF] |
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