Anno2012
AutoriCorsale C; Carrotta R; Mangione MR; Vilasi S; Provenzano A; Cavallaro G; Bulone D; San Biagio PL
AbstractRecognizing the complexity of the fibrillogenesis process provides a solid ground for the development of therapeutic strategies aimed at preventing or inhibiting protein-protein aggregation. Under this perspective, it is meaningful to identify the possible aggregation pathways and their relative products. We found that A?-peptide dissolved in a pH 7.4 solution at small peptide concentration and low ionic strength forms globular aggregates without typical amyloid ?-conformation. ThT binding kinetics was used to monitor aggregate formation. Circular dichroism spectroscopy, AFM imaging, static and dynamic light scattering were used for structural and morphological characterization of the aggregates. They appear stable or at least metastable with respect to fiber growth, therefore appearing as an incidental product in the pathway of fibrillogenesis.
RivistaJournal Of Physics. Condensed Matter
ISSN0953-8984
Impact factor
Volume24
Pagina inizio
Pagina fine244103
Autori IBFDonatella BULONE, Pier Luigi SAN BIAGIO, Rita CARROTTA, Maria Rosalia MANGIONE, Alessia PROVENZANO, Silvia VILASI
Linee di Ricerca IBFMD.P01.002.001
Sedi IBFIBF.PA