Entrapment of A beta sub(1-40) peptide in unstructured aggregates

Recognizing 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 pro...

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Published inJournal of physics. Condensed matter Vol. 24; no. 24; pp. 1 - 7
Main Authors Corsale, C, Carrotta, R, Mangione, M R, Vilasi, S, Provenzano, A, Cavallaro, G, Bulone, D, San Biagio, P L
Format Journal Article
LanguageEnglish
Published 20.06.2012
Subjects
Agglomeration
Aggregates
Condensed matter
Imaging
Light scattering
Monitors
Pathways
Peptides
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Summary:Recognizing 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 beta -peptide dissolved in a pH 7.4 solution at small peptide concentration and low ionic strength forms globular aggregates without typical amyloid beta -confonnation. 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.
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ISSN:0953-8984
1361-648X
DOI:10.1088/0953-8984/24/24/244103