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Amyloid Fibrils Formation of Concanavalin A at Basic pH

Mechanisms of partial unfolding and aggregation of proteins are of extreme interest in view of the fact that several human pathologies are characterized by the formation and deposition of protein-insoluble material, mainly composed of amyloid fibrils. Here we report on an experimental study on the heat-induced aggregation mechanisms, at basic pH, of concanavalin A (ConA), used as a model system. Thioflavin T (ThT) fluorescence and multiangle light scattering allowed us to detect different intertwined steps in the formation of ConA aggregates. In particular, the ThT fluorescence increase, observed in the first phase of aggregation, reveals the formation of intermolecular β-sheet structure which constitutes a rate-limiting step of the process. The intertwining between the formation of β-aggregate structures and the whole aggregation process is discussed as a function of protein concentration: a coagulation process produces the same kind of aggregates at the different concentrations studied. Multiangle light...

Authors:   R. Carrotta; V. Vetri; F. Librizzi; V. Martorana; V. Militello; M. Leone; R. Carrotta; V. Vetri; F. Librizzi; V. Martorana; V. Militello
Journal:   Journal of Physical Chemistry B
Year:   2011
DOI:   10.1021/jp1042409
Publication date:   10-Mar-2011
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