Figure 5

Schematic representation of the aggregation. A) Dynamic of the aggregation. GFP-GST aggregates progressively form both soluble and insoluble aggregates. Chaperone activity can reverse the process of aggregation in a way that is inversely proportional to the degree of complexity reached by the aggregates and could also play a role in the aggregate maturation towards more structured complexes. B) Aggregate model. The aggregation of GFP-GST probably starts with misfolded single proteins that collapse into pre-fibrillar structures. These catalyze the aggregation of new molecules to form larger amyloid fibrils. In the initial phases, the co-presence of molecules with different degree of misfolding and amyloidation seems apparent. Pre-fibrils could form the core of the aggregation seeds to which partially misfolded GFP-GST molecules bind. Some of these still conserve a native-like structure compatible with fluorescence functionality. The aggregation nets can trap other proteins in a probably non-specific manner.