Carbon dots as tools to monitor protein aggregation in conformational diseases

The possibility to monitor peptides and proteins aggregation is of paramount importance in the so-called conformational diseases, as the understanding of many physiological pathways, as well as pathological processes involved in the development of such diseases, depends very much on the actual possibility to monitor biomolecules oligomeric distribution and aggregation. In this thesis, a novel experimental method to monitor protein aggregation, based on the change of fluorescent properties of carbon dots upon protein binding will be developed. The results obtained in the case of insulin with this newly proposed experimental approach have already been recently published, but the method needs to be improved and tested on several other aggregation-prone proteins such as amyloid beta peptides and tau protein. The greatest advantage of the hereby presented methodology over all the other experimental methods considered is the possibility to monitor the initial stages of protein aggregation at the different experimental conditions sampled and the absence of possible disturbances and-or molecular probes during the aggregation process.