In the last decades protein drug formulations have become a field of emerging interest. Unfortunately, proteins have the tendency to form aggregates and lose their bioactivity in the process. In some cases the formation of aggregates has also been associated with toxicity. Therefore techniques and strategies to a) prevent protein formulations from aggregation and b) analyze formulations in order to recognize aggregation are essential. A known technique to analyze protein aggregation is fluorescence spectroscopy. Aggregated proteins often show a different fluoroscopic spectrum than in their native state. Furthermore, the use of extrinsic fluorescent dyes can reveal additional information about the Protein structure. We propose here a project in which the student will be working with a commercially available protein (e.g., lysozyme) and apply different stressors like heat, pH, ionic strength, to it, which are known to cause proteins to aggregate. He will also use trp-PEG in order to examine if it is possible to prevent lysozyme from aggregation. Afterwards he would analyze the proteins with fluorometric methods and determine the extent and nature of the aggregation. PARTIE EXPERIMENTALE