Protein-based drugs are widely used for therapeutic treatments. Protein drugs can show a higher specificity and lower toxicity than small molecule drugs, like Aspirin or Diazepam. However, protein drugs show a lower stability and are more affected by external stress factors such as higher temperature. One option to improve the stability of protein drugs is the optimization of the formulation i.e. the conditions in which they are stored. This process is specific for each protein and therefore time consuming and costly. My PhD project was part of a bigger project, called ‘Protein-excipient Interaction and Protein-Protein Interaction in formulation’ (PIPPI).
Within this project we had the goal to characterize different kinds of protein drugs in a systematic way and develop a public database, which everyone can access. This can serve as a starting point for future protein drug development. My project specializes on the combination of many different biophysical techniques to rationally select conditions where a protein is stable and thus active as a therapeutic. A special focus of my project was how changes in the protein structure affect the likelihood of protein-protein interactions, which can lead to aggregation and thus loss of protein function.
