A protein’s three-dimensional structure is crucial for its biological function. Exploring of how the protein sequence and posttranslational modifications determine the structure is fundamental to an improved understanding of the mechanisms of protein folding and misfolding. Beyond that, this knowledge can be used to design new peptides and proteins with novel structures and functions.
The research of the Thomas group is centered around this key problem. Firstly, we use de novo designed peptide components to create peptide scaffolds with catalytic activity and novel peptide materials. We focus on small well-characterized self-assembling and reliably folding peptides which can be accessed by chemical synthesis. This facilitates chemical modifications, a requirement for adding function. To achieve our goal, we will test available peptide designs and adapt them for our purposes. Furthermore, we will design and characterize new peptide building blocks, and finally we will develop modular design strategies to head towards functional devices. A second research area is focused on studying aggregation mechanisms of proteins, which are relevant in neurodegenerative diseases such as the amyotrophic lateral sclerosis. Based on our findings, we plan to design small molecules and peptides which will inhibit the aggregation processes.