Peptide Lipid Interaction / Peptide Transport (M. Dathe/J. Oehlke)

The Dathe/ Oehlke group is interested in the structural requirements of peptides as uptake-promoting and targeting tools for attached cargos and lipid-based carriers. Furthermore, we look at the role of the lipid matrix in mediating transmembrane transport and in modulating the selectivity of membrane lytic peptides. Our strategy has been to undertake a comparative investigation of cellular uptake and biological activity of a model cargo (PNA) conjugated with cell-penetrating peptides and derivatives thereof showing systematically altered structural properties.

Mass Spectrometry (E. Krause)

Mass spectrometry is a key technology in proteome research. Our research group focuses on the elucidation of functionally important proteins and their post-translational modifications using electrospray ionisation (ESI) and matrix-assisted laser desorption/ionisation (MALDI) mass spectrometry in combination with miniaturized separation techniques and stable isotope labelling. These methods have allowed us to study protein-protein interactions which play important roles in processes such as T-cell signalling and the assembly of spliceosomes.

Synthetic Organic Biochemistry (V. Hagen)

Our research focuses on the design of photoremovable protecting groups and the synthesis, characterisation and application of photoactivatable biomolecules so-called caged compounds. Caged compounds are used as tools in studies of rapid cellular processes and their precise resolution in time and space.

Medicinal Chemistry (J. Rademann)

We develop strategies in the areas of synthetic organic chemistry, library design, and bioassays. Most protein targets of the group are disease-related enzymes including proteases and phosphatases relevant to clinical indications including cancer, Alzheimer, tuberculosis, and SARS. Recently, the targeted proteins have been extended towards receptors and protein-protein interactions.

Biophysics of Membrane Proteins (S. Keller)

We are interested in the mechanisms of folding and reconstitution of polytopic a-helical membrane proteins (such as receptors and channels) as well as of protein–protein and protein–ligand interactions. We use a range of biophysical methods (in particular, spectroscopy and calorimetry) to examine the thermodynamics and kinetics of this pharmacologically relevant class of proteins and their interactions with small molecules.

Protein Chemistry (D. Schwarzer)

Our group is developing chemical tools to study the physiological function of posttranslational protein modifications. A central goal is the development of probes that serve as baits to trap, isolate and identify modification-specific binding proteins.