Abteilung Physikalische Biotechnologie
Overview
We use X-ray crystallography to study protein function at the atomic level. Our main interests lie in the field of "rational drug design", where we try to fuse the experimental structural data and thermodynamic measurements of protein ligand interactions in a computational framework to advance the drug discovery process.
New techniques in drug discovery are essential for the fast and efficient development of novel innovative drugs to deal with the challenges of the future. Structure determinations of various members of serine proteinases have provided a basis for computer-based drug design within this class of enzymes. In many proteins of interest, however, this course is blocked through a lack of suitable crystals.
As a strategy for circumventing such problems, we are investigating the use of surrogate proteins for studying protein-ligand interactions. To test the feasibility of this approach, we have chosen bovine trypsin as a scaffold to reconstruct the ligand binding site of factor Xa .
The simple modular design of trypsin, its readiness to crystallise and straightforward handling lends itself to such drug design by proxy.