|Univ.-Prof. Dr. Hans Brandstetter
|Dr. Esther Schönauer
|Biochemical and structural characterization of bacterial collagenases
In my dissertation I am working on bacterial collagenases, in particular collagenases from Clostridium histolyticum and the extremophilic Bacillus cereus strain Q1.
Because of its unusual triple-helical structure and very high proline and hydroxyproline content, collagen – the most abundant protein in mammals and a main component of the extracellular matrix – is a protein of remarkable tensile strength and proteolytic stability. In contrast to most proteases bacterial collagenases are highly efficient at digesting collagen. As such they are of interest for various biotechnological and medical applications, but also represent interesting drug targets. However, the mechanism behind bacterial collagenolysis has remained elusive.
We aim at elucidating the structure-function relationship of these enzymes using recombinantly expressed wildtype and chimeric collagenases for detailed biochemical and structural analyses.