RESEARCH - D. Kümmel

Biochemistry

and Structural biology

 

Inhibitor and protein design

X-ray crystallography is valuable tools for drug design and development as well as protein engineering for the improvement of biological research tools and biotechnology applications. We have several ongoing collaboration projects addressing these issues, including recently the structure determination of a snake toxin (α-corbatoxin, which inhibits the nicotinic acetylcholine receptor) bound to a peptide inhibitor identified by phage display. We are also part of a study for the development of an antibiotic targeting an essential enzyme in Mycobacterium tuberculosis, also involving the use crystallographic fragment screening. In addition, we have crystallized optimized proteins for biorthogonal labeling strategies as well as enzymes with an altered substrate spectrum with the goal to provide structural information for further development based on rational design.

 

Lynagh et al. (2020)
Peptide Inhibitors of the α-Cobratoxin-Nicotinic Acetylcholine Receptor Interaction.
J Med Chem doi: 10.1021/acs.jmedchem.0c01202

Michailidou et al. (2020)
Engineered SAM Synthetases for Enzymatic Generation of AdoMet Analogs with Photocaging Groups and Reversible DNA Modification in Cascade Reactions.
Angew Chem Int Ed Engl doi: 10.1002/anie.202012623