Gebäude E 8.1 (HIPS), Seminarraum EG (0.27), 66123 Saarbrücken
Proteases and protease-like enzymes are ubiquitous in all aspects of life and have thus been established as therapeutic targets for various diseases, such as cancer, hypertension, thrombosis, diabetes, as well as viral and bacterial infections. Notably, a substantial number of pharmaceutically relevant protease inhibitors have been developed or at least been inspired by natural products. A frequent structural feature of protease inhibitors from nature is the presence of warheads that mediate their specific binding to the active site of target enzymes and may allow mechanism-based inhibition. Warheads often consist of electrophilic groups, which are prone to being attacked by nucleophilic residues, generating covalent adducts. Such moieties include β-lactones, Michael systems, epoxyketones, etc. Metalloproteinase inhibitors may contain hydroxamate or phosphoramidate groups that facilitate chelation of active site metal ions. These warheads are not only interesting from a pharmacological perspective but often also represent fascinating subjects to study new biosynthetic principles. In my talk, I will discuss our recent progress to investigate key reactions in the biological formation of protease inhibitors from bacterial sources. The potential to apply this information for genome mining and bioengineering approaches will be discussed.
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Professor Dr. Alexandra K. Kiemer
Vorsitzende der DPhG Landesgruppe Saar
