This news release is available in German.
Proteins are made up of a chain of amino acids and are vital for all cell processes. Proteases are among the most important types of protein. Like "molecular scissors", they cut other proteins at given positions and thereby execute important cell functions. By cutting the amino acid chains to the right length or breaking proteins apart they, for example, activate or deactivate proteins, decompose defective ones or switch signal sequences that serve to transport proteins to their proper position within a cell.
But proteases are important not only for human cells bacteria also rely on them. There are hardly any effective antibiotics left in the fight against pathogens like multi-resistant strains of Staphylococcus aureus bacteria or Mycobacterium tuberculosis which causes tuberculosis.
Researchers around the world are thus working ardently to find new ways of disarming the proteases in these strains to combat them. At the heart of this effort lies the so-called ClpP protease. It comprises 14 subunits and has a central regulatory function. The usual approach to deactivating this protease is to block all active centers of the ClpP. These are effectively the "cutting edges of the scissors", i.e. the portions of the protein that are responsible for breaking apart other proteins.
"However, the inhibitors used in the past have one decisive disadvantage," explains Stephan Sieber who heads the Chair for Organic Chemistry II at the Technische Universitaet Muenchen (TUM). "They don't permanently disarm the proteins, but only work for a few hours. On top of that, to be effective they must attack all active centers of the protein."
New strategies against bacteria
In collaboration with
|Contact: Dr. Andreas Battenberg|
Technische Universitaet Muenchen