Exploring methods for the creation of new-to-nature antimicrobials
Introduction to my research
My research revolves around the recombination and heterologous expression of post-translationally modified peptides. Prokaryotes lack cell-organelles to modify proteins after they have been expressed, but modification still occurs. Small proteins are sometimes modified by dedicated enzymes that can install a wide range of modifications upon recognition of an N-terminal signal sequence, i.e. leader peptide. These modifications are of great significance as they can be necessary to make the peptide biologically active, like making it an active antibiotic. By making different combinations of modification enzymes and substrates (peptides), I hope to learn more about new modification enzymes and implement them to make new-to-nature peptides with anti-microbial activity.
The classes of post-translationally modified peptides I work with are Sactipeptides and Class II Lanthipeptides. Bachelor and Master projects I can offer include work on the previously mentioned goals, or parts thereof. The projects can include the design and performing of
- Molecular cloning (genetically modifying bacteria; Lactococcus lactis, Escherichia coli)
- Protein work (expression and purification of peptides)
- Mass spectrometry and data-analysis
- Activity testing of created potentially antibiotic compounds