Montag, 20. November 2017, 16:30 - 18:00 iCal

Mag. Dr. Roman Lichtenecker

Institut für Organische Chemie der Fakultät für Chemie, Universität Wien

"Methods from the organic chemistry toolbox to study the characteristics of peptides and proteins"

Carl Auer v. Welsbach Hörsaal der Fakultät für Chemie
Boltzmanngasse 1, 1090 Wien


Methods from the organic chemistry toolbox to study the characteristics of peptides and proteins


The structure and interplay of macromolecules determines the cell’s proliferation, development, function and fate. A deep understanding of their complex conformational properties and interaction networks represents the key issue to unravel the principles of life at a molecular level. Only if the roles of the single nodes in e.g. protein signal cascades or metabolic networks are known and the interaction mechanisms understood, subtle changes leading to pathogenic progression and disease development can be addressed by developing non-endogenous therapeutic compounds. NMR spectroscopy is the method of choice to characterize protein structure and investigate macromolecular interaction at atomic resolution. In contrast to X-ray crystallography, the NMR approach allows to image the highly dynamic properties of protein samples under conditions, which resemble their natural cellular environment. However, NMR investigation of large macromolecules is limited by sensitivity and resolution issues. Data acquisition and interpretation are still time consuming processes and sample preparation is often associated with high costs. In the last two decades, protein NMR underwent an impressive evolution to overcome these drawbacks. This process was driven by novel isotope labelling techniques in order to produce protein samples with defined patterns of 13C, 15N and 2H. In part one of the presentation, our recent research on a toolbox of isotope labelled compounds will be presented, which are metabolized to the corresponding amino acids using in-vivo protein overexpression systems. Our efforts to establish novel techniques of selective Val-, Leu-, Phe-, Tyr-, Trp- and His-residue labelling will be described. The resulting protein samples provide isotope patterns which are tailored to the needs of diverse NMR experiments and are currently applied by our cooperation partners to elucidate the structures of large protein complexes, investigate sparsely-populated high energy conformations or guide drug-development processes.

Part two of the presentation will describe the interesting structural topologies of D/L-peptides (peptides with alternating stereochemistry in their amino acid building blocks). We applied thiol-tags to control the conformational promiscuity of this compound class in a dynamic combinatorial fashion. Additionally, we identified antimicrobial representatives via directed compound library design and characterized their properties and mode of action.


Fakultät für Chemie


Brigitte Schwarz
Fakultät für Chemie der Universität Wien