Veronika Ehmke


PhD Student


HCI G-312


+41-44-633 4169


Veronika Ehmke



Study of Chemistry at Ludwig-Maximilians-University (LMU) Munich, Germany


Research Exchange with Prof. P. Sadler at University of Edinburgh, UK


Bachelor thesis with Prof. T. Carell at LMU Munich


Master thesis with Prof. T. Carell at LMU Munich

since 2009:

PhD with Prof. F. Diederich at ETH Zurich


Structure-Based Design and Synthesis of Nonpeptidic Inhibitors for the Antimalarial Target Falcipain-2

Malaria, a life-threatening disease caused by Plasmodium parasites, kills each year more than one million people and more than 500 million clinical cases are registered. The recent emergence of multi-drug resistant strains of Plasmodium falciparum, the parasite that causes the most dangerous form of malaria to humans, demands the urgent development of new therapeutic agents with novel modes of action. During their stay in the human body, the parasites infect erythrocytes and catabolize hemoglobin to provide nutrients for their own growth and maturation. In the hemoglobin degradation process parasitic cysteine proteases, the Falcipains, are involved. As this catabolism is vital for parasitic survival, inhibition of this class of proteases offers a valid approach to potential new antimalarials. The main objective of this project is the detailed exploration of the active site binding properties of Falcipain-2 by structure-based design and synthesis of new inhibitors. Non-mechanism-based inhibitors that are nonpeptidic and highly selective towards related human enzymes as well as towards serine proteases are targeted.


K. Gutsmiedl, C. T. Wirges, V. Ehmke, T. Carell, Org. Lett. 2009, 11, 2405-2408. Copper-Free "Click" Modification of DNA via Nitrile Oxide-Norbornene 1,3-Dipolar Cycloaddition.

V. Ehmke, C. Heindl, M. Rottmann, C. Freymond, W. B. Schweizer, R. Brun, A. Stich, T. Schirmeister, F. Diederich, ChemMedChem 2011, 6, 273-278. Potent and Selective Inhibition of Cysteine Proteases from Plasmodium falciparum and Trypanosoma brucei.

V. Ehmke, F. Kilchmann, C. Heindl, K. Cui, J. Huang, T. Schirmeister, F. Diederich, Med. Chem. Commun. 2011, 2, 800-804. Peptidomimetic Nitriles as Selective Inhibitors of the Malarial Cysteine Protease Falcipain-2.

M. Vrabel, E. Kaya, S. Prill, V. Ehmke, T. Carell, Collect. Czech. Chem. Commun. 2011, 76, 1089-1101. Optimization of the Posttranslational Click Modification of Proteins.

V. Ehmke, J. E. Q. Quinsaat, P. Rivera-Fuentes, C. Heindl, C. Freymond, M. Rottmann, R. Brun, T. Schirmeister, F. Diederich, Org. Biomol. Chem. 2012, 10, 5764-5768. Tuning and Predicting Biological Affinity: Aryl Nitriles as Cysteine Protease Inhibitors.

V. Aureggi, V. Ehmke, J. Wieland, W. B. Schweizer, B. Bernet, D. Bur, S. Meyer, M. Rottmann, C. Freymond, R. Brun, B. Breit, F. Diederich, Chem. Eur. J. 2012, DOI: 10.1002/chem.201202941. Potent Inhibitors of Malarial Aspartic Proteases, the Plasmepsins, by Hydroformylation of Substituted 7-Azanorbornenes.

Last update: Nov. 2012