University of Connecticut |
Education: M.Sc., Biozentrum University of Basel; PhD, Sandoz Pharma AG & University of Basel Research Interests: Our lab is working on the structure - based rational design of small proteins that are able to self-assemble into nanoparticles with icosahedral symmetry. We are investigating the biophysical properties and the medical applications of such nanoparticles. Functionalized nanoparticles are being designed for as drug targeting and delivery systems. Synthetic vaccines are being developed by using these nanoparticles as repetitive antigen display systems. Selected Publications:
Stetefeld, J., Jenny, M., and Burkhard, P. (2006). Intersubunit signaling inglutamate-1-semialdehyde-aminomutase. PNAS, 103 (37), 13688-13693 Raman, S.K., Machaidze, G., Lustig, A., Aebi, U. and Burkhard, P. (2006). Structure-based design of peptides that self-assemble into regular polyhedral nanoparticles. Nanomedicine, 2 (2), 95-102 Strelkov, S., Herrmann, H., Geisler, N., Zimbelmann, R., Aebi, U. and Burkhard, P. (2002). Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. EMBO J, 21 (6), 1255-1266.Burkhard, P., Dominici, P., Borri-Voltattorni, C., Jansonius, J.N., & Malashkevich, V.N. (2001). Structural insight into Parkinson's disease treatment gained from drug-inhibited DOPA decarboxylase. Nature Struct Biol, 8 (11), 963 - 967. Meier, M., Janosik, M., Kery, V., Kraus, J. & Burkhard, P. (2001). Structure of human cystathionine b-synthase: A unique pyridoxal 5'-phosphate dependent hemeprotein. EMBO J, 20 (15), 3910-3916. Burkhard, P., Stetefeld, J. & Strelkov, S. (2001). Coiled coils: a highly versatile protein folding motif. Trends in Cell Biology, 11, 82-88. Burkhard, P., Meier, M. & Lustig, A. (2000). Design of a minimal protein oligomerization domain, a structural approach. Protein Science, 9, 2294-2301. |
