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Dr. Stefan Bossmann

 

Professor

M.S., University of Saarland, Germany (1988)
Ph.D., University of Saarland, Germany (1991)
Postdoctoral Research Fellow, Columbia University (1991-3)
Professor, University of Karlsruhe (1993-2004)

Email: sbossman@ksu.edu
Office Phone: 785-532-6817
Lab Phone: 785-532-3090
Fax: 785-532-6666

Bossmann Group

 

 

My complete response to the TB discussion started on 9.11.2007 in the Kansas State Collegian - What's the Matter with Tuberculosis.pdf (click to read)

Research Overview

My research projects explore the unique physical and chemical properties of channel proteins (porins) isolated from Mycobacterium smegmatis (MspA) and Mycobacterium tuberculosis. It is noteworthy that tuberculosis is the infectious disease with the highest number of casualties worldwide. Due to the steadily developing resistance against most of the antibiotics employed for the treatment of tuberculosis, new strategies for the delivery of drugs are urgently needed.

MspA-Nanopore as seen by Electron Micrography

My research in this area will be concerned with:
• The understanding of the working principles of porin channels in natural (membrane) and artificial (electrodes) environments.
• The use of porins as tools for the developments of functional nanostructures.
• The development of a transport vector through the mycobacterial membrane.
• The use of water-soluble, hydrophobic copolymers as artificial matrices for MspA.
• And finally: the development of supramolecular model systems, which serve as physical models for the biological function of the porin systems.

Molecular Machines

Molecular Machines
The distinct chemical stability and geometric dimensions of the porin from Mycobacterium smegmatis (MspA) make it the ideal bio-component of supramolecular transistors and machines. Principally, various systems can be built, using the requirements of future applications. The development of supramolecular and molecular assemblies using MspA as a vital component will make use of MspA-mutants possessing cysteine-units at defined positions. The connection between the MspA-mutant with nano-gold-particles will be achieved by means of the chemical reaction of the thiol-groups from the four cysteine units with the gold surface. The hydrophilic interior of the canal favors the binding of mechanically linked ruthenium-polypyridyl-bis-viologen-cathenanes within the porin structure.

MspA-Nanochannels on MICA as detected by AFM

Selected Publications

Hu, Y.-Z.; Bossmann, S. H.; Loyen, D. v.; Schwarz, O.; Dürr, H.; Huch, V.; Veith, M. A Novel 2,2 -Bipyridine[2]catenane and its Ruthenium Complex: Synthesis, Structure and Intramolecular Electron Transfer, J. Am. Chem. Soc. 1998, 120, 5822-5823.

Niederweis, M., Heinz, Ch.; Janik, K.; Bossmann, S. H. Nanostructuring by Deposition of Protein Channels Formed on Carbon Surfaces, Nano Letters 2002, 2, 1206-1210.

Bossmann, S. H.; Janik, K.; Pokhrel, M. R.; Heinz, C.; Niederweis, M. Reconstitution of the Porin from Mycobacterium smegmatis at HOPG Covered with Hydrophobic Host Layers, Surf. Interface Anal. 2004, 36, 127-134.

Hong Kong Symposium in Honour of Prof. Po Lock Yue