The formation of insoluble amyloid deposits by protein fibrillogenesis is a common hallmark of many neurodegenerative diseases such as Alzheimer's or Parkinson's disease. In cooperation with Prof. B. Koksch (Institute of Chemistry and Biochemistry at the Freie Universität Berlin) simple peptide systems are structurally characterized which are designed to model the conformational transition that is responsible for the formation of amyloids.
Cooperation with Prof. B. Koksch (FU Berlin)
K. Pagel, T. Seri, H. v. Berlepsch, J. Griebel, R. Kirmse, C. Böttcher and B. Koksch (2008)
How metal ions affect amyloid formation: Cu2+- and Zn2+-sensitive peptides
Chem. Bio. Chem. 9, 531 - 536.
K. Pagel, S. C. Wagner, R. R. Araghi, H v. Berlepsch, C. Böttcher and B. Koksch (2008)
Intramolecular Charge Interactions as a Tool to Control the Coiled-Coil-to-Amyloid Transformation
Chem. Eur. J. 14, 11442 - 11451.
S. C. Wagner, M. Roskamp, H. Cölfen, C. Böttcher, S. Schlecht and B. Koksch (2009)
Switchable electrostatic interactions between gold nanoparticles and coiled coil peptides direct colloid assembly
Org. Biomol. Chem. 7, 46 - 51.
H. v. Berlepsch, E. Brandenburg, B. Koksch and C. Böttcher (2010)
Peptide Adsorption to Cyanine Dye Aggregates Revealed by Cryo-Transmission Electron Microscopy
Langmuir 26 (13), 11452 - 11460.