The mad cow disease on the trail
Dr. Kai Schlepckow in the working group of Prof. Harald Schwalbe at the Goethe University succeeded for the first time in gaining detailed insights into the formation mechanism of oligomers of the prion protein. “For every single amino acid, we were able to trace at what point in time it intervened in the aggregation process. This process is much more complex than previously thought, ”reports Prof. Schwalbe. This information is of vital importance because without it it will not be possible to develop therapeutics that prevent the formation of infectious particles.
With the aid of nuclear magnetic resonance spectroscopy (NMR) spectroscopy, the process of oligomerization could be followed with atomic resolution. In this way it was possible to examine different areas of the prion protein molecule on their specific contributions to the oligomerization. "We were intrigued to see that the molecules do not behave uniformly during the oligomerization. Rather, various molecular regions are involved in different sections of this process. Thus, we the formation mechanism of oligomers of the prion protein with unprecedented accuracy describe, "says Dr. Schlepckow together the results of the study, which was recently described as Very Important Paper in the prestigious journal Angewandte Chemie published.
Publication:
Kai Schlepckow and Harald Schwalbe: Molecular Mechanism of prion protein Oligomerization at Atomic Resolution, Angew Chem Int Ed Engl 2013.
http://dx.doi.org/10.1002/ange.201305184
http://dx.doi.org/10.1002/anie.201305184
Source: Frankfurt [Goethe University]