RUB-Researchers from the Chair for Biophysics have developed a new method for the detailed study of the interaction between pharmaceuticals and their target proteins. The pharmaceutical industry has already taken notice of the new infrared spectroscopy technique; the method is supposed to be implemented to investigate pharmacological agent-protein interactions in the EU project K4DD, which is supported by various major European pharmaceutical companies. "We now have a tool in our hands with which we can research the dynamics of pharmacologically interesting proteins in atomic detail," Prof. Dr. Klaus Gerwert said. "We want to undertake a targeted screening of substance libraries to look for potential pharmacological agents." PD Dr. Carsten Ktting added that "with our technique future pharmaceuticals can be more closely tailored to illness-causing proteins, which can noticeably reduce the negative side effects of these drugs." They described the new method together with Dr. Jrn Gldenhaupt and Philipp Pinkerneil in the scientific journal ChemPhysChem, which dedicated its cover story to this topic.
The new method: from three to one
With infrared difference spectroscopy, researchers follow dynamic processes in proteins. For a long time, these processes could only be observed in light-activated proteins, but not in proteins that are activated by binding with ligands but this is usually how many illness relevant molecules are activated. To analyze the dynamics of such proteins, researchers have to fasten them to the measurement surface and pour a pharmacological-substance over them; the proteins can then interact with and be activated by this substance. Even though this binding technique is possible, it cannot be used for all proteins. The RUB-Team worked around this problem by combining infrared (IR) spectroscopy with a surface-sensitive technique (attenuated total reflectance) and so-called "His-Tagging" (anchoring proteins to the
|Contact: Prof. Dr. Klaus Gerwert|