Amyloid-type Protein Aggregation
The research group "Amyloid-type Protein Aggregation" investigates how amyloid protein aggregates are formed, how they proliferate in a prion-like manner and how they damage synapses and neurons. Of course, we are also investigating how amyloid aggregates can be targeted and directly disassembled back into functional monomers with highly specific drug candidates.
Amyloid-type protein aggregation is crucial in all protein misfolding diseases. In particular, neurodegenerative diseases are triggered and driven by it. How primary nucleation leads to the first elongation- and proliferation-capable amyloid oligomers is still not fully understood. The growth of amyloid fibrils is already quite conceivable, but especially in the case of intracellular amyloids, e.g. α-Syn, TDP43 and Tau, it is not yet understood how they spread from cell to cell. It is completely unclear what exactly causes the toxicity of amyloids. Investigating and understanding all this is the focus of the research group. This also includes the elucidation of mechanisms that our body has developed in the course of evolution against amyloids and their toxic effects. Equally in focus is the development of drug candidates that reverse amyloid aggregation and restore function to the monomeric proteins released as a result.
Prof. Dr. Dieter Willbold
Building 05.8v / Room 3028
All atomic-resolution methods in structural biology:
- JuStruct (Jülich Center for Structural Biology)
- Bio-molecular NMR Center
- cryo-EM in the Ernst Ruszka Center (ERC, ERC 2.0)
- transgenic animal models in the animal house