Thermodynamic and kinetic insights into the formation of amyloid
About
In vitro and ex vivo studies on the mechanism of amyloid formation using biophysical methods
Research Topics
- Protein-protein and protein-ligand interaction
- Alzheimer’s disease
- AL amyloidosis
- Transmissible spongiform encephalopathy
Our team works in the field of pathological protein aggregation. In a number of neurodegenerative diseases, protein deposits in the brain, either intra- or extracellular, are an important pathological feature. These deposits often contain protein in a specific, β-sheet-rich conformation called amyloid. The following questions are in the foreground for us: How are amyloid fibrils formed? At what point in the context of the conversion of a functional endogenous protein into amyloid fibrils do toxic oligomers occur? What do they look like? How similar are these processes for different proteins? What role does the native, functional protein structure with its underlying amino acid sequence play in these processes? Are there amyloid fibrils without toxic oligomers as intermediates or by-products? We work on these and other questions with numerous biophysical methods, in which analytical ultracentrifugation plays a significant role. The knowledge acquired in this way will make it easier to identify new target structures for effective therapy and also give new impulses for diagnostics.
M.Sc. Thomas Pauly
M.Sc. Florian Tucholski
M.Sc. Nazanin Fazelnia