Polyelectrolyte scaffolds can be tuned to optimize the strength of electrostatic interactions with basic residues on proteins. Analysing these interactions at the molecular level, e.g. as a function of scaffold architecture is challenging. To unravel underlying mechanisms, an in-depth analysis of the interaction of polyelectrolytes with proteins will be performed here. Essential components of the work plan include investigating the functional relevance of local polyelectrolyte charge densities, the significance of the specific spatial arrangements of charges, and the impact of polyelectrolyte properties on protein folding and clustering. Hence, various advanced biophysical methods and instrumental techniques will be used to characterize the interaction between polyelectrolyte scaffolds and peptide assemblies as well as proteins in solution and on solid surfaces.

Project A1 addresses the equilibrium properties and in particular the highly important ion-specific effects. Glycosaminoglycans will be the subject of A2 whereas project A3 will study structural consequences of protein binding such as amyloid formation. The projects summarized in Theme A will therefore provide the foundation for all further projects in B and C. Collaboration will provide access to complementary techniques and will enable us to collect quantitative data being key to achieve the central objective of this IRTG described above.

 

Project A1 - Polyelectrolyte protein interactions Project A2 - Glycosaminoglycans and their interaction with amyloid-forming peptides Project A3 -  Elucidating structural implications of polyelectrolyte protein interactions