Our research aims at understanding biomolecular interactions of proteins and polypeptides mediating biological and disease-associated processes via peptide chemistry and at developing novel molecules and tools to control or visualize these processes.

We are especially interested in understanding protein interactions mediating amyloid protein misfolding and related cell degeneration and in devising peptide-based molecules and chemical approaches to suppress these processes. We are also interested in characterizing proinflammatory chemokine interactions in atherosclerosis and in designing peptides to modulate these interactions and control their effects. We are using protein(peptide) chemical design and synthesis strategies and a broad range of biochemical and biophysical methods.

Current research activities aim at:

-- understanding protein misfolding and amyloid self-assembly underlying cell degeneration and pathogenesis of the protein aggregation diseases Alzheimer`s disease (AD) and type II diabetes (T2D).

-- devising peptide-based molecules to interfere with or visualize amyloid self-assembly as therapeutic leads or non-invasive amyloid diagnostics in AD and T2D. 

-- characterizing interactions of the proinflammatory atypical chemokine MIF with its receptors and designing conformationally constrained peptides to intervene with these interactions as therapeutic leads for atherosclerosis.