Protein chemistry; determination of binding kinetics by surface plasmon resonance (Biacore); protein equilibrium binding with microscale-thermophoresis; mass spectrometry;   

Extracellular matrix remodelling, Tumor invasion and metastasis; extravascular lipolysis;

My research group focuses primarily on LU-domain containing proteins with clear functions in human disease. We have two main focus areas: one in cancer invasion and metastasis (uPAR and C4.4A) and one in intravascular lipolysis related to familial chylomicronimia (GPIHBP1). We define kinetic and dynamic properties of protein-ligand interactions with biophysical methods and highly pure protein preparations. Based on this information we seek to design intervention strategies and translate these into relevant clinical settings. Amongst other achievements we have: 1) solved the first crystal structures of uPAR, 2) demonstrated that dynamics of the modular structure of uPAR drives its function, 3) designed a constitutively active uPAR, 4) designed a small 9-mer peptide (AE105) that binds and inhibits uPAR, 5) transformed this peptide into an efficient PET-probe for non-invasive imaging of uPAR expression, and 6) uncovered a new molecular model for intravascular lipolysis reconciling genetic data from GWAS with a new concept of protein regulation (disorder–creates–order in the control of lipoprotein lipase activity).

Consultent for Shire (Boston, US)