Tumor Angiogenesis Assays

Marco Rusnati, Antonella Bugatti

Surface plasmon resonance (SPR) is an optical technique to evaluate biomolecular interactions. Briefly, SPR measures the capacity of two molecules to bind each other by detecting reflected light from a prism-gold film interface. One of the two putative interactants (called ligand) is chemically immobilized onto the gold film. When the sensor is exposed to a sample containing the second interactant (called analyte), its binding to the immobilized ligand causes a change of the refractive index of the material above the gold surface that is monitored as a real-time graph of the response units against time, producing a real-time graph called sensorgram. SPR has become a golden standard technology for label-free, real-time interaction analysis in basic research and drug discovery in a wide array of biomedical areas, including oncology and virology [1, 2]. Here we describe the exploitation of SPR for the study of the capacity of the pro-oncogenic, pro-angiogenic HIV-1 p17 matrix protein [3, 4] to bind to heparin, a structural analog of heparan sulfate proteoglycans (HSPGs) receptors, and for the identification of novel HSPGs-antagonists to be used as anti-p17 drugs.