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.
CITATION STYLE
Rusnati, M., & Bugatti, A. (2016). Surface plasmon resonance analysis of heparin-binding angiogenic growth factors. In Methods in Molecular Biology (Vol. 1464, pp. 73–84). Humana Press Inc. https://doi.org/10.1007/978-1-4939-3999-2_7
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