Device for the determination of binding affinities of molecules by the measurement of surface plasmon resonance spectroscopy

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Surface plasmon resonance spectroscopy (SPR) is one of the most commonly used methods to analyze protein interactions. With this technique, a broad spectrum of interaction possibilities can be characterized. In addition to protein-protein interactions, interactions with small molecule ligands, nucleic acids, and binding to liposomes and model membranes can be investigated. Surface plasmon resonance spectroscopy involves immobilizing a binding partner on a metal surface and rinsing an analyte over the measuring cell. A molecular interaction changes the refractive index of the incident light and can be made visible as wavelength- or angle-dependent detection of the reflected light. At the Institute for Structural Biology of the University of Bonn we would like to perform a variety of binding analyses with proteins and so-called single domain antibodies (also nanobodies). The core facility Nanobodies produces up to 20 series of nanobodies in three annual campaigns. In order to test the specific binding of the nanobodies to their target proteins, we would like to carry out SPR analyses in high throughput. In addition, we analyze protein-protein interactions and interactions with small molecule drugs. The SPR device will also be used to train master's and doctoral students, giving them the opportunity to learn modern protein-analyical techniques at the University.