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

表面等离子体共振光谱（SPR）是分析蛋白质相互作用最常用的方法之一。利用这种技术，可以表征广泛的相互作用可能性。除了蛋白质-蛋白质相互作用之外，还可以研究与小分子配体、核酸的相互作用以及与脂质体和模型膜的结合。表面等离子体共振光谱法涉及将结合配偶体固定在金属表面上并在测量池上冲洗分析物。分子相互作用改变入射光的折射率，并且可以作为反射光的波长或角度依赖性检测而变得可见。在波恩大学结构生物学研究所，我们希望对蛋白质和所谓的单域抗体（也称为纳米抗体）进行各种结合分析。核心设施Nanobodies在三个年度活动中生产多达20个系列的纳米抗体。为了测试纳米抗体与其靶蛋白的特异性结合，我们希望以高通量进行SPR分析。此外，我们还分析了蛋白质-蛋白质相互作用以及与小分子药物的相互作用。SPR设备还将用于培训硕士和博士生，使他们有机会在大学学习现代蛋白质分析技术。

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.