In order to perform good kinetic experiments, not only the experimental conditions have to be optimized, but the evaluation procedure as well. The focus of this work is the in-depth comparison of different approaches and algorithms to determine kinetic rate constants for biomolecular interaction analysis (BIA). The different algorithms are applied not only to flawless simulated data, but also to real-world measurements. We compare five mathematical approaches for the evaluation of binding curves following pseudo-first-order kinetics with different noise levels. In addition, reflectometric interference spectroscopy (RIfS) measurements of two antibodies are evaluated to determine their binding kinetics. The advantages and disadvantages of the individual approach will be investigated and discussed in detail. In summary, we will raise awareness on how to evaluate and judge results from BIA by using different approaches rather than having to rely on “black box” closed (commercial) software packages.

为了进行良好的动力学实验，不仅要优化实验条件，还要优化评估程序。这项工作的重点是深入比较不同的方法和算法，以确定生物分子相互作用分析 (BIA) 的动力学速率常数。不同的算法不仅适用于完美的模拟数据，也适用于真实世界的测量。我们比较了五种数学方法来评估具有不同噪声水平的伪一级动力学之后的结合曲线。此外，评估两种抗体的反射干涉光谱 (RIfS) 测量以确定它们的结合动力学。将详细研究和讨论个别方法的优点和缺点。总之，