We have just published a new paper in the European Journal of Medicinal Chemistry showing how to design better FAP-targeting radioligands by focusing on how long they stay bound to their target, not just how tightly they bind. In this work, we introduce a practical kinetic screening workflow that measures binding and unbinding rates for fibroblast activation protein inhibitors (FAPIs), giving a much clearer picture of which molecules are likely to remain longer in tumors. We then combine these experiments with molecular docking simulations to visualize how different chemical designs interact with the enzyme at the atomic level and to explain why some compounds dissociate much more slowly than others. By linking experimental kinetics with computational binding models, the study provides a rational, structure-based roadmap for optimizing FAPIs with longer residence times—a key requirement for effective theranostic applications. Overall, this approach helps researchers move from trial-and-error chemistry to data-driven, computationally guided radioligand design.