Publications Repository - Helmholtz-Zentrum Dresden-Rossendorf

The development of novel ligands for G-protein-coupled receptors (GPCRs) typically entails the characterization of their binding affinity, which is often performed with radioligands in a competition or saturation binding assay format. Since GPCRs are transmembrane proteins, receptor samples for binding assays are prepared from tissue sections, cell membranes, cell lysates, or intact cells. As part of our investigations on modulating the pharmacokinetics of radiolabeled peptides for improved theranostic targeting of neuroendocrine tumors with a high abundance of the somatostatin receptor sub-type 2 (SST₂), we characterized a series of ⁶⁴Cu-labeled [Tyr³]octreotate (TATE) derivatives in vitro in saturation binding assays. Herein, we report on the SST₂ binding parameters measured toward intact mouse pheochromocytoma cells (MPC) and corresponding cell lysates and discuss the observed differences taking the physiology of SST₂ and GPCRs in general into account. Furthermore, we point out method-specific advantages and limitations.