title: Receptor binding assay for NO-independent activators of soluble guanylate cyclase.
abstract: The characterization of the interaction between a ligand and its receptor is crucial for a broad variety of applications in academia as well as in the pharmaceutical industry. Although various sophisticated high-throughput technologies have been established to investigate the binding of ligands to their receptors, classical filtration-based receptor binding assays still have some advantages when smaller number of samples need to be tested. Here we describe a technically easy, cheap, and reliable receptor binding assay that was successfully applied to determine the binding constant of the NO-independent activator of soluble guanylate cyclase, cinaciguat, and the impact of other small molecules on its interaction with the enzyme.
authors.affiliation: CSL Limited, BIO21 Institute, Parkville, VIC, Australia.
authors.forename: Peter M
authors.initials: PM
authors.lastname: Schmidt
authors.forename: Johannes-Peter
authors.initials: JP
authors.lastname: Stasch
mesh_terms: D001565:Benzoates / Q000378:metabolism / Q000494:pharmacology*; D006162:Guanylate Cyclase / Q000378:metabolism; D057166:High-Throughput Screening Assays / Q000379:methods*; D008024:Ligands; D009569:Nitric Oxide / Q000378:metabolism*; D011485:Protein Binding; D018160:Receptors, Cytoplasmic and Nuclear / Q000819:agonists* / Q000378:metabolism; D000071756:Soluble Guanylyl Cyclase
chemical_list: D001565:Benzoates; D008024:Ligands; D018160:Receptors, Cytoplasmic and Nuclear; D009569:Nitric Oxide; C480588:BAY 58-2667; D006162:Guanylate Cyclase; D000071756:Soluble Guanylyl Cyclase