Screening small molecule or fragment libraries against GPCRs and ion channels is challenging due to the inability to effectively express adequate amounts of stable and functional receptors to enable lead discovery or drug development programs. The characterization of ligand binding mechanisms and binding kinetics of wild type membrane proteins through powerful techniques such as thermal shift or surface plasmon resonance requires they be solubilized, purified and prepared in challenging formats, frequently resulting in sample degradation and loss of binding, and/or function.


Our technology platform allows for the development of EMPs™ in the absence of ligands, which will limit the introduction of conformation bias often seen when variants are developed around agonists or antagonists. For the application of cell-based screening, modulation of receptor expression and increased stability allows for fine-tuning of signaling. Since EMPs™ are more stable and homogeneous, they are more amenable than wild type receptors for biophysical profiling and protein-based screening.