Membrane proteins are prime drug targets due to their essential role in regulating physiological processes. Familiar examples include G-protein coupled receptors (GPCR), histidine and tyrosine kinases, and cytokine receptors, in addition to a vast range of ion channels, enzymes, and transporters.
With more than half of all currently validated drugs on the market targeting membrane proteins, the importance of this protein family to drug development is well established. However, membrane proteins are notoriously difficult to study, mainly because their hydrophobicity makes them extremely unstable following their extraction from the cell membrane.
Understanding the interaction between a membrane protein and a small molecule drug or monoclonal antibody therapeutic is fundamental to drug development since it provides valuable insight regarding drug potency and efficacy. Yet to fully understand such liaisons, it is vital that the measurement of binding kinetics between these molecules is reliable.