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Biosensors measure the real-time reversible interactions between biologically-relevant molecules independent of labels. Typically, they harness an optical phenomenon to detect the binding of a solution molecule (analyte) to its immobilized partner (ligand) on a sensor and record the output as a “sensorgram”, which tracks the binding signal in arbitrary units proportional to mass sensed at the surface of the biosensor as a function of time. These cutting-edge biophysical tools are revolutionizing our understanding of molecular-level processes because they reveal an entire binding profile between unlabeled reactants and dissect it into kinetic components from which an affinity can be deduced. By definition, the affinity or equilibrium dissociation constant (KD, in units of molar concentration, M) is the ratio of the kinetic rate constants (kd/ka) where kd is the dissociation rate constant in units of reciprocal seconds (1/s) and ka is the association rate constant in units of 1/Ms. Knowing the affinity of an interaction is important to drug discovery because it affects the dose at which a drug is efficacious; drugs that bind their targets tightly can be administered at lower levels than those that bind weakly and thus are less likely to exhibit undesirable side-effects and are more cost-effective. End-point analyses, like ELISA, are less informative and rely upon labeling the reactants and adsorbing one of them, which can spoil their native activity, give high non-specific background signals, and limit the scope of an assay. Biosensors are commonplace in industrial and academic research laboratories worldwide and the Biacore technology has dominated the commercial sector for almost two decades. Recently, other manufacturers have innovated on the concept of a flow cell and how samples are handled to increase the number of interactions that can be studied simultaneously in an automated mode, enable longer measurements, and consume less sample (Rich & Myszka, 2007).

Complementary Use of Label-Free Real-Time Biosensors in Drug Discovery of Monoclonal Antibodies