Backscattering Interferometry for Low Sample Consumption Molecular Interaction Screening

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Backscattering interferometry (BSI), which uses a simple optical train comprising a He—Ne laser, a microfluidic channel, and a position sensor, has now enabled the measurement of both tethered and free-solution, label-free, molecular interactions within just nanoliters of sample. The simple macro-to-micro interface allows for a highly efficient assay work flow, which has been used to interrogate molecular binding interactions between proteins, ions and protein, and small molecules and proteins, with a high dynamic range of dissociation constants ( KD) and unmatched sensitivity. With this technique, the equilibrium KD for several different binding partners was determined, typically using just picomole—micromole quantities of the binding pair at physiologically relevant concentrations.