Highly parallel measurements of interaction kinetic constants with a microfabricated optomechanical device.

We used mechanical trapping of molecular interactions to demonstrate a highly parallel approach to measure the kinetics of biomolecular interactions. This approach consumes 25 fmol of material per measurement and permits 320 measurements in a single experiment. We measured association and dissociation curves for the interactions of 6-His and T7 epitope tags with their antibodies, from which we determined the off rates, on rates, and dissociation constants.