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

ABSTRACT: 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.

SUBMITTER: Bates SR

PROVIDER: S-EPMC2749446 | biostudies-other | 2009 Aug

REPOSITORIES: biostudies-other

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