Free-solution, label-free molecular interactions studied by back-scattering interferometry

D.J. Bornhop, J.C. Latham, A. Kussrow, D.A. Markov, R.D. Jones, H.S. Sørensen

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    Free-solution, label-free molecular interactions were investigated with back-scattering interferometry in a simple optical train composed of a helium-neon laser, a microfluidic channel, and a position sensor. Molecular binding interactions between proteins, ions and protein, and small molecules and protein, were determined with high dynamic range dissociation constants (K-d spanning six decades) and unmatched sensitivity (picomolar K-d's and detection limits of 10,000s of molecules). With this technique, equilibrium dissociation constants were quantified for protein A and immunoglobulin G, interleukin-2 with its monoclonal antibody, and calmodulin with calcium ion Ca2+, a small molecule inhibitor, the protein calcineurin, and the M13 peptide. The high sensitivity of back-scattering interferometry and small volumes of microfluidics allowed the entire calmodulin assay to be performed with 200 picomoles of solute.
    Original languageEnglish
    JournalScience
    Volume317
    Issue number5845
    Pages (from-to)1732-1736
    ISSN0036-8075
    DOIs
    Publication statusPublished - 2007

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