Publications & Literature
Journal references, abstracts, and presentations are excellent resources for exploring the many ways in which BSI technology is being put to work in life science and medical research. We encourage you to return often to this page to keep abreast of new developments in Back-Scattering Interferometry.
Journal Publications
Screening Trends in Drug Discovery: Vol. 10, 14-16 (April, 2009)
Characterizing Molecular Interactions: Label-free, Back-Scattering Interferometry
Amanda Kussrow, Darryl J. Bornhop, Nathan Harris, Stephen Dotson, Scot Weinberger, William Rich
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Science 21:Vol. 317 (September, 2007)
Free-Solution, Label-Free Molecular Interactions Studied by Back-scattering Interferometry
Darryl J. Bornhop, J.C. Latham, Amanda Kussrow, D.A. Markov, Richard D. Jones and Henrik S. Sørensen
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Angewandte Chemie (International ed. in English) 2006 Jan 30;45(6):955-8.
Photobiotin surface chemistry improves label-free interferometric sensing of biochemical interactions
Latham JC, Markov DA, Sørensen HS, Bornhop DJ.
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JACS, 2004 Dec 22;126(50):16659-64 (2004)
Label-Free Molecular Interaction Determinations with Nanoscale Interferometry
Dmitry A. Markov, Kelly Swinney, and Darryl J. Bornhop
Abstract
Quantification of protein-protein and ligand-substrate interactions is central to understanding basic cellular function and for evaluating therapeutics. To mimic biological conditions, such studies are best executed without modifying the proteins or ligands (i.e., label-free). While tools for label-free assays exist, they have limitations making them difficult to fully integrate into microfluidic devices. Furthermore, it has been problematic to reduce detection volumes for on-channel universal analyte quantification without compromising sensitivity, as needed in label-free methods. Here we show how backscattering interferometry in rectangular channels (BIRC) facilitates label-free studies within picoliter volumes. The simple and unique optical train was based on rectangular microfluidic channels molded in poly(dimethylsiloxane) and low-power coherent radiation. Quantification of irreversible streptavidin-biotin binding and reversible protein A-human IgG Fc molecular interactions in a 225 pL detection volume was carried out label-free and noninvasively. Detection limits of 47 x 10(-15) mol of biotin reacted with surface-immobilized streptavidin were achieved. In the case of reversible interactions of protein A and the Fc fragment of human IgG, detection limits were determined to be 2 x 10(-15) mol of IgG Fc. These experiments demonstrate for the first time that (1) high-sensitivity universal solute quantification is possible using interferometry performed within micrometer-sized channels formed in inexpensive PDMS chips, (2) label-free reversible molecular interaction can be studied with femtomoles of solute, and (3) BIRC has the potential to quantify binding affinities in a high-throughput format.
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