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Free-Solution, Label-Free Molecular Interactions Studied by Back-Scattering Interferometry
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
Baclofen and Other GABAB Receptor Agents Are Allosteric Modulators of the CXCL12 Chemokine Receptor CXCR4
The effect of GABAergic agents on CXCR4 suggests new therapeutic potentials for neurological and immune diseases and allosteric modulation, in accordance with electrophysiology experiments.
Measurement of monovalent and polyvalent carbohydrate-lectin binding by back-scattering interferometry.
The operational simplicity and generality of BSI, along with the near-native conditions under which the target binding proteins are immobilized, make BSI an attractive method for the quantitative characterization of the binding functions of lectins and other proteins.
Characterizing aptamer small molecule interactions with backscattering interferometry.
Backscattering interferometry (BSI), a label-free and free-solution sensing technique, can be used to effectively characterize SM-aptamer interactions, providing Kd values on microliter sample quantities and at low nanomolar sensitivity.
Label-free quantification of membrane-ligand interactions using backscattering interferometry
Backscattering interferometry (BSI) can accurately quantify ligand-receptor binding affinities in a variety of membrane environments by detecting minute changes in the refractive index of a solution and allowing binding interactions of proteins with their ligands to be measured at picomolar concentrations.
Interferometric methods for label-free molecular interaction studies.
Backscattering interferometry uniquely offers the additional advantage of measuring binding interactions in free solution while still using small amounts of sample, which enables the detection and study of binding events without the use of expensive and disruptive labels.
Origin and prediction of free-solution interaction studies performed label-free
It is demonstrated that a simple mass-weighted dη/dC response function is the incorrect equation to determine that the change in RI is produced by binding or folding event in free solution, and proposed a model for the free-solution response function (FreeSRF), validated and highly predictive when combined with quality structural data and reliable calculations of solvent-addressable surface area.
Evolution and protein packaging of small-molecule RNA aptamers.
A high-affinity RNA aptamer (K(d) = 50 nM) was efficiently identified by SELEX against a heteroaryldihydropyrimidine structure, chosen as a representative drug-like molecule with no cross reactivity
The potential of backscattering interferometry as an in vitro clinical diagnostic tool for the serological diagnosis of infectious disease.
Backscattering interferometry enables the detection of syphilis antibody-antigen interactions in the presence of human serum, showing promise as a diagnostic tool for the serological diagnosis of
Comparison of free-solution and surface-immobilized molecular interactions using a single platform.
Backscattering interferometry is used to quantify the binding affinity of mannose and glucose to concanavalin A (ConA), a 106 KDa homotetramer protein, in free solution using picomoles of the protein, and results indicate that the apparentbinding affinity of the sugar-lectin pair increases as the distance between ConA and the surface decreases.