Bio-layer Interferometry
Bio-layer Interferometry - Related Videos
13:57
Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
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Cited by 117 •
2014
The protocols here describe kinetic assays of protein-protein interactions with Bio-layer Interferometry. F-type ATP synthase, which is involved in cellular energy metabolism, can be inhibited by its ε subunit in bacteria. We have adapted Bio-layer Interferometry to study interactions of the catalytic complex with ε’s inhibitory C-terminal domain.
10:41
Capturing the Interaction Kinetics of an Ion Channel Protein with Small Molecules by the Bio-layer Interferometry Assay
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Cited by 8 •
2018
The protocol here describes the interactions of purified hEAG1 ion channel protein with the small molecule lipid ligand phosphatidylinositol 4, 5-bisphosphate (PIP2). The measurement demonstrates that BLI could be a potential method for novel small-molecule ion channel ligand screening.
05:13
Biolayer Interferometry Technology to Detect Interactions between Ligand and Analyte
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2025
In this video, we demonstrate biolayer interferometry (BLI) technology to detect the intermolecular interactions between ligands and target analytes in real-time. BLI measures changes in the interference pattern of white light reflected off a layer of immobilized ligands on a biosensor surface as they interact with analytes in solution.
12:14
The Generation of Higher-order Laguerre-Gauss Optical Beams for High-precision Interferometry
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Cited by 7 •
2013
Large laser-interferometers are being constructed to create a new type of astronomy based on gravitational waves. Their sensitivities, as for many other high-precision experiments, are approaching fundamental noise limits such as the atomic vibration of their components. We are pioneering technologies to overcome these limits using novel laser beam shapes.
16:38
Bridging the Bio-Electronic Interface with Biofabrication
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Cited by 3 •
2012
This article describes a biofabrication approach: deposition of stimuli-responsive polysaccharides in the presence of biased electrodes to create biocompatible films which can be functionalized with cells or proteins. We demonstrate a bench-top strategy for the generation of the films as well as their basic uses for creating interactive biofunctionalized surfaces for lab-on-a-chip applications.
FAQs
Binding occurs on a fiber-optic sensor whose surface carries an interaction partner. As additional material accumulates at that surface, the optical thickness changes, shifting the interference pattern. The instrument records this shift as a wavelength response over time, allowing the binding event to be followed continuously rather than inferred only from an endpoint measurement.
The coating presents one interaction partner at the sensor surface and determines which binding event can be observed. In immunology and infection studies, that partner may be an antibody, antigen, receptor, or pathogen-associated molecule. Selecting the appropriate coated component enables researchers to examine a defined interaction and evaluate whether binding is specific to the intended counterpart.
The time-dependent wavelength response can support analysis of binding affinity, association, and dissociation rates. Affinity describes the overall strength of the interaction, while association and dissociation rates describe how quickly binding develops and how rapidly complexes separate. Examining these measures together provides a more detailed picture of interaction behavior than a simple positive or negative result.
Because the readout comes from a change in optical thickness at the sensor surface, the interaction can be monitored without relying on a labeling signal. This supports direct real-time characterization of antibodies, antigens, receptors, and pathogen-associated molecules. The resulting measurements can help distinguish interaction specificity and quantify kinetic behavior during immunological or host-pathogen studies.
Researchers first prepare a fiber-optic sensor with one interaction partner on its surface. The sensor is then used to observe binding by molecules presented as the counterpart, while the instrument tracks the resulting interference-related wavelength response in real time. The recorded signal is subsequently interpreted to estimate affinity, association and dissociation rates, and interaction specificity.
The method is useful when investigators need to screen antibodies, characterize antigen or receptor interactions, or examine binding involving pathogen-associated molecules. It also supports therapeutic development and diagnostic assay design. In host-pathogen research, real-time measurements can help clarify how strongly and specifically molecular components interact, providing quantitative context for immune recognition and infection-related mechanisms.