Dual-channel Spr
Dual-channel Spr - Related Videos
06:58
Surface Plasmon Resonance (SPR)
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2023
Surface plasmon resonance (SPR) is the underlying optical phenomenon behind label-free biosensors to evaluate the molecular affinity, kinetics, specificity, and concentration of biomolecules. In SPR, biomolecular interactions occur on a biosensor made of a thin layer of metal on a prism. Real-time interactions of biomolecules can be monitored by measuring the changes of light reflected off the underside of the metal. This video describes the basic concepts of SPR and how it is used to analyze...
10:30
Simultaneously Capturing Real-time Images in Two Emission Channels Using a Dual Camera Emission Splitting System: Applications to Cell Adhesion
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Cited by 4 •
2013
Dual camera emission splitting systems for two-color fluorescence microscopy generate real-time image sequences with exceptional optical and temporal resolution, a requirement of certain live cell assays including parallel plate flow chamber adhesion assays. When software is employed to merge images from simultaneously acquired emission channels, pseudocolored image sequences are produced.
14:44
Scalable Fabrication of Stretchable, Dual Channel, Microfluidic Organ Chips
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Cited by 43 •
2018
Here, we present a protocol that describes the fabrication of stretchable, dual channel, organ chip microfluidic cell culture devices for recapitulating organ-level functionality in vitro.
08:25
Voltage and Calcium Dual Channel Optical Mapping of Cultured HL-1 Atrial Myocyte Monolayer
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Cited by 9 •
2015
This article describes the technique used to perform dual channel optical mapping in cultured HL-1 atrial cell monolayers. This unique protocol allows the simultaneous visualization of both calcium (Ca) and voltage (Vm) activity in the same area for the detailed detection and analysis of electrophysiological properties of culture monolayers.
11:21
Photoconversion of Purified Fluorescent Proteins and Dual-probe Optical Highlighting in Live Cells
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Cited by 5 •
2010
This protocol describes a general approach to perform photoconversion of fluorescent proteins on a confocal laser scanning microscope. We describe procedures for the photoconversion of puried protein samples, as well as for dual-probe optical highlighting in live cells with mOrange2 and Dronpa.
FAQs
The resonance shift arises because binding changes the refractive index close to the metal sensor film. Polarized light excites surface plasmons, and the resulting change in resonance provides a time-dependent signal rather than a single endpoint. This makes the readout responsive to molecular association at the surface and supports monitoring interaction behavior as it occurs.
A reference channel provides a comparison signal for effects that are not uniquely caused by the intended interaction. Bulk changes in the sample environment or nonspecific surface effects may influence the measured response, so comparing channels helps separate those contributions from binding-related changes. This correction-oriented design is central to interpreting dual-channel data more confidently.
A binding event changes the local refractive index at the sensor surface, and that optical change shifts the resonance signal. The measured response therefore depends on what occurs near the metal film rather than merely on the presence of molecules somewhere in the sample. This surface-localized relationship explains why binding produces a trackable SPR response.
Binding kinetics describe how interaction signals change over time, while affinity indicates how strongly the interacting partners associate. Dual-channel SPR can also support concentration measurements. Together, these outputs help characterize an interaction beyond simple detection, allowing biological researchers to compare binding behavior and quantify relevant properties for protein, nucleic acid, or small-molecule studies.
A conceptual measurement workflow begins by directing polarized light at the metal sensor film in each channel, then observing resonance changes as analyte binding alters the local refractive index. Researchers compare the interaction and reference responses during the measurement. The resulting paired signals can then be analyzed for kinetics, affinity, or concentration, depending on the study.
The platform can be applied to interactions involving proteins, nucleic acids, and small molecules. This breadth makes it suitable for studying different classes of binding partners without changing the core sensing principle. In practice, the paired-channel format is most informative when researchers need to evaluate the target interaction while accounting for background or nonspecific contributions.
It is used in biological research, drug discovery, and assay development when researchers need real-time interaction information and comparative signal interpretation. In drug discovery, the measurements can help characterize candidate binding behavior; in assay development, the reference channel can support assessment of background effects. These uses connect mechanistic interaction analysis with practical test-design decisions.