Spr Analysis
Spr Analysis - 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...
09:35
Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)
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Cited by 9 •
2014
Surface Plasmon Resonance (SPR) is a label-free method for detecting bio-molecular interactions in real time. Herein, a protocol for a membrane protein:receptor interaction experiment is described, while discussing the pros and cons of the technique.
15:04
A Neuronal and Astrocyte Co-Culture Assay for High Content Analysis of Neurotoxicity
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Cited by 46 •
2009
This article describes a novel protocol and reagent set designed for sensitive measurement of neurotoxic effects of compounds and treatments on co-cultures of neurons and astrocytes using high content analysis. Results demonstrate that high content analysis represents an exciting novel technology for neurotoxicity assessment.
10:39
Automated Analysis of Intracellular Phenotypes of Salmonella Using ImageJ
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Cited by 3 •
2022
Salmonella invades and replicates inside intestinal epithelial cells both in Salmonella-specific vacuoles and free in the cytosol (hyper-replication). A high-throughput fluorescence microscopy-based protocol is described here to quantify the intracellular phenotypes of Salmonella by two complementary image analyses through ImageJ, reaching single-cell resolution and scoring.
11:24
High-throughput Imaging and Analysis Workflow for Evaluating Skin Cell Phenotypes and Proliferation States in Tissue Samples
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Cited by 1 •
2025
The combination of iterative-bleaching-extends-multiplexity (IBEX) and a commercial nucleotide labeling assay (Click-iT EdU) enables the detection and categorization of dividing cell types in highly dynamic processes in fixed frozen murine tissue sections. Furthermore, a novel open-source image processing pipeline provides high-throughput image acquisition and analysis.
FAQs
Binding increases the amount of material at the sensor surface, changing the local refractive index. The instrument records this change as a shift in the surface plasmon signal while the analyte flows across the immobilized antibody, antigen, or other binding partner. Because the response occurs during the interaction, researchers can follow binding in real time.
The association curve describes signal changes as the analyte binds, whereas the dissociation curve follows the interaction after binding conditions change and the complex separates. Examining both phases allows researchers to evaluate binding kinetics, including how rapidly an interaction develops and how long it persists. These measurements also support affinity assessment.
A measurable signal shows that material accumulated at the sensor surface, but interpretation also depends on whether the interaction reflects the intended molecular recognition event. Comparing the binding behavior of selected immune or infection-related partners helps assess specificity. This distinction is important when characterizing antibody-antigen recognition, host-pathogen interactions, or candidate therapeutic binding.
Because the assay does not require a detection label, the recorded response comes from the binding-related refractive-index change at the sensor surface rather than from a separate signal-generating tag. This supports direct, real-time observation of the interaction. Researchers can therefore focus on kinetic behavior, affinity, and specificity for the molecular pair being studied.
The assay begins with immobilization of one interaction partner on a sensor surface, followed by passage of the analyte across that surface. The instrument monitors the resulting plasmon-signal shift as binding occurs and as the interaction dissociates. Researchers then analyze the association and dissociation curves to extract kinetic, affinity, and specificity information.
In immunology, the method can characterize how antibodies recognize antigens and can compare the resulting interaction behavior through binding kinetics, affinity, and specificity. These measurements support studies of immune recognition and can inform biomarker development, vaccine research, and diagnostic assay design. The real-time format is especially useful when researchers need interaction data rather than only endpoint detection.
Researchers can apply the assay to host-pathogen interactions and to the evaluation of candidate therapeutics. By measuring how interaction signals develop and decline, they can determine whether relevant molecular partners bind and assess the strength and persistence of those interactions. These results can contribute to understanding infection-related recognition and to selecting candidates for further investigation.