Biacore-Type Dual-Channel SPR Optical Engine
Kretschmann prism geometry with high-resolution 780 nm diode laser and linear CCD array.
Quantify the resonance angle shift of a gold-film SPR immunosensor as a function of analyte protein concentration to determine association kinetics and Langmuir adsorption linearity. Explore interactive physiological instrumentation simulation, biomechanics, and biomedical engineering telemetry.
Ready to sample with Antigen C = 15.0 nM.
Adjust Antigen C, then execute biomedical trial.
Biomedical engineering telemetry and physiological states are evaluated rigorously using 64-bit IEEE 754 precision. Residuals reflect ordinary least-squares regression across successive observations. Continuous data structures support high-fidelity biological and physiological modeling.
The linear sensitivity model applies in the low-concentration sub-saturation regime (C_ag ≤ 30 nM). Evaluated using a 50 nm gold sensor chip functionalized with covalently coupled monoclonal anti-human IgG via an alkanethiol self-assembled monolayer (SAM). Analyte is human IgG diluted in HBS-EP running buffer (pH 7.4) perfused at 30 μL/min.
Kretschmann prism geometry with high-resolution 780 nm diode laser and linear CCD array.
Provides plasmonic gold surface with covalently immobilized anti-human IgG capture antibodies.
Maintains continuous laminar flow (30 μL/min) across sample and reference flowcells.
Eliminates refractive index thermal drift with ±0.01 °C Peltier thermal control.
NIST-traceable protein standards prepared in HBS-EP running buffer (10 to 60 nM).
Tracks angle dip minimum with 0.1 millidegree (0.1 Resonance Unit, RU) resolution.
Quantify the resonance angle shift of a gold-film SPR immunosensor as a function of analyte protein concentration to determine association kinetics and Langmuir adsorption linearity. Standardized parameter settings: 5.0, 10.0, 15.0, 20.0, 25.0, 30.0 nM.
Dock the functionalized CM5 gold chip into the optical block and prime flow channels with HBS-EP running buffer at 30 μL/min until baseline drift is < 0.2 mdeg/min.
Configure Channel 1 as non-specific reference (mock-immobilized) and Channel 2 as active antibody surface for inline differential subtraction.
Inject 5.0 nM human IgG antigen for 180 seconds, allowing binding association to reach equilibrium plateau; log net resonance angle shift Δθ in millidegrees.
Inject a 30-second pulse of 10 mM glycine-HCl (pH 2.0) to dissociate bound antigen and regenerate baseline antibody binding capacity.
Sequentially inject antigen standards of 10.0, 15.0, 20.0, 25.0, and 30.0 nM, executing regeneration and baseline re-referencing at each step.
Plot steady-state angle shift Δθ against concentration C_ag, performing linear regression to evaluate SPR refractive sensitivity k_spr.
Points are your recorded observations. The solid regression line validates SPR Immunosensor Kinetics mathematical scaling.
| # | Antigen Concentration C_ag (nM) | Resonance Angle Shift Δθ (mdeg) | Antigen concentration C_ag (nM) | Resonance angle shift Δθ (millidegrees) | Remove |
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