Unveiling Hidden Insights: Enhanced Analytics with New Heights of Sensitivity
Last updated: May 2025
Overview
Sensitivity plays a crucial role in kinetics, affinity, and quantitation assays. High sensitivity allows for the accurate detection of low concentrations of analytes and ensures that binding kinetics or quantitation parameters can be determined even at the lowest ligand and analyte concentrations. This is vital for determining accurate affinities or concentrations in biomolecular interaction analysis.
The Octet® R8e system provides higher sensitivity, flexible assay design, and extended run times. By utilizing enhanced biolayer interferometry, it transforms biomolecular interaction analysis and accelerates biotherapeutic development. Its improved signal-to-noise ratio enables precise kinetics characterization of low molecular weight analytes such as compounds and small proteins, as well as the detection of low-concentration analytes.
This document highlights how the system’s enhanced technology and data analysis capabilities support biopharmaceutical research at every stage, from drug discovery to drug development, to bioprocessing, and quality control (QC). It empowers researchers to uncover hidden insights, make informed decisions, and expedite the journey to therapeutic breakthroughs.
- Document type: Application Note
- Page count: 12
- Read time: 18 minutes
Key Takeaways
- Accurately measure human IgG concentrations as low as 3.9 ng/mL (26 pM) with a single-step quantitation assay, extending the limit of quantitation (LOD).
- Achieve superior signal-to-noise performance at low human IgG concentrations (3.9, 7.8, and 15.6 ng/mL), enabling faster and more accurate analyte concentration determination through reduced noise and improved data point separation.
- Perform kinetic analysis of interactions between carbonic anhydrase and small molecule analytes—furosemide, sulpiride, and benzenesulfonamide—without Savitzky-Golay filtering in sensorgrams.
- Enhance data collection during initial binding and dissociation phases to uncover hidden molecular interactions, resulting in more accurate association and dissociation rate constants and deeper insights into molecular interactions.
- Utilize an extended experimental run time of 16 hours with minimize evaporation, allowing for precise determination of dissociation rate constants.
- Characterize human IgG goat Fab binding with 2 hours dissociation rate measurement, achieving percentage CVs <8% across six replicates in an overnight run.
Sensorgram Comparison, Example Data From the Article
The increased signal-to-noise on the Octet® R8e enables accurate analysis of binding events at responses below 0.1 nm. Here, Insulin peptide (5,808 Da) binding to a capture antibody shows distinct responses for each analyte concentration below 0.06 nm (1.25 μg/mL ligand concentration) when assessed on the Octet® R8e. For all figures, Savitzky-Golay filtering is not used, highlighting the improvement in signal-to-noise on the Octet® R8e system.
