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METHODS NOTE / BINDING EVIDENCE

SPR vs BLI for antibody affinity:
choose evidence, not a number.

Surface plasmon resonance (SPR) and bio-layer interferometry (BLI) can both support antibody–antigen interaction studies. Their usefulness depends less on a brand of instrument than on the molecular format, capture strategy, assay conditions, signal quality and controls.

Published 10 Oct 2026 · Research-use educational resource · Data handling

What exactly are kon, koff and Kd?

In a simple reversible 1:1 interaction, the association rate constant kon describes complex formation and the dissociation rate constant koff describes complex separation. The equilibrium dissociation constant is KD = koff / kon. Lower equilibrium Kd corresponds to tighter binding under the assumptions of that model.

Real antibodies can deviate from a 1:1 system. Bivalent IgG binding, heterogeneous antigens or heterogeneous ligand surfaces may require different interpretation. Always state whether a result is a model-derived apparent affinity or a defensible intrinsic interaction estimate.

SPR and BLI: practical differences

ConsiderationSPRBLI
DetectionSurface refractive-index responseInterference shift at biosensor tip
FluidicsTypically flow-basedDip-and-read plate format
Study designWell suited to detailed kinetic methodsConvenient for multi-sample screening
Common risksMass transport, bulk effects, surface artifactsSensor loading, shaking/mixing, nonspecific signal
InterpretationBoth require controls, quality review and an appropriate binding model

Artifacts to check before believing a strong binder

  • Immobilization and orientation: a captured antigen may not present the relevant epitope as it appears on cells.
  • Surface density and avidity: multivalent formats can show slower apparent dissociation than a monovalent interaction.
  • Mass transport: diffusion or mixing can limit observed rates rather than true molecular kinetics.
  • Nonspecific interactions: sticky molecules can generate misleading responses even against reference surfaces.
  • Antigen quality: aggregation, misfolding, tags or inactive fractions compromise the experiment.
  • Model fit: apparent numerical precision should not exceed the experimental evidence.

Useful mitigations may include alternative orientations, lower surface densities, reference/control proteins, matched buffers, replicate dilution series and orthogonal cell or binding measurements when biology demands them.

What to request in a CRO data package

  • Raw or suitably exported sensorgrams, not just a Kd summary.
  • Antigen construct, source, quality, concentration series and sample handling conditions.
  • Capture/immobilization design, reference subtraction and regeneration approach, if used.
  • Model assumptions, fitted values with limits and a clear statement of data-quality flags.
  • A conclusion that considers specificity and developability alongside affinity.

When comparing candidates, use consistent target lots, assay formats and controls where feasible. Never rank a panel solely by apparent Kd when expression, aggregation or target presentation differs materially.

Related reading: validating AI-generated antibodies and preclinical developability decision design.

Scientific context

These links provide background context and do not imply partner endorsement.