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BLI measures real-time protein binding by detecting changes in light interference patterns when molecules bind to a sensor surface.

Method

Label-free optical detection

Data

Real-time kinetics

Sensitivity

Sub-nanomolar detection
1

Ligand Immobilization

Designed proteins immobilized on biosensor tip using Twin-Strep-Tag
2

Analyte Binding

Target protein flows over sensor surface
3

Signal Detection

Binding causes detectable light interference shift
4

Kinetic Analysis

Association and dissociation rates calculated

Key Parameters

BLI provides three critical binding parameters: k_on (association), k_off (dissociation), and K_D (equilibrium constant).
  • k_on - Association rate constant
  • k_off - Dissociation rate constant
  • K_D - Equilibrium dissociation constant (k_off/k_on)

How we use BLI at Adaptyv

We use the Gator Bio Pro for BLI measurements. Our typical workflow involves:
  • Protein immobilization: User-designed proteins are expressed with a linker and Twin-Strep-Tag
  • Target protein binding: Biosensor is moved into solutions of the target protein at different concentrations
  • Kinetic analysis: Real-time binding measurements to determine association and dissociation kinetics
This approach enables efficient characterization of binding interactions for designed proteins with high sensitivity.