Biolayer Interferometry
Label-free technology for real-time analysis of biomolecular interactions. Our laboratory has established expertise in BLI-based assays, which are performed using an Octet QKe system (Sartorius) for kinetic and affinity characterization. It enables rapid and quantitative determination of binding kinetics (kon, koff) and affinity (KD) without the need for labeling or complex sample preparation.
The platform is widely applied in drug discovery, preclinical, and translational research for the characterization of biologics, including monoclonal antibodies, antibody fragments, nanobodies, recombinant proteins, and receptor–ligand interactions.
Assays require minimal sample consumption and are compatible with a broad range of biological matrices. In addition to in vitro screening workflows, the technology supports the interpretation of in vivo studies by analyzing samples such as serum and plasma from pharmacokinetic, pharmacodynamic, and immunogenicity experiments, enabling assessment of binding activity and functional integrity of biologics.
Furthermore, the system is used for the screening of nanobody candidates derived from phage display libraries, including periplasmic extracts, to identify binders with specific affinity toward target antigens.
Applications
| Application | Description |
|---|---|
| Binding Kinetics Analysis | Real-time measurement of association and dissociation rates (ka, kd) and binding affinity (KD). |
| Antibody & Nanobody Characterization | Evaluation of monoclonal antibodies, bispecific formats, fragments, and nanobodies for target binding performance. |
| Phage Display Screening (Nanobodies) | Affinity screening of nanobody candidates from periplasmic extracts to identify binders against specific targets. |
| Receptor–Ligand Interactions | Characterization of protein–protein interactions relevant to signaling pathways and mechanism of action. |
| Biologics Development Support | Selection and optimization of therapeutic candidates during early drug discovery and preclinical development. |
| Epitope Binning | Classification of antibodies and nanobodies based on binding competition and epitope specificity. |
| Assay Development & Optimization | Development of robust binding assays for complex or low-affinity interaction systems. |
Key Features
- Label-free real-time interaction analysis
- Quantification of binding kinetics (ka, kd) and affinity (KD)
- Compatibility with antibodies, nanobodies, and protein–protein systems
- Screening of phage display–derived nanobody libraries
- Minimal sample preparation requirements
- Low sample consumption
- Suitable for biologics discovery and preclinical development
- Supports translation between in vitro binding data and in vivo study design