Understanding how small molecules interact with their biological targets is essential for drug discovery and lead optimization. Biolayer interferometry (BLI) enables real-time, label-free measurement of molecular interactions, but its application to small molecules has traditionally been limited by sensitivity challenges. Recent advances in BLI technology are expanding its potential for measuring binding kinetics and affinity in small molecule research.
This application note presents the use of BLI to characterize interactions between small molecule inhibitors and carbonic anhydrase II, including experimental approaches for measuring binding kinetics and comparing results with surface plasmon resonance (SPR) data.
Download this application note to learn:
- How BLI can measure binding kinetics and affinity for small molecules with low molecular weights
- Key experimental considerations for obtaining reproducible small molecule binding measurements
- How BLI-derived kinetic and affinity measurements compare with published SPR data
