Affinity and kinetics are both vital to understand in the drug development process. These binding parameters affect the pharmacodynamics and pharmacokinetics of a drug, the efficacy of the drug, and also the per-dose cost. Most laboratory screening techniques give a ranking of apparent activities or apparent affinities, however many methods are prone to false positives and provide incomplete data on binding parameters.
In this paper, you’ll learn:
- Why binding kinetics are critical to understand in many different drug development applications
- Why measurement of only the equilibrium dissociation constant, KD, is insufficient to understand drug-target interactions
- Why label-free methodologies are critical to obtaining accurate binding data
- How to utilize biosensors to detect binding partners
- The drug development questions that can be answered with biosensors
- What “Enhanced Surface Plasmon Resonance” is and how it works