Related Experiment Video
Updated: Aug 18, 2026

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis
Published on: August 15, 2013
Estimation of drug-protein binding parameters on assuming the validity of thermodynamic equilibrium
1Institute of Experimental Pharmacology, Slovak Academy of Sciences, Bratislava. exfasolt@savba.sk
Abstract:
This contribution focuses the reader's attention on the pitfalls usually emerging during the phase of evaluation of experimental data of drug-protein binding studies. To overcome the occurrence of problem(s) apparently defying solution, the concept of "affinity spectra" is recommended to be implemented for data evaluation. A (general) "binding study protocol" is also suggested, which can prevent the formation of inadequate conclusions and the generation of unrealistic drug-protein binding parameters.
Related Concept Videos
The Equilibrium Binding Constant and Binding Strength
The Equilibrium Binding Constant and Binding Strength
Protein-Drug Binding: Mechanism and Kinetics
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
Protein-Drug Binding: Determination Methods
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
Physiological Pharmacokinetic Models: Assumption with Protein Binding
Nonlinear Pharmacokinetics: Bioavailability and Protein-Drug Binding
To quantify the extent of bioavailability, pharmacologists often use a parameter called .

