A 19F NMR-based strategy provides binding properties and structure-affinity relationships of capecitabine and gefitinib to human serum albumin.
Monitoring the interaction between drugs and proteins is critical to understanding drug transport and metabolism underlying pharmacodynamics. The binding capacities to human serum albumin of two anticancer drugs, capecitabine and gefitinib, were compared via an approach combining 19F NMR, 1H saturation transfer difference (STD) NMR, circular dichroism and docking simulations. Results showed that the two drugs interaction with human serum albumin caused 19F NMR signal shifted to different directions. Capecitabine had accurate binding site and higher binding affinity than gefitinib. This study provided fresh insights into ligand–protein interaction and the strength of 19F NMR approach in biomedical research was well illustrated in this case.