The Relationship between Hydrophobicity and Drug-Protein Binding in Human Serum Albumin: A Quartz Crystal Microbalance Study

In this paper, the quartz crystal microbalance with dissipation monitoring (QCM-D) was used to investigate hydrophobicity and binding strength (KD) for 10 different drugs interacting human serum albumin (HSA). Quantitative structure activity relationship (QSAR) analysis determine between drug (ClogP) HSA log(1/KD). The results are compared prior knowledge on bovine (BSA) binding. We demonstrate a positive correlation of ligand-protein show statistically significant similarity trend reported in BSA. findings presented work provide insight into role that bound water plays interactions. Further, comparison BSA provides quantitative justification use these proteins interchangeably drug-based kinetics.