Molecular Docking Studies of 14 Drugs and Toxins in the Binding Site 1 of Human Serum Albumin with Fatty Acids

摘要

@@ Human serum albumin (HSA) is an abundant plasma protein that binds a wide range of drugs and restricts their free, active concentrations. Detailed knowledge of interaction mechanisms between drugs and HSA is of crucial importance for us to understand the pharmacokinetic behavior of a drug and always the main point of discussions. In this paper, docking studies were used to investigate the interaction of a structurally diverse set of 14 drugs and smallmolecule toxins (OPB, PIZ, WRR, AZQ, HLT, T44, C1F, IMN, 1FL, B3I, IDB, IOS, IBP, DIU) with HSA. The study shows that the docking total scores of the ligands have the high linear correlation coefficient (R2 =0. 80) with experimental activities (1gKa)，which indicates the docking model is reasonable and allows us to predict the binding affinities between HSA and new compounds based on this docking model. The interactions between ligands and HSA are dominated by hydrophobic contacts, hydrogen bond interactions and π-π interactions.