Molecular Docking Studies of 14 Drugs and Toxins in the Binding Site 1 of Human Serum Albumin with Fatty Acids
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.
human serum albumin molecular docking site 1 drugs fatty acids
Jianxiong Diao Ye Sun Fei Ding Xinling Yang Ying Sun Li Zhang
College of Resources and Environmental Science, China Agricultural University, Beijing 100193, China PMDD Lab. ,Department of Applied Chemistry, College of Science,China Agricultural University, Beijin
国际会议
北京
英文
345-346
2012-09-15（万方平台首次上网日期，不代表论文的发表时间）