Drugs and fatty acide competition for the binding sites in human serum albumin

Abstract

Human serum albumin (HSA) is a highly abundant and extensively studied transport protein in human blood. It binds and transports a wide range of compounds, including fatty acids, heavy metal ions, metabolites, and nutrients. Binding with a double bond ligand enhances electron transport and electrical conductivity. HSA also displays catalytic activity and regulates osmotic pressure. Its unique structure allows interactions with diverse chemical and biochemical substances. HSA is utilized in medicine, pharmaceuticals, and environmental protection, and shows promise as a biosensor. In this study, molecular docking calculations were performed to investigate the competition between fatty acids and some drugs for the nine binding sites in HSA. A special interest was given to the influence of fatty acids on the number and positions of drug binding sites on HSA. Attention was focused on the binding energy of a ligand to HSA, as well as the interaction between ligand molecules and aminoacides in the binding site. The ability to transport drugs to specific receptors, enabling their unimpeded passage through membranes and biological barriers, has garnered increasing attention. HSA binds and transports medicinal substances, facilitating their storage and metabolism. This reduces the active concentration of drugs in the blood, improves their distribution, and extends their therapeutic effect.