مشخصات پژوهش

The binding characteristics of drugs with proteins are important in pharmaceutical and medical sciences because the absorption, distribution and metabolism of drugs are based on their interaction with proteins. A significant amount of different drugs can be reversibly bound to albumin and transported throughout the bloodstream. Therefore, albumin as a drug carrier plays an important role in drug bringing to the cell and its selective delivery. Pyrimidines are heterocyclic aromatic compounds similar to benzene and pyridine. Their derivatives play an important role in human vital functions and have attracted a lot of attention due to their biological activities, such as anti-inflammatory, anti-cancer, anti-bacterial and anti-fungal properties. In the present study, the binding properties of human serum albumin (HSA) with a synthetic pyrimidine compound were investigated. At first, different concentrations of this compound were titrated to protein solution and the possibility of ligand- protein interaction was examined by UV-vis spectroscopy. Then, fluorescence measurements were done to find the binding characteristics. Based on absorbance data, there were visible changes in the micro-environment of HSA due to ligand binding. Using fluorescence emission data, and related equations, Stern –volmer and quenching constant were obtained. Binding constant and sites were also obtained based on Hill equation. Results showed that the binding of the ligand to HSA was happened through static mechanism and one binding site was estimated for this binding. These results may help for better drug design and consumption in medical approaches. However, more examinations are needed for better understanding of the binding properties.