THERMODYNAMIC STUDIES ON THE INTERACTION OF 5-FLUOROURACIL WITH HUMAN SERUM ALBUMIN Research Article

The interaction of 5-Fluorouracil with human serum albumin have been studied. The mechanism of binding of 5-Fluorouracil (5-FU) with Human serum albumin (HSA) was investigated by fluorescence, absorption and lifetime measurements. The analysis of fluorescence data indicated the presence of static quenching mechanism in the binding. Various binding parameters have been evaluated. The thermodynamic parameters, enthalpy change (∆H), and entropy change (∆S) were also calculated according to fluorescence data. The results show that hydrophobic interaction is a predominant intermolecular force for stabilizing the complex.