Background: Drugs circulate in the bloodstream in two forms: either free or bound to plasma proteins. Thus, a precise understanding of drug-protein interactions is essential for the design and development of pharmaceuticals. This study examines the interaction between the drug febuxostat and bovine serum albumin, both in the presence and absence of uric acid.
Aim: Given that a precise understanding of drug-protein interactions is crucial for the design and development of drugs and their efficacy, this study aims to evaluate the interaction between bovine serum albumin and the drug febuxostat in the presence of uric acid using spectroscopic methods (UV-Vis and Infrared) as well as electrochemical methods (cyclic voltammetry and square wave voltammetry). Methodology: The interaction of febuxostat with bovine serum albumin in the presence of uric acid was investigated using UV-visible, FT-IR spectroscopies and electrochemical techniques. The data obtained from UV-visible spectroscopy allowed the calculation of the binding constant and the number of binding sites of the drug in the presence and absence of uric acid using the Benesi-Hildebrand equation. Infrared spectroscopic analyzes were performed to investigate the structural changes in the protein resulting from the interaction between febuxostat and albumin. In addition, variations in the oxidation peak current intensity of uric acid in the presence of the drug and protein were used to further investigate this interaction.
Findings: The interaction of the gout medication febuxostat with bovine serum albumin in the presence of uric acid was investigated for the first time using UV-Visible and ATR-FTIR spectroscopy techniques, along with electrochemical methods. Based on the results of UV-visible spectroscopy and the application of the Benesi-Hildebrand equation, the drug binding constant (Kb) and the number of drug binding sites (n) were calculated. The results indicated that in the presence of uric acid, the interac