Investigation of relaxation times in 5-fluorouracil and human serum albumin mixtures

Background: Human serum albumin (HSA) is often selected as a subject of any study because albumin is the most abundant protein in human blood plasma. NMR is recognized as a valuable method to determine the structure of proteins-ligand and protein-drug complexes. Objective - Aim of the study: In this study, protein drug interactions were investigated using 5-Fluorouracil anticancer drug and human serum albumin protein. Materials and methods: In this context 400 MHz NMR spectrometry was used and NMR relaxation rates in drug-albumin complex were investigated with respect to increase albumin concentration and increase in 5-Fluoro-uracil (5-FU)-albumin solution temperature. Results: The results of this study indicated that 5-FU had a weak association with albumin, and it easily dissociated from the protein to which it was attached. Conclusion: The obtained results also gave us useful information about molecular dynamics of drug-albumin interactions.