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

Abstract

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 anti-cancer 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-Fluorouracil (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.

Calculation of Dynamic Properties of Drug-Added Aqueous Solutions with T1 T2 Relaxation Times

“…Albumin, the most abundant protein in human serum, is a monomeric structure with a molecular weight of 66 kD, consisting of three helical segments, each divided into two subregions, and has many ligand-binding abilities [31]. The most important factor affecting the distribution of intravenous drugs is the binding affinity of that drug to albumin in human blood serum, and therefore, the interaction between the drug and albumin must be optimal for the drug to reach the target organ and provide an effective treatment.…”