Evaluation of binding properties of bovine serum albumin and pyrimidine ligand: Spectroscopic and molecular docking approach

A study of complex formation between pyrimidine ligand and serum albumin should allow us to determine the specificity of interactions of the pyrimidine ligands with proteins. Herein, the in vitro binding behavior of synthetized pyrimidine ligand with bovine serum albumin (BSA) was investigated using spectrofluorometric, UV-Vis. spectrophotometric and docking examinations. The fluorescent character of bovine serum albumin (BSA) is attributed to the existence of Trp (tryptophan) remains. The fluorescent character of BSA in attending of pyrimidine ligand was investigated by utilizing the excitation wavelength of 280 nm and the emission was determined at 300-500 nm at 298, 303 and 308 K. Pyrimidine ligand quenched the BSA intrinsic fluorescence by static mechanism. BSA absorption shift took place owing to the interaction and complex formation. As the temperature enhanced, the binding constant values reduced indicating an un-stable complex formation at high temperature. Owing to the minus amounts of enthalpy and entropy alterations, van der Waals forces and hydrogen bonding were proposed to be included in the BSA-ligand interaction. (C) 2021 Elsevier B.V. All rights reserved.

Automated summary

The study investigated the binding behavior of a synthesized pyrimidine ligand with bovine serum albumin using spectrofluorometric, UV-Vis. spectrophotometric and docking examinations. The results showed that the quenching of BSA fluorescence by the pyrimidine ligand was due to a static mechanism, with the complex formation being unstable at high temperatures. Van der Waals forces and hydrogen bonding were proposed to be involved in the BSA-ligand interaction.