Complexation of Ibuprofen with Bovine Serum Albumin: Spectroscopic Study and Molecular Simulation
DOI:
https://doi.org/10.15407/ujpe70.11.776Keywords:
bovine serum albumin, ibuprofen, fluorescence quenching, molecular dockingAbstract
The interaction of ibuprofen with bovine serum albumin (BSA) in the aqueous environment has been studied using both experimental and computer simulation methods. The fluorescence quenching spectra are obtained at a constant BSA concentration of 2μM, varying ibuprofen concentrations of 0–1.5 μM, and three fixed temperatures of 293, 303, and 313 K. The intensity dependences follow the Stern–Volmer equation and testify to the static quenching mechanism. Together with the temperature-induced growth of the binding constant, this result points to the predominantly hydrophobic nature of the interaction. The obtained binding constants equal lg KS = 4.3÷5.0 at the binding stoichiometry close to 1 : 1. The thermodynamic analysis of the complexation showed that ΔG < 0, ΔH > 0, and ΔS > 0, G, H, S which confirms the spontaneous and entropy-driven character of the binding process. Molecular docking simulation using AutoDock 4.2.6 made it possible to identify three main binding sites of ibuprofen with BSA. The most energetically favorable binding modes include van der Waals, hydrogen bonding, hydrophobic, and electrostatic interactions; nevertheless, contacts with hydrophobic residues of BSA prevail. The calculated spatial arrangement of ibuprofen with respect to tryptophan residues corresponds to the experimentally observed fluorescence quenching.
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