Biophysical and thermodynamical insights into the interaction of mefenamic acid with human serum albumin, based on combined multi-spectroscopic and molecular modeling approaches

Year 2024, Volume: 28 Issue: 1, 372 - 384, 28.06.2025

Golnaz Parvizifard Mostafa Zakariazadeh Hossein Haghaei Mina Shaban Somaieh Soltani

Abstract

The molecular mechanism of interaction between Mefenamic acid (MA) and human serum albumin (HSA) was investigated. UV-Visible absorption, fluorescence, and FT-IR spectroscopies, with molecular docking, have been used for assay of complex formation, quenching mechanism study, thermodynamic evaluations, and molecular details of the interaction mechanism. The quenching constant (Ksv) of 1.51×105 M-1 was obtained, while the results are indicating the dynamic quenching mechanism. The number of binding sites (n) and apparent binding constants (KA) were 1.51 and 6.55×107 M-1, respectively that resembles positive cooperativity and and strong binding of MA to HSA. The negative sign of standard enthalpy change (ΔH = -88.51 KJ/mol), standard entropy change (ΔS = -146.24 J/mol K), and Gibbs free energy (ΔG = -44.93 KJ/mol) indicated that the van der Waals interactions and hydrogen bonds are facilitating the MA-HSA complex formation. Addition of the metal ions, glucose, urea, and basic pHs decrease the MA-HSA binding constant. Molecular docking simulation showed that mainly positively charged amino acid residues contribute to the MA-HSA interaction.

Keywords

Mefenamic acid , NSAID-HSA interaction , Spectroscopy methods , Molecular docking

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