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<p>The molecular interaction of Metaxalone (MTX), skeletal muscle relaxant and bovine serum albumin (BSA) was studied. This was done through a number of biophysical and molecular modelling methods. According to fluorescence spectroscopy at excitation wavelength (290&#xa0;nm) and three temperatures, MTX is an efficient quencher of the intrinsic fluorescence of BSA by mechanism of static quenching. This interaction also caused some observable changes in the UV-Vis absorption spectrums, which implies the observed alteration in the three-dimensional structure of BSA. The study of binding constants revealed a decrease in the value of a thermodynamically stable MTX-BSA complex with temperature. Thermodynamic analyses revealed negative enthalpy (ΔH<b>)</b> and entropy (ΔS<b>)</b> values, meaning that the van der Waals forces and hydrogen bonding caused the binding in the first place. In addition, site I was identified as the primary site of MTX binding in BSA which is essential by site marker displacement assays and confirmed by molecular docking studies by Sudlow, Site I. To examine the electrical properties of it, we further optimised the geometry of the energetically preferred docked MTX conformation at the B3LYP/6-311G (d, p) level of DFT. By applying cyclic voltammetry, the optimal BSA concentration of 10 µM was determined to conduct the electrochemical analysis because higher concentrations did not allow the movement of electrons, which was probably due to the formation of a protein coating on the electrode. The redox behaviour of the MTXBSA system with concentration implied complexation and restricted transfer of electrons at high MTX concentrations, probably due to the attainment of the binding capacity of BSA.</p>

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Comprehensive spectroscopic, electrochemical and computational analysis of the interaction between metaxalone and bovine serum albumin

  • 期刊论文

  • 发表日期：

    2026年7月31日

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  • Aayushi Sharma,
  • Anju Singh

摘要

The molecular interaction of Metaxalone (MTX), skeletal muscle relaxant and bovine serum albumin (BSA) was studied. This was done through a number of biophysical and molecular modelling methods. According to fluorescence spectroscopy at excitation wavelength (290 nm) and three temperatures, MTX is an efficient quencher of the intrinsic fluorescence of BSA by mechanism of static quenching. This interaction also caused some observable changes in the UV-Vis absorption spectrums, which implies the observed alteration in the three-dimensional structure of BSA. The study of binding constants revealed a decrease in the value of a thermodynamically stable MTX-BSA complex with temperature. Thermodynamic analyses revealed negative enthalpy (ΔH) and entropy (ΔS) values, meaning that the van der Waals forces and hydrogen bonding caused the binding in the first place. In addition, site I was identified as the primary site of MTX binding in BSA which is essential by site marker displacement assays and confirmed by molecular docking studies by Sudlow, Site I. To examine the electrical properties of it, we further optimised the geometry of the energetically preferred docked MTX conformation at the B3LYP/6-311G (d, p) level of DFT. By applying cyclic voltammetry, the optimal BSA concentration of 10 µM was determined to conduct the electrochemical analysis because higher concentrations did not allow the movement of electrons, which was probably due to the formation of a protein coating on the electrode. The redox behaviour of the MTXBSA system with concentration implied complexation and restricted transfer of electrons at high MTX concentrations, probably due to the attainment of the binding capacity of BSA.