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<p>The effect of polystyrene nanoparticles (PSNPs) on binding interaction between Ganglefenum, an angionervalgic, anesthetic, and spasmolytic drug, and bovine serum albumin (BSA) was investigated using UV–Vis spectroscopy, fluorescence spectroscopy, attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopy, and dynamic light scattering (DLS) techniques. UV–Vis spectroscopic analysis revealed that Ganglefenum forms a stable ground state complex with BSA, whereas fluorescence studies indicated the formation of comparatively less stable complexes, which may be attributed to competing quenching processes, conformational alterations, and non-radiative decay pathways affecting BSA fluorescence. Structural analysis based on deconvolution of the FTIR amide I band demonstrated significant changes in the secondary structure of BSA upon interaction with both Ganglefenum and PSNPs. DLS measurement showed the formation of larger complexes, as evidenced by changes in particle size distribution and diffusion coefficients for PSNPs, PS-bound BSA, and PS-bound BSA-Ganglefenum systems. The results of these studies suggest that PSNPs may interfere with the binding interactions between Ganglefenum and BSA.</p> Graphical Abstract <p></p>

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Spectroscopic and DLS investigation of polystyrene nanoparticle exposure on Ganglefenum binding to bovine serum albumin

  • 期刊论文

  • 发表日期：

    2026年7月16日

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  • Karine R. Grigoryan,
  • Ashkhen L. Zatikyan,
  • Zara L. Grigoryan,
  • Artur A. Gabrielyan,
  • Hasmik A. Shilajyan

摘要

The effect of polystyrene nanoparticles (PSNPs) on binding interaction between Ganglefenum, an angionervalgic, anesthetic, and spasmolytic drug, and bovine serum albumin (BSA) was investigated using UV–Vis spectroscopy, fluorescence spectroscopy, attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopy, and dynamic light scattering (DLS) techniques. UV–Vis spectroscopic analysis revealed that Ganglefenum forms a stable ground state complex with BSA, whereas fluorescence studies indicated the formation of comparatively less stable complexes, which may be attributed to competing quenching processes, conformational alterations, and non-radiative decay pathways affecting BSA fluorescence. Structural analysis based on deconvolution of the FTIR amide I band demonstrated significant changes in the secondary structure of BSA upon interaction with both Ganglefenum and PSNPs. DLS measurement showed the formation of larger complexes, as evidenced by changes in particle size distribution and diffusion coefficients for PSNPs, PS-bound BSA, and PS-bound BSA-Ganglefenum systems. The results of these studies suggest that PSNPs may interfere with the binding interactions between Ganglefenum and BSA.

Graphical Abstract