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<p>The current study describes the synthesis and characterization of AgNPs stabilized with a diester-based cationic gemini surfactant (C<sub>12</sub>-E2O2-C<sub>12</sub>), and their interaction behavior with protein. The main aim of the study was to explore how the surfactant-coated nanoparticle surface controls the binding and structural response of porcine serum albumin (PSA), acting here as the model protein. Synthesized C<sub>12</sub>-E2O2-C<sub>12</sub>-AgNPs were characterized by a spherical morphology, average size of 12.57&#xa0;nm, and positive surface potential of + 19.50 ± 8.55 mV, confirming their stable dispersion. UV–Vis and fluorescence spectroscopic analyses revealed spontaneous and moderate binding of PSA to the nanoparticles, with the binding constants of 3.44 × 10⁴ M⁻¹ and 7.40 × 10⁴ M⁻¹, respectively. The interaction was mainly driven by electrostatic and hydrophobic forces, leading to changes in the secondary structure of PSA, as supported by FTIR and deconvolution of the amide I band. Surface tension studies further confirmed PSA-induced modulation of the interfacial property of the C<sub>12</sub>-E2O2-C<sub>12</sub>-AgNPst system, with a decrease in CMC and rise in molecular area (A<sub>min</sub>), suggesting protein-mediated reorganization at the interface. Overall, these results offer new insights into the role of gemini surfactant-coated AgNPs in modulating protein–nanoparticles interactions relevant for biomedical and biosensing applications.</p> Graphical Abstract <p></p>

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Exploring the Interaction of Diester-Bonded Cationic Gemini Surfactant Functionalized Silver Nanoparticles with PSA: Analysis Involving Spectroscopic and Tensiometric Approaches

  • 期刊论文

  • 发表日期：

    2026年1月20日

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  • Mohd. Akram,
  • Saif Uz Zafar,
  • Mohammad Salim,
  • Kabir-ud-Din

摘要

The current study describes the synthesis and characterization of AgNPs stabilized with a diester-based cationic gemini surfactant (C12-E2O2-C12), and their interaction behavior with protein. The main aim of the study was to explore how the surfactant-coated nanoparticle surface controls the binding and structural response of porcine serum albumin (PSA), acting here as the model protein. Synthesized C12-E2O2-C12-AgNPs were characterized by a spherical morphology, average size of 12.57 nm, and positive surface potential of + 19.50 ± 8.55 mV, confirming their stable dispersion. UV–Vis and fluorescence spectroscopic analyses revealed spontaneous and moderate binding of PSA to the nanoparticles, with the binding constants of 3.44 × 10⁴ M⁻¹ and 7.40 × 10⁴ M⁻¹, respectively. The interaction was mainly driven by electrostatic and hydrophobic forces, leading to changes in the secondary structure of PSA, as supported by FTIR and deconvolution of the amide I band. Surface tension studies further confirmed PSA-induced modulation of the interfacial property of the C12-E2O2-C12-AgNPst system, with a decrease in CMC and rise in molecular area (Amin), suggesting protein-mediated reorganization at the interface. Overall, these results offer new insights into the role of gemini surfactant-coated AgNPs in modulating protein–nanoparticles interactions relevant for biomedical and biosensing applications.

Graphical Abstract