<p>In response to the growing threat of antibiotic resistance, this study explores protein-based nanoparticles as multifunctional platforms capable of improving antimicrobial efficacy and facilitating targeted therapeutic delivery. Bovine serum albumin (BSA) and ovalbumin (OVA) were used to fabricate native, glycated, and acetylated nanoparticles, enabling systematic evaluation of how chemical modifications influence antibacterial activity. Comprehensive characterization—including UV–Vis spectroscopy, dynamic light scattering (DLS), zeta potential analysis, scanning electron microscopy (SEM), and bioinformatic modeling—confirmed that surface modification significantly altered nanoparticle size, surface charge, and hydrophobicity. Agar well diffusion assays indicated that Gram-positive <i>Staphylococcus aureus</i> is more sensitive than Gram-negative <i>Escherichia coli</i>, likely due to differences in cell wall architecture and membrane permeability. Acetylated nanoparticles exhibited enhanced activity against <i>S. aureus</i>, consistent with increased hydrophobicity and stronger membrane interactions, whereas glycated BSA and OVA showed modest improvements against <i>E. coli</i>, potentially reflecting enhanced dispersion and surface hydrophilicity. Broth microdilution MIC assays corroborated these trends, demonstrating that nanoparticle formation generally improves antibacterial efficacy against Gram-positive bacteria. No minimum bactericidal concentration (MBC) was observed under the tested conditions, indicating a primarily bacteriostatic mode of action. Collectively, these findings suggest that protein-based nanoparticles—through tunable surface properties—offer promising platforms for enhancing antimicrobial therapy and enabling targeted drug delivery.</p>

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Comparative Analysis of Antimicrobial Activity of Nanoparticles Derived from Native and Modified Bovine Serum Albumin and Ovalbumin

  • Fereshteh Alizadeh,
  • Seyyed Abolghasem Ghadami,
  • Bahareh Attaran,
  • Zahra Esfahani

摘要

In response to the growing threat of antibiotic resistance, this study explores protein-based nanoparticles as multifunctional platforms capable of improving antimicrobial efficacy and facilitating targeted therapeutic delivery. Bovine serum albumin (BSA) and ovalbumin (OVA) were used to fabricate native, glycated, and acetylated nanoparticles, enabling systematic evaluation of how chemical modifications influence antibacterial activity. Comprehensive characterization—including UV–Vis spectroscopy, dynamic light scattering (DLS), zeta potential analysis, scanning electron microscopy (SEM), and bioinformatic modeling—confirmed that surface modification significantly altered nanoparticle size, surface charge, and hydrophobicity. Agar well diffusion assays indicated that Gram-positive Staphylococcus aureus is more sensitive than Gram-negative Escherichia coli, likely due to differences in cell wall architecture and membrane permeability. Acetylated nanoparticles exhibited enhanced activity against S. aureus, consistent with increased hydrophobicity and stronger membrane interactions, whereas glycated BSA and OVA showed modest improvements against E. coli, potentially reflecting enhanced dispersion and surface hydrophilicity. Broth microdilution MIC assays corroborated these trends, demonstrating that nanoparticle formation generally improves antibacterial efficacy against Gram-positive bacteria. No minimum bactericidal concentration (MBC) was observed under the tested conditions, indicating a primarily bacteriostatic mode of action. Collectively, these findings suggest that protein-based nanoparticles—through tunable surface properties—offer promising platforms for enhancing antimicrobial therapy and enabling targeted drug delivery.