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<p>In this study, mechanistic analysis using SDS-PAGE identified a 58&#xa0;kDa protein as the biomolecule responsible for AgNPs biosynthesis and capping. Colorimetric microplate-based assay confirmed the protein as nitrate reductase, with structural preservation evidenced by a 29.68% activity increase (1.856 to 2.407 U/g) following AgNPs synthesis. Functionalization of AgNPs with ampicillin was indicated by SPR shift from 422.5 to 340.5&#xa0;nm and disappearance of the FTIR band at 1736&#xa0;cm⁻¹. Amp–AgNPs conjugate was stable (3 months), semi-spherical crystalline, polydisperse (PDI: 0.192), average diameter of 27.26&#xa0;nm, zeta potential of − 24.9 mV, and showed broad pH (1–9) and thermal (5–55&#xa0;°C) stability. Docking analysis revealed strong binding of ampicillin within the nitrate reductase catalytic pocket through hydrogen bonding, hydrophobic, and electrostatic interactions, confirming the conjugate stability. Amp–AgNPs (50&#xa0;µg/mL) exhibited potent antibacterial activity against β-lactamase-producing bacteria with inhibition zones of 27.3&#xa0;mm (<i>Escherichia coli</i>), 25.0&#xa0;mm (<i>Enterococcus faecalis</i>), and 26.3&#xa0;mm (<i>Staphylococcus aureus</i>), and MICs of 3.3, 4.7, and 4.3&#xa0;µg/mL, respectively. SEM analysis revealed severe structural changes, indicating synergistic membrane disruption and antibiotic delivery. Amp–AgNPs potently inhibited β-lactamase in the iodometric assay, supporting their potential as alternative therapeutic agents. Future studies should focus on in vivo efficacy and expand this strategy to additional drug delivery applications.</p>

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Biomolecular strategy for designing antibiotic–silver nanoparticles conjugate via nitrate reductase mediated β-lactamase inhibition with molecular docking insights

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年1月3日

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  • Gerges Gad Faheem,
  • Bahig A. El Deeb,
  • Mohamed Ismeal,
  • Mahmoud S. Bakhit

摘要

In this study, mechanistic analysis using SDS-PAGE identified a 58 kDa protein as the biomolecule responsible for AgNPs biosynthesis and capping. Colorimetric microplate-based assay confirmed the protein as nitrate reductase, with structural preservation evidenced by a 29.68% activity increase (1.856 to 2.407 U/g) following AgNPs synthesis. Functionalization of AgNPs with ampicillin was indicated by SPR shift from 422.5 to 340.5 nm and disappearance of the FTIR band at 1736 cm⁻¹. Amp–AgNPs conjugate was stable (3 months), semi-spherical crystalline, polydisperse (PDI: 0.192), average diameter of 27.26 nm, zeta potential of − 24.9 mV, and showed broad pH (1–9) and thermal (5–55 °C) stability. Docking analysis revealed strong binding of ampicillin within the nitrate reductase catalytic pocket through hydrogen bonding, hydrophobic, and electrostatic interactions, confirming the conjugate stability. Amp–AgNPs (50 µg/mL) exhibited potent antibacterial activity against β-lactamase-producing bacteria with inhibition zones of 27.3 mm (Escherichia coli), 25.0 mm (Enterococcus faecalis), and 26.3 mm (Staphylococcus aureus), and MICs of 3.3, 4.7, and 4.3 µg/mL, respectively. SEM analysis revealed severe structural changes, indicating synergistic membrane disruption and antibiotic delivery. Amp–AgNPs potently inhibited β-lactamase in the iodometric assay, supporting their potential as alternative therapeutic agents. Future studies should focus on in vivo efficacy and expand this strategy to additional drug delivery applications.