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<p>Plant-based serine protease inhibitors represent a promising class of bioactive compounds with potential therapeutic relevance. In this study, serine protease inhibitor-enriched peptide fractions were isolated from <i>Zingiber officinale</i>, <i>Allium sativum</i>, and <i>Momordica charantia</i>. Fractions were enriched using ammonium sulfate precipitation, followed by ion-exchange chromatography, and characterized using preliminary physicochemical approaches, including SDS-PAGE (≈ 1-15KDa), UV-visible spectroscopy, Fourier-transform infrared analysis, and amino acid profiling. The peptide-enriched fractions exhibited moderate antibacterial activity against <i>Escherichia coli</i> and <i>Bacillus thurigiensis</i>, with MIC values in the mg/ml range, consistent with partially purified natural fractions. Antifungal activity against <i>Aspergillus niger</i> was observed at approximately 4&#xa0;mg/mL. In a plant-based Tobacco Mosaic Virus (TMV) model using <i>Nicotiana leaves</i>, the peptide-enriched fractions reduced lesion development, indicating measurable antiviral activity. In this experimental system, the maximum inhibition ranged from approximately 58% to 86% depending on the assay format. Thrombolytic assays demonstrated moderate clot lysis (up to 42.95%) with low hemolytic activity under the tested conditions. Molecular docking suggested potential interactions between peptide motifs and serine protease targets, providing a basis for experimental evaluation. Consistent with this, enzyme inhibition assays demonstrated serine protease inhibitory activity, with <i>IC</i><sub><i>50</i></sub> values ranging from 0.15 nM (ASP fraction) to 24 µM (ZOP fraction). Kinetic analyses further revealed distinct modes of inhibition, including competitive, uncompetitive, and mixed mechanisms, depending on the fraction evaluated. As structural identity and purity were not confirmed using the mass spectrometry-based approaches, these findings should be interpreted as an early-stage functional assessment. Definitive structural characterization and further biological validation are necessary to clarify their mechanistic and translational relevance.</p>

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Plant-derived serine protease inhibitor peptides: in vitro antimicrobial and antiviral activities combined with in silico mechanistic insights

  • 期刊论文

  • 发表日期：

    2026年5月13日

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  • Shagufta Kamal,
  • Asif Shahzad,
  • Amna Kamal,
  • Kanwal Rehman,
  • Ismat Bibi,
  • Muhammad Sajid Hamid Akash

摘要

Plant-based serine protease inhibitors represent a promising class of bioactive compounds with potential therapeutic relevance. In this study, serine protease inhibitor-enriched peptide fractions were isolated from Zingiber officinale, Allium sativum, and Momordica charantia. Fractions were enriched using ammonium sulfate precipitation, followed by ion-exchange chromatography, and characterized using preliminary physicochemical approaches, including SDS-PAGE (≈ 1-15KDa), UV-visible spectroscopy, Fourier-transform infrared analysis, and amino acid profiling. The peptide-enriched fractions exhibited moderate antibacterial activity against Escherichia coli and Bacillus thurigiensis, with MIC values in the mg/ml range, consistent with partially purified natural fractions. Antifungal activity against Aspergillus niger was observed at approximately 4 mg/mL. In a plant-based Tobacco Mosaic Virus (TMV) model using Nicotiana leaves, the peptide-enriched fractions reduced lesion development, indicating measurable antiviral activity. In this experimental system, the maximum inhibition ranged from approximately 58% to 86% depending on the assay format. Thrombolytic assays demonstrated moderate clot lysis (up to 42.95%) with low hemolytic activity under the tested conditions. Molecular docking suggested potential interactions between peptide motifs and serine protease targets, providing a basis for experimental evaluation. Consistent with this, enzyme inhibition assays demonstrated serine protease inhibitory activity, with IC50 values ranging from 0.15 nM (ASP fraction) to 24 µM (ZOP fraction). Kinetic analyses further revealed distinct modes of inhibition, including competitive, uncompetitive, and mixed mechanisms, depending on the fraction evaluated. As structural identity and purity were not confirmed using the mass spectrometry-based approaches, these findings should be interpreted as an early-stage functional assessment. Definitive structural characterization and further biological validation are necessary to clarify their mechanistic and translational relevance.