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Objective <p>Tuberculosis (TB), continues to be one of the leading infectious diseases worldwide. The present study aims to explore the effectiveness of Buffalo colostrum whey peptides as natural mycobacterial agents, particularly in the context of the rising multidrug resistance frequently encountered in current treatment regimes.</p> Methodology <p>Colostrum whey peptides generated using various proteases were identified by nLC-MS/MS. The tryptic peptide library was functionally annotated, and their bioactivities were assessed using BIOPEP database. Antimicrobial assays were supported by SEM studies and proteomic approaches. Targeted peptide interactions were examined through molecular docking studies. The mechanism of peptide action was deduced by analysing oxidative stress markers.</p> Results <p>Colostrum whey peptides ranging from 150–855 Da, generated using Pepsin, Pancreatin, Trypsin, Alcalase, and Thermolysin digests, were evaluated for antimicrobial activity. Among these, tryptic peptides demonstrated the most potent inhibitory activity against <i>M. smegmatis</i>, as confirmed by antimicrobial assays and SEM studies, which revealed significant morphological cell wall disruptions in treated cells, thereby validating the antimicrobial action. Functional annotation and clustering of tryptic peptides identified 17 distinct peptide clusters; with protein interaction networks predicted using STRING analysis. Gene Ontology classification indicated that most peptides were localized in the cytoplasm and associated with metabolic and catalytic functions. Proteomic profiling of <i>M. smegmatis</i> following peptide treatment revealed differential expression of key enzymes in the electron transport chain, specifically 1,4-dihydroxy-2-naphthoyl-CoA synthase (MenB) and acyl-CoA dehydrogenase (Fad12). These findings were further supported by molecular docking analyses. Additionally, elevated reactive oxygen species (ROS) levels and suppressed activities of antioxidant enzymes (superoxide dismutase and catalase) suggest that oxidative stress contributes to the observed antimicrobial mechanism. Overall, these results highlight buffalo colostrum–derived whey peptides as promising food-based antimicrobials for tuberculosis.</p> Conclusion <p>This study explored the antimicrobial activity of buffalo colostrum-derived peptides against <i>M. smegmatis</i>. Tryptic peptides were found to be most potent mycobacterial agents, inducing differential expression of MenB and concomitant alterations in oxidative stress markers. These findings were further supported by molecular docking studies, which demonstrated interactions between several peptides and MenB, suggesting the therapeutic potential of food-based antimicrobials.</p>

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Buffalo Colostrum Peptides as Natural Antimicrobials Targeting Menaquinone by Inducing Oxidative stress Pathways in Mycobacterium smegmatis

  • 期刊论文

  • 发表日期：

    2026年1月7日

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  • B. E. Usha,
  • H. S. Aparna

摘要

Objective

Tuberculosis (TB), continues to be one of the leading infectious diseases worldwide. The present study aims to explore the effectiveness of Buffalo colostrum whey peptides as natural mycobacterial agents, particularly in the context of the rising multidrug resistance frequently encountered in current treatment regimes.

Methodology

Colostrum whey peptides generated using various proteases were identified by nLC-MS/MS. The tryptic peptide library was functionally annotated, and their bioactivities were assessed using BIOPEP database. Antimicrobial assays were supported by SEM studies and proteomic approaches. Targeted peptide interactions were examined through molecular docking studies. The mechanism of peptide action was deduced by analysing oxidative stress markers.

Results

Colostrum whey peptides ranging from 150–855 Da, generated using Pepsin, Pancreatin, Trypsin, Alcalase, and Thermolysin digests, were evaluated for antimicrobial activity. Among these, tryptic peptides demonstrated the most potent inhibitory activity against M. smegmatis, as confirmed by antimicrobial assays and SEM studies, which revealed significant morphological cell wall disruptions in treated cells, thereby validating the antimicrobial action. Functional annotation and clustering of tryptic peptides identified 17 distinct peptide clusters; with protein interaction networks predicted using STRING analysis. Gene Ontology classification indicated that most peptides were localized in the cytoplasm and associated with metabolic and catalytic functions. Proteomic profiling of M. smegmatis following peptide treatment revealed differential expression of key enzymes in the electron transport chain, specifically 1,4-dihydroxy-2-naphthoyl-CoA synthase (MenB) and acyl-CoA dehydrogenase (Fad12). These findings were further supported by molecular docking analyses. Additionally, elevated reactive oxygen species (ROS) levels and suppressed activities of antioxidant enzymes (superoxide dismutase and catalase) suggest that oxidative stress contributes to the observed antimicrobial mechanism. Overall, these results highlight buffalo colostrum–derived whey peptides as promising food-based antimicrobials for tuberculosis.

Conclusion

This study explored the antimicrobial activity of buffalo colostrum-derived peptides against M. smegmatis. Tryptic peptides were found to be most potent mycobacterial agents, inducing differential expression of MenB and concomitant alterations in oxidative stress markers. These findings were further supported by molecular docking studies, which demonstrated interactions between several peptides and MenB, suggesting the therapeutic potential of food-based antimicrobials.