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Purpose <p>Antimicrobial peptides of Male <i>Bombyx mori.</i>&#xa0;were extracted and validated.</p> Methods <p>Antibacterial peptides were extracted by enzymatic digestion techniques. Six monomer peptides were isolated was named mBMP1 to mBMP6, amino acid composition of them were detected, antimicrobial effects of mBMP6 verified by network pharmacology and molecular docking.</p> Results <p>Sequence homology of the antibacterial peptide Attacin was 95%. Based on network pharmacology theory, the therapeutic targets of mBMP6 and the potential pathogenic targets of pathogenic <i>Escherichia coli</i> were screened. In total, 232 mBMP6 targets and 7426 E. coli pathogenic targets were screened, and PPI analysis was carried out, resulting in 138 nodes and 431 edges. The most pathogenic targets of <i>E. coli</i> were AKT1, STAT3, SRC, HDAC1, EZH2, and SIRT1. Further GO analysis and KEGG pathway enrichment analysis were performed, followed by visual analysis. Through the construction of the mBMP6—active ingredient—target—pathway network, IPGF was identified as the most potent target among the mBMP6 against <i>E. coli</i>, and molecular docking with the six most potent pathogenic targets of <i>E. coli</i> was obtained. Binding ability of six proteins to antibacterial targets, from strongest to weakest, was SIRT1 (−&#xa0;6.34), AKT1 (−&#xa0;5.72), SRC (−&#xa0;5.39), HDAC1 (−&#xa0;5.23), EZH2 (−&#xa0;4.52), STAT3 (−&#xa0;3.12). The antibacterial zone test showed that the antibacterial effect of antimicrobial peptides on <i>Escherichia coli</i> was more obvious than that on <i>Staphylococcus aureus</i>. The minimum inhibitory concentration was 200 mg/L, and the growth inhibition rate was 57.3%.</p> Conclusion <p>mBMP6 had a significant inhibitory effect on <i>E. coli</i>.</p>

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Antibacterial Effect and Network Pharmacology Mechanism of Male Bombyx mori. on Escherichia Coli

  • 期刊论文

  • 发表日期：

    2025年1月28日

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  • Mengqing Guo,
  • Ning Dong,
  • Chunxue Liu,
  • Rui Ma,
  • Shen Li,
  • Yao Sun

摘要

Purpose

Antimicrobial peptides of Male Bombyx mori. were extracted and validated.

Methods

Antibacterial peptides were extracted by enzymatic digestion techniques. Six monomer peptides were isolated was named mBMP1 to mBMP6, amino acid composition of them were detected, antimicrobial effects of mBMP6 verified by network pharmacology and molecular docking.

Results

Sequence homology of the antibacterial peptide Attacin was 95%. Based on network pharmacology theory, the therapeutic targets of mBMP6 and the potential pathogenic targets of pathogenic Escherichia coli were screened. In total, 232 mBMP6 targets and 7426 E. coli pathogenic targets were screened, and PPI analysis was carried out, resulting in 138 nodes and 431 edges. The most pathogenic targets of E. coli were AKT1, STAT3, SRC, HDAC1, EZH2, and SIRT1. Further GO analysis and KEGG pathway enrichment analysis were performed, followed by visual analysis. Through the construction of the mBMP6—active ingredient—target—pathway network, IPGF was identified as the most potent target among the mBMP6 against E. coli, and molecular docking with the six most potent pathogenic targets of E. coli was obtained. Binding ability of six proteins to antibacterial targets, from strongest to weakest, was SIRT1 (− 6.34), AKT1 (− 5.72), SRC (− 5.39), HDAC1 (− 5.23), EZH2 (− 4.52), STAT3 (− 3.12). The antibacterial zone test showed that the antibacterial effect of antimicrobial peptides on Escherichia coli was more obvious than that on Staphylococcus aureus. The minimum inhibitory concentration was 200 mg/L, and the growth inhibition rate was 57.3%.

Conclusion

mBMP6 had a significant inhibitory effect on E. coli.