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<p>The present study explored antimicrobial peptides (AMPs) from the haemolymph of the Nistari race of mulberry silkworms, <i>Bombyx mori</i> L. larvae, based on their protein content, purification, characterization, and bioactivity. The crude haemolymph had 20.978&#xa0;mg/ml of protein and showed strong antimicrobial activity, with zones of inhibition of 21.33&#xa0;mm (<i>Clostridium</i> sp.), 18.66&#xa0;mm (<i>Bacillus</i> sp.), and 25.33&#xa0;mm (<i>Vibrio</i> sp.), which was similar to chloramphenicol. The reverse-phase high-performance liquid chromatography (RP-HPLC) was used to purify peptides, resulting in four major fractions. Among these, SI-PI (16.744&#xa0;min) and SI-PIII (23.752&#xa0;min) were active antimicrobial agents, while SI-PII and SI-PIV were inactive. Matrix-assisted laser desorption/ionization (MALDI) and liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS) showed SI-PI (2454.3940 Da; LKSNYLRLELVLPLWFHKW) and SI-PIII (1999.1731 Da; FRLLARKLNETHLLYL) had amphipathic amino acid content suitable for membrane interaction. Scanning electron microscopy (SEM) validated peptide-induced bacterial morphological alterations, such as pore formation, cytoplasmic leakage, and cell lysis. Overall, <i>B. mori</i>-derived AMPs exhibited strong antimicrobial activity, either beating or rivalling broad-spectrum antibiotics, and provide good candidates for the development of alternative therapeutics against bacterial pathogens.</p> Graphical abstract <p></p>

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A comprehensive evaluation of antimicrobial peptide biosynthesis in Bombyx mori L. larvae: a relative analysis of their properties

  • 期刊论文

  • 发表日期：

    2026年3月29日

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  • Deeya Ghosh Dastidar,
  • Barna Chakraborty,
  • Suman Kumar Halder,
  • Souvik Roy

摘要

The present study explored antimicrobial peptides (AMPs) from the haemolymph of the Nistari race of mulberry silkworms, Bombyx mori L. larvae, based on their protein content, purification, characterization, and bioactivity. The crude haemolymph had 20.978 mg/ml of protein and showed strong antimicrobial activity, with zones of inhibition of 21.33 mm (Clostridium sp.), 18.66 mm (Bacillus sp.), and 25.33 mm (Vibrio sp.), which was similar to chloramphenicol. The reverse-phase high-performance liquid chromatography (RP-HPLC) was used to purify peptides, resulting in four major fractions. Among these, SI-PI (16.744 min) and SI-PIII (23.752 min) were active antimicrobial agents, while SI-PII and SI-PIV were inactive. Matrix-assisted laser desorption/ionization (MALDI) and liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS) showed SI-PI (2454.3940 Da; LKSNYLRLELVLPLWFHKW) and SI-PIII (1999.1731 Da; FRLLARKLNETHLLYL) had amphipathic amino acid content suitable for membrane interaction. Scanning electron microscopy (SEM) validated peptide-induced bacterial morphological alterations, such as pore formation, cytoplasmic leakage, and cell lysis. Overall, B. mori-derived AMPs exhibited strong antimicrobial activity, either beating or rivalling broad-spectrum antibiotics, and provide good candidates for the development of alternative therapeutics against bacterial pathogens.

Graphical abstract