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<p>Antimicrobial resistance significantly contributes to treatment failures in bacterial infections and poses a major global public health challenge, urgently necessitating the development of new antimicrobial agents, such as antimicrobial peptides (AMPs), which represent a promising drug class. This study aimed to develop a novel, highly effective, low-toxicity antimicrobial agent employing a hybridization strategy to fuse the broad-spectrum AMP LL-37 with the low-toxicity <i>Musca domestica</i> antifungal peptide-1&#xa0;A. The resulting hybrid peptides (ML-1, ML-2, and ML-3) exhibited markedly reduced cytotoxicity and hemolytic activity relative to LL-37. Notably, ML-2 demonstrated broad-spectrum antimicrobial activity, with particularly exerted effective antibacterial and antibiofilm effects against <i>Pseudomonas aeruginosa</i> in vitro. Moreover, with excellent stability, ML-2 retained activity against <i>P. aeruginosa</i> following pepsin treatment and thermal stress. Importantly, <i>P. aeruginosa</i> developed resistance to ML-2 more slowly than to the potent antibiotic ciprofloxacin. Mechanistically, ML-2 killed bacteria by increasing cell membrane permeability and disrupting cell integrity. Altogether, these findings suggest that the hybrid peptide ML-2 has potential as a novel antimicrobial agent against <i>P. aeruginosa</i>.</p>

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Novel Hybrid Peptide ML-2 with Antibacterial and Antibiofilm Activity Against Pseudomonas aeruginosa

  • 期刊论文

  • 发表日期：

    2026年3月24日

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  • Shenghua Wu,
  • Yanping Shi,
  • Yang He,
  • Tao Zhang,
  • Feilong Chen,
  • Yingchun Zhang,
  • Tao Wang

摘要

Antimicrobial resistance significantly contributes to treatment failures in bacterial infections and poses a major global public health challenge, urgently necessitating the development of new antimicrobial agents, such as antimicrobial peptides (AMPs), which represent a promising drug class. This study aimed to develop a novel, highly effective, low-toxicity antimicrobial agent employing a hybridization strategy to fuse the broad-spectrum AMP LL-37 with the low-toxicity Musca domestica antifungal peptide-1 A. The resulting hybrid peptides (ML-1, ML-2, and ML-3) exhibited markedly reduced cytotoxicity and hemolytic activity relative to LL-37. Notably, ML-2 demonstrated broad-spectrum antimicrobial activity, with particularly exerted effective antibacterial and antibiofilm effects against Pseudomonas aeruginosa in vitro. Moreover, with excellent stability, ML-2 retained activity against P. aeruginosa following pepsin treatment and thermal stress. Importantly, P. aeruginosa developed resistance to ML-2 more slowly than to the potent antibiotic ciprofloxacin. Mechanistically, ML-2 killed bacteria by increasing cell membrane permeability and disrupting cell integrity. Altogether, these findings suggest that the hybrid peptide ML-2 has potential as a novel antimicrobial agent against P. aeruginosa.