Antimicrobial effects of novel Hermetia illucens peptides

Антимикробное действие новых пептидов Hermetia illucens
Emine Derin, Laurence Van Moll, Milan Wouters, Linda De Vooght, Federica De Stefano, Carmen Scieuzo, Paul Cos, Patrizia Falabella
2026-02-24

Hermetia illucens peptidesHill_BB_C7176broad-spectrum antibacterial activitylipopolysaccharide (lipid A) bindingmembrane permeabilization (propidium iodide uptake)
Antimicrobial resistance represents a significant global health challenge, implicated in nearly 5 million deaths per year. This study investigates the antimicrobial properties of selected peptides derived from the Black Soldier Fly (BSF), identified in silico. Ten synthesized peptides were evaluated in vitro against Gram-positive bacteria (Staphylococcus aureus, Bacillus cereus), Gram-negative bacteria (Escherichia coli, Pseudomonas aeruginosa), and fungi (Aspergillus fumigatus, Candida albicans ). Cytotoxicity was assessed using human lung fibroblasts and red blood cells. Among the peptides, Hill_BB_C7176 demonstrated broad-spectrum antibacterial activity, no cytotoxicity and low hemolytic activity (IC₅₀: 31.6 - >32 µM). The peptide displayed rapid bactericidal activity achieving complete eradication at 8× its minimal inhibitory concentration. Propidium iodide uptake increased in a concentration dependent manner, indicating membrane permeabilization contributing to antibacterial activity. In addition, Hill_BB_C7176 exhibited strong binding affinity to lipopolysaccharide (lipid A). In vivo, Hill_BB_C7176 improved survival of Galleria mellonella larvae infected with S. aureus and E. coli, showing similar survival outcomes to reference antibiotics under the experimental conditions tested. These findings highlight the antibacterial potential of BSF-derived antimicrobial peptides, particularly Hill_BB_C7176, supporting the further research on the antibacterial activity of BSF antimicrobial peptides.
1
Concentration-dependent propidium iodide uptake indicates Hill_BB_C7176 permeabilizes bacterial membranes as a mechanism of action.
2
Hill_BB_C7176 demonstrated strong binding affinity to lipopolysaccharide (lipid A).
3
Hill_BB_C7176 exhibited rapid bactericidal action, achieving complete eradication at 8× its minimal inhibitory concentration.
4
Hill_BB_C7176 showed broad-spectrum antibacterial activity with no cytotoxicity to human lung fibroblasts and low hemolytic activity (IC₅₀: 31.6 - >32 µM).
5
In vivo, Hill_BB_C7176 improved survival of Galleria mellonella larvae infected with S. aureus and E. coli, with survival comparable to reference antibiotics under tested conditions.
6
Ten peptides derived from Black Soldier Fly were identified in silico and synthesized for in vitro antimicrobial testing against Gram-positive, Gram-negative bacteria and fungi.

Selected antimicrobial peptides derived from the Black Soldier Fly (Hermetia illucens), specifically Hill_BB_C7176

Antibacterial and antifungal activity, cytotoxicity/hemolytic profile, mechanism of action (membrane permeabilization and LPS/lipid A binding), rapid bactericidal kinetics, and in vivo efficacy of the BSF-derived peptides

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2026-02-24
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Emine Derin
Laurence Van Moll
Milan Wouters
Linda De Vooght
Federica De Stefano
Carmen Scieuzo
Paul Cos
Patrizia Falabella
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