article · Frontiers in Food Science and Technology
Algerian honeybee venom has been biochemically characterised and evaluated for its antioxidant and antimicrobial properties. Analysis revealed a composition dominated by low-molecular-weight peptides under 5 kilodaltons and a total protein content of 204.8 micrograms BSA equivalents per millilitre. In laboratory tests, the venom demonstrated substantial antioxidant activity through free-radical scavenging. It also exhibited antimicrobial effects, showing strong activity against Gram-positive bacteria, particularly Staphylococcus aureus, moderate efficacy against Gram-negative bacteria, and measurable activity against the fungus Candida albicans. Computational docking simulations indicated that melittin, the venom's primary peptide, can bind to both the bacterial target PBP2a and the cellular target Keap1. These molecular interactions suggest that melittin could potentially help resensitise methicillin-resistant Staphylococcus aureus to beta-lactam antibiotics while engaging pathways that trigger antioxidant responses.
Bacterial resistance to standard antibiotics and cellular damage from oxidative stress present severe challenges in modern healthcare. By demonstrating that components of honeybee venom can simultaneously inhibit resistant bacteria like MRSA and target pathways linked to oxidative stress, this research highlights natural peptides as potential blueprints for developing therapies that address both antimicrobial resistance and tissue-damaging oxidative conditions.
The research presents early-stage laboratory and computational evidence that honeybee venom peptides could serve as templates for therapeutic development. Pharmaceutical developers focused on infectious diseases and oxidative stress could explore melittin-derived molecules, particularly for resensitising resistant bacteria to existing antibiotics. However, because the findings rely on in vitro assays and molecular docking predictions, the work remains at an early discovery stage, requiring extensive preclinical validation and safety testing before any clinical translation.
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Introduction Honeybee venom is a complex bioactive secretion dominated by melittin, with recognized antioxidant and antimicrobial therapeutic potential. This study characterized Algerian honeybee venom (AHBV) through biochemical profiling, in vitro antioxidant and antimicrobial assays, and in silico molecular docking to explore melittin’s dual targeting capacity. Methods AHBV was characterized using size-exclusion fast protein liquid chromatography, Fourier-transform infrared spectroscopy, the Bradford assay, the ABTS radical-scavenging assay, antimicrobial evaluation, and molecular docking of melittin against PBP2a and Keap1 using pyDock. Results Size-exclusion fast protein liquid chromatography revealed a protein profile dominated by low-molecular-weight peptides (<5 kDa), with only minor higher-molecular-weight components, consistent with the known composition of Apis mellifera venom. Fourier-transform infrared spectroscopy confirmed the proteinaceous, peptide-rich nature of the venom through characteristic amide I and II bands. Total protein content, determined by the Bradford assay, was 204.8 ± 16.26 μg BSA equivalents/mL. AHBV exhibited marked antioxidant activity in the ABTS radical-scavenging assay (727.0 ± 4.9 μmol Trolox equivalents/mg). Antimicrobial evaluation demonstrated significant activity against Gram-positive bacteria, particularly Staphylococcus aureus (MIC 15.62–62.5 μg/mL), moderate efficacy against Gram-negative strains (MIC 125–500 μg/mL), and measurable antifungal activity against Candida albicans (MIC 250 μg/mL). Molecular docking of melittin against PBP2a and Keap1 revealed a potential dual targeting: melittin is predicted to bind the PBP2a allosteric pocket with a pyDock score of −40.406 kcal/mol, and potentially engage the Keap1 Kelch domain (−31.537 kcal/mol) through hydrophobic contacts critical for Nrf2 recognition. Discussion This interaction suggests a mechanism for resensitizing MRSA to β-lactam antibiotics, indicating a possible role in activating the antioxidant response pathway. Taken together, these findings provide region-specific data on Algerian honeybee venom and position melittin as a promising bifunctional therapeutic candidate against antimicrobial resistance and oxidative stress-related disorders.
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DOI: 10.3389/frfst.2026.1919918
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