Functional characterization, antimicrobial effects, and potential antibacterial mechanisms of new mastoparan peptides from hornet venom (Vespa ducalis, Vespa mandarinia, and Vespa affinis)

Antibiotic-resistant bacteria are a major threat to global public health, and there is an urgent need find effective, antimicrobial treatments that can be well tolerated by humans. Hornet venom known have properties, contains peptides with similarity eptides (AMPs), mastoparans. We identified multiple new AMPs from the glands of Vespa ducalis (U-VVTX-Vm1a, U-VVTX-Vm1b, U-VVTX-Vm1c), mandarinia (U-VVTX-Vm1d), affinis (U-VVTX-Vm1e). All these highly similar sequences related toxic peptide, mastoparan. Our newly α-helical structures, amphiphilic, properties. Both U-VVTX-Vm1b U-VVTX-Vm1e killed bacteria, Staphylococcus aure us ATCC25923 Escherichia coli ATCC25922, at concentrations 16 μg/mL 32 μg/mL, respectively. None five exhibited strong toxicity as measured via their hemolytic activity on red blood cells. was able increase permeability E. ATCC25922 degrade its genomic DNA. These results promising, demonstrate value investigating hornet treatment, add growing arsenal such naturally derived treatments. • Five mastoparan venom. excellent antibacterial effect against aureus coli. showed membrane rupture mechanism low activities.