From:  Expanding horizon of antimicrobial peptides: mechanistic complexity and biomedical potential

 Insect antimicrobial peptides.

Peptide typeSourceStructureMechanism of actionExamplesReferences
CecropinsSilk moth (Hyalophora cecropia)α-Helical, amphipathicMembrane disruption via pore formation; broad-spectrum antibacterial activityCecropin A, cecropin B[109]
DefensinsInsect hemolymph (e.g., Drosophila, beetles)β-Sheet stabilized by disulfide bondsMembrane permeabilization; inhibition of bacterial and fungal growthDefensin A, defensin B[110]
AttacinsSilk moth (Hyalophora cecropia)Glycine-rich proteinsInhibits bacterial cell wall synthesis; effective mainly against Gram-negative bacteriaAttacin A, attacin B[111]
DiptericinsFlies (Drosophila spp.)Glycine-rich peptidesInhibit bacterial growth by targeting outer membrane proteinsDiptericin A, diptericin B[112]
DrosomycinDrosophila melanogasterCysteine-rich, β-sheet peptideAntifungal activity; disrupts fungal cell membranesDrosomycin[113]
Defensin-like peptidesHoneybee (Apis mellifera)β-Sheet stabilized by disulfide bondsBroad-spectrum antimicrobial activity; membrane permeabilizationAbaecin, apidaecin[114]