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

 Amphibian antimicrobial peptides.

Peptide typeSourceStructureMechanism of actionExamplesReferences
MagaininsFrog skin (Xenopus laevis)α-Helical, amphipathicMembrane disruption via pore formation (barrel-stave, toroidal, or carpet models)Magainin-1, magainin-2[98]
BrevininsFrog skin (Rana spp.)α-Helical, amphipathicMembrane permeabilization; induction of cell lysisBrevinin-1, brevinin-2[99]
DermaseptinsFrog skin (Phyllomedusa spp.)α-Helical, cationicMembrane disruption; selective antimicrobial activity against bacteria, fungi, and protozoaDermaseptin B2, dermaseptin S1[100]
TemporinsFrog skin (Rana temporaria)Short α-helical peptidesDisruption of microbial membranes; broad-spectrum activityTemporin A, temporin L[101]
EsculentinsFrog skin (Rana esculenta)α-Helical, amphipathicMembrane permeabilization; inhibition of bacterial growthEsculentin-1, esculentin-2[102]
RanatuerinsFrog skin (Rana tigrina)α-Helical, amphipathicMembrane disruption; anti-bacterial and anti-fungal activityRanatuerin-1, ranatuerin-2[103]