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

 Microbial antimicrobial peptides.

Peptide typeSourceStructureMechanism of actionExamplesReferences
BacteriocinsLactococcus, Bacillus, Streptococcus spp.Ribosomally synthesized, diverse (α-helical, β-sheet, cyclic)Membrane permeabilization; inhibition of cell wall synthesis; target-specific bacteriaNisin, pediocin, lactacin F[129]
LantibioticsLactococcus, Streptococcus spp.Cyclic, thioether-containing peptidesBind lipid II; inhibit peptidoglycan synthesis; induce pore formationNisin, subtilin[130]
MicrocinsE. coli, EnterobacteriaceaeSmall, < 10 kDa, cationic peptidesMembrane disruption; inhibit essential enzymes; interfere with DNA/RNA synthesisMicrocin J25, microcin B17[131]
GramicidinsBacillus brevisLinear α-helical peptidesForm transmembrane ion channels; disrupt the membrane potentialGramicidin A, gramicidin D[132]
PolymyxinsPaenibacillus polymyxaCyclic lipopeptidesDisrupt Gram-negative bacterial outer membranes by binding LPSPolymyxin B, polymyxin E[133]
BacitracinBacillus subtilisCyclic peptide antibioticInhibits cell wall biosynthesis by interfering with bactoprenol recyclingBacitracin[134]

LPS: lipopolysaccharide.