TABLE 3.
Selected examples of natural antibacterial peptides
| Peptide | Structure | Source(s) | Proposed antibacterial mechanism | Reference(s) |
|---|---|---|---|---|
| Magainin | α-Helix | Frog | Permeabilizes bacterial membrane | 161, 273 |
| Cecropin A | α-Helix | Silk moth | Membrane destabilizing | 73, 106 |
| Mellitin | α-Helix | Bee | Membrane destabilizing | 32, 63 |
| LL-37 | α-Helix | Human | Membrane permeabilization; strongly salt antagonized | 12, 172, 176 |
| Buforin II | α-Helix/extended | Toad | Binding of nucleic acid | 187, 188 |
| α/β-Defensins | β-Sheet | Mammals, analogues in insects and fungi | Many are strongly salt antagonized; cell membrane and intracellular targets, inhibits macromolecular synthesis | 108, 147, 262 |
| Protegrin | β-Sheet | Human, porcine | Very potent, membrane permeabilization | 95 |
| Polyphemusin | β-Sheet | Horseshoe crab | Very potent, translocates into cells | 202, 280 |
| Indolicidin | Extended | Bovine | Inhibits macromolecular synthesis, Ca2+-calmodulin interaction | 61, 104, 227 |
| PR-39 | Extended | Porcine | Inhibits DNA/RNA/protein synthesis, no pore formation | 22 |