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. Author manuscript; available in PMC: 2009 Sep 24.
Published in final edited form as: Curr Pharm Des. 2009;15(21):2377–2392. doi: 10.2174/138161209788682325

Table 1. Classes of AMPs.

Class Structure Properties Examples Source(s) Physiological Location Reference(s)
Anionic Negatively charged Maximin, Dermicidin Amphibians, humans Airway epithelia [1, 21]
Linear Cationic, α-helical Cecropin, magainin pluerocidin Amphibians, mammals, insects skin [1, 12, 13, 59]
Linear, Cationic, enriched Cationic, enriched in amino acids, extended Abaecin, Indolicidin, histatins Insects, mammals Skin, intestinal epithelium [1, 31, 63]
Peptide fragments Cationic, β-turn Lactoferrin, cathelicidins humans blood [1, 25, 26]
Charged peptides with cysteine Cationic, anionic, forms disulfide bonds, possess cysteine α-, β-, and θ-defensins, protegrin Birds, reptiles, mammals, plants ubiquitous [6, 90, 228]