Abstract
Many different antimicrobial peptides are expressed by mammalian and avian leukocytes [reviewed in 1]. These peptides, which serve as endogenous antibiotics, are amphipathic and cationic molecules comprised of 12-40 amino acid residues. Most, if not all, target and perturb microbial membranes, often by forming voltage-gated channels. Many antimicrobial peptides have a-helical secondary structures, while others contain cystine-stabilized (β-sheets. A few antimicrobial peptides are histidine or prolinerich.
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Lehrer, R.I., Lee, I.H., Menzel, L., Waring, A., Zhao, C. (2001). Clavanins and Styelins, α-Helical Antimicrobial Peptides from The Hemocytes of Styela clava . In: Beck, G., Sugumaran, M., Cooper, E.L. (eds) Phylogenetic Perspectives on the Vertebrate Immune System. Advances in Experimental Medicine and Biology, vol 484. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1291-2_7
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DOI: https://doi.org/10.1007/978-1-4615-1291-2_7
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