Ribosomally synthesized peptides with antimicrobial activity are produced by prokaryotes, plants, and a wide variety of animals, both vertebrates and invertebrates. These peptides represent an important defense against micro-organisms. Although the peptides differ greatly in primary structures, they are nearly all cationic and very often amphiphilic, which reflects the fact that many of these peptides kill their target cells by permeabilizing the cell membrane. Moreover, many of these peptides may roughly be placed into one of three groups: (1) those that have a high content of one (or two) amino acid(s), often proline, (2) those that contain intramolecular disulfide bonds, often stabilizing a predominantly β-sheet structure, and (3) those with amphiphilic regions if they assume an α-helical structure. Most known ribosomally synthesized antimicrobial peptides have been identified and characterized during the past 15 years. As a result of these studies, insight has been gained into fundamental aspects of biology and biochemistry such as innate immunity, membrane-protein interactions, and protein modification and secretion. Moreover, it has become evident that these peptides may be developed into useful antimicrobial additives and drugs. This review presents a broad overview of the main types of ribosomally synthesized antimicrobial peptides produced by eukaryotes and prokaryotes.
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Similar content being viewed by others Explore related subjectsDiscover the latest articles and news from researchers in related subjects, suggested using machine learning. Author information Authors and AffiliationsDepartment of Biochemistry, University of Oslo, Post 1401, Blindern, 0316 Oslo, Norway Tel. +47-2285-6633, -6632, -7351; Fax +47-2285-4443, , , , , , NO
J. Nissen-Meyer
Laboratory of Microbial Gene Technology, Agricultural University of Norway, Ås, Norway, , , , , , NO
Ingolf F. Nes
Received: 30 August 1996 / Accepted: 26 November 1996
About this article Cite this articleNissen-Meyer, J., Nes, I. Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action. Arch Microbiol 167, 67–77 (1997). https://doi.org/10.1007/s002030050418
Issue Date: March 1997
DOI: https://doi.org/10.1007/s002030050418
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