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Structural features and biological activities of the cathelicidin‐derived antimicrobial peptides
Author(s) -
Gennaro Renato,
Zanetti Margherita
Publication year - 2000
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(2000)55:1<31::aid-bip40>3.0.co;2-9
Subject(s) - cathelicidin , antimicrobial peptides , antimicrobial , chemistry , computational biology , biological activity , biochemistry , peptide , in vitro , biology , organic chemistry
Cathelicidins are a numerous group of mammalian proteins that carry diverse antimicrobial peptides at the C‐terminus of a highly conserved preproregion. These peptides, which become active when released from the proregion, display a remarkable variety of sizes, sequences, and structures, and in fact comprise representatives of all the structural groups in which the known antimicrobial peptides have been classified. Most of the cathelicidin‐derived peptides exert a broad spectrum and potent antimicrobial activity and also bind to lipopolysaccharide and neutralize its effects. In addition, some of them have recently been shown to exert other activities and might participate in host defense also by virtue of their ability to induce expression of molecules involved in a variety of biological processes. This review is aimed at providing a general overview of the cathelicidins and of the peptides derived therefrom, with emphasis on aspects such as structure, biological activities in vitro and in vivo, and structure/activity relationship studies. © 2000 John Wiley & Sons, Inc. Biopoly 55: 31–49, 2000