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Peptide Antimicrobial Agents

Overview
Specialty Microbiology
Date 2006 Jul 19
PMID 16847082
Citations 798
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Abstract

Antimicrobial host defense peptides are produced by all complex organisms as well as some microbes and have diverse and complex antimicrobial activities. Collectively these peptides demonstrate a broad range of antiviral and antibacterial activities and modes of action, and it is important to distinguish between direct microbicidal and indirect activities against such pathogens. The structural requirements of peptides for antiviral and antibacterial activities are evaluated in light of the diverse set of primary and secondary structures described for host defense peptides. Peptides with antifungal and antiparasitic activities are discussed in less detail, although the broad-spectrum activities of such peptides indicate that they are important host defense molecules. Knowledge regarding the relationship between peptide structure and function as well as their mechanism of action is being applied in the design of antimicrobial peptide variants as potential novel therapeutic agents.

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References
1.
Cotter P, Hill C, Ross R . Bacteriocins: developing innate immunity for food. Nat Rev Microbiol. 2005; 3(10):777-88. DOI: 10.1038/nrmicro1273. View

2.
Helmerhorst E, Breeuwer P, Vant Hof W, Oomen L, Veerman E, Amerongen A . The cellular target of histatin 5 on Candida albicans is the energized mitochondrion. J Biol Chem. 1999; 274(11):7286-91. DOI: 10.1074/jbc.274.11.7286. View

3.
Giansanti F, Massucci M, Giardi M, Nozza F, Pulsinelli E, Nicolini C . Antiviral activity of ovotransferrin derived peptides. Biochem Biophys Res Commun. 2005; 331(1):69-73. DOI: 10.1016/j.bbrc.2005.03.125. View

4.
Wang Z, Wang G . APD: the Antimicrobial Peptide Database. Nucleic Acids Res. 2003; 32(Database issue):D590-2. PMC: 308759. DOI: 10.1093/nar/gkh025. View

5.
Andersson E, Rydengard V, Sonesson A, Morgelin M, Bjorck L, Schmidtchen A . Antimicrobial activities of heparin-binding peptides. Eur J Biochem. 2004; 271(6):1219-26. DOI: 10.1111/j.1432-1033.2004.04035.x. View