Abstract
Antimicrobial peptides (AMPs) are part of the armament that insects have developed to fight off pathogens. Insect AMPs are typically cationic and often made of less than 100 amino acid residues. Although their structures are diverse, most of the AMPs can be assigned to a limited number of families. The most common structures are represented by peptides assuming a α-helical conformation in organic solutions or disulfide-stabilized β-sheets with or without α- helical domains present. The diverse activity spectrum of these peptides may indicate different modes of action. Genetic analysis in the Drosophila model evidenced that multiple signal transduction pathways are activating the genes coding AMPs.
Keywords: antimicrobial peptides, insect immunity, microbial infection, cecropin, defensin, proline-rich, innate defense, cationic peptide
Protein & Peptide Letters
Title: Insect Antimicrobial Peptides: Structures, Properties and Gene Regulation
Volume: 12 Issue: 1
Author(s): Philippe Bulet and Reto Stocklin
Affiliation:
Keywords: antimicrobial peptides, insect immunity, microbial infection, cecropin, defensin, proline-rich, innate defense, cationic peptide
Abstract: Antimicrobial peptides (AMPs) are part of the armament that insects have developed to fight off pathogens. Insect AMPs are typically cationic and often made of less than 100 amino acid residues. Although their structures are diverse, most of the AMPs can be assigned to a limited number of families. The most common structures are represented by peptides assuming a α-helical conformation in organic solutions or disulfide-stabilized β-sheets with or without α- helical domains present. The diverse activity spectrum of these peptides may indicate different modes of action. Genetic analysis in the Drosophila model evidenced that multiple signal transduction pathways are activating the genes coding AMPs.
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Cite this article as:
Bulet Philippe and Stocklin Reto, Insect Antimicrobial Peptides: Structures, Properties and Gene Regulation, Protein & Peptide Letters 2005; 12 (1) . https://dx.doi.org/10.2174/0929866053406011
DOI https://dx.doi.org/10.2174/0929866053406011 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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