By Guangshun Wang
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Extra resources for Antimicrobial Peptides (Advances in Molecular and Cellular Biology Series)
2002) Antimicrobial peptides of multicellular organisms. Nature 415, 389–395. , Lubkowski, J. and Lu, W. (2007) Toward understanding the cationicity of defensins. Arg and Lys versus their noncoded analogs. Journal of Biological Chemistry 282, 19653–19665. 2 Lantibiotic-related Research and the Application Thereof Brian Healy, Jim O’Mahony, Colin Hill,* Paul D. Cotter* and R. Paul Ross Abstract Since the 1925 discovery that strains of Escherichia coli can retard the growth of neighbouring bacteria, the study of bacteriocins has continuously evolved.
Wang et al. 4 Peptide-binding targets and mechanisms of action Fig. 5. Representative structures of antimicrobial peptides in the Antimicrobial Peptide Database (APD): (A) α-helix (frog magainin; PDB ID: 2MAG); (B) β-sheet (bovine lactoferricin B; PDB ID: 1LFC); (C) αβ with both α-helices and β-sheet (insect heliomicin; PDB ID: 1I2U); (D) non-αβ structure (bovine indolicidin; PDB ID: 1G89). edu/AP). magnetic resonance) are searched simultaneously, only AMPs with non-αβ three-dimensional structures are found.
It is also clear that the biological functions of AMPs are not limited to antimicrobial activities, as discussed above. In particular, mammalian cathelicidins and defensins have multiple biological functions, in particular immune modulation. g. see human LL-37, APD ID: 310). Therefore, this field can annotate detailed information regarding the biology of AMPs as host defence molecules. Detailed classification and annotation also enable a more meaningful bioinformatic analysis of AMPs. Such results are useful in guiding peptide prediction and design, which we discuss in Chapter 4.