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Structure–activity relationship of an antibacterial peptide, maculatin 1.1, from the skin glands of the tree frog, Litoria genimaculata
Author(s) -
Niidome Takuro,
Kobayashi Kazuhisa,
Arakawa Hiromi,
Hatakeyama Tomomitsu,
Aoyagi Haruhiko
Publication year - 2004
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.560
Subject(s) - peptide , tree frog , antibacterial activity , antibacterial peptide , vesicle , chemistry , frog skin , peptide sequence , structure–activity relationship , cationic polymerization , biochemistry , dorsum , stereochemistry , biophysics , biology , membrane , anatomy , bacteria , in vitro , ecology , sodium , genetics , organic chemistry , gene
Maculatin 1.1 (Mac) is a cationic antibacterial peptide isolated from the dorsal glands of the tree frog, Litoria genimaculata , and has a sequence of GLFGVLAKVAAHVVPAIAEHF‐NH 2 . A short peptide lacking the N ‐terminal two residues of Mac was reported to have no activity. To investigate the structure–activity relationship in detail, several analogs and related short peptides of Mac were synthesized. CD measurement showed that all the peptides took more or less an α‐helical structure in the presence of anionic lipid vesicles. Analogs which are more basic than Mac had strong antibacterial and hemolytic activities, while short peptides lacking one or two terminal residues exhibited weak or no activity. Outer and inner membrane permeabilization activities of the peptides were also reduced with shortening of the peptide chain. These results indicate that the entire chain length of Mac is necessary for full activity, and the basicity of the peptides greatly affects the activity. Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd.