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Synthesis and biological activity of lipophilic analogs of the cationic antimicrobial active peptide anoplin
Author(s) -
Chionis Kostas,
Krikorian Dimitrios,
Koukkou AnnaIrini,
SakarellosDaitsiotis Maria,
PanouPomonis Eugenia
Publication year - 2016
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.2939
Subject(s) - antimicrobial , peptide , chemistry , antimicrobial peptides , circular dichroism , stereochemistry , amino acid , biochemistry , cationic polymerization , peptide synthesis , zymomonas mobilis , antibacterial activity , peptide sequence , bacteria , biology , organic chemistry , ethanol fuel , fermentation , gene , genetics
Anoplin is a short natural cationic antimicrobial peptide which is derived from the venom sac of the solitary wasp, Anoplius samariensis . Due to its short sequence G 1 LLKR 5 IKT 8 LL‐NH 2 , it is ideal for research tests. In this study, novel analogs of anoplin were prepared and examined for their antimicrobial, hemolytic activity, and proteolytic stability. Specific substitutions were introduced in amino acids Gly 1 , Arg 5 , and Thr 8 and lipophilic groups with different lengths in the N‐terminus in order to investigate how these modifications affect their antimicrobial activity. These cationic analogs exhibited higher antimicrobial activity than the native peptide; they are also nontoxic at their minimum inhibitory concentration (MIC) values and resistant to enzymatic degradation. The substituted peptide GLLKF 5 IKK 8 LL‐NH 2 exhibited high activity against Gram‐negative bacterium Zymomonas mobilis (MIC = 7 µg/ml), and the insertion of octanoic, decanoic, and dodecanoic acid residues in its N‐terminus increased the antimicrobial activity against Gram‐positive and Gram‐negative bacteria (MIC = 5 µg/ml). The conformational characteristics of the peptide analogs were studied by circular dichroism. Structure activity studies revealed that the substitution of specific amino acids and the incorporation of lipophilic groups enhanced the amphipathic α ‐helical conformation inducing better antimicrobial effects. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.