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Feleucin‐ BO 1: A Novel Antimicrobial Non‐Apeptide Amide from the Skin Secretion of the Toad, Bombina orientalis, and Design of a Potent Broad‐Spectrum Synthetic Analogue, Feleucin‐ K 3
Author(s) -
Hou Xiaojuan,
Du Qiang,
Li Renjie,
Zhou Mei,
Wang Hui,
Wang Lei,
Guo Can,
Chen Tianbao,
Shaw Chris
Publication year - 2015
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/cbdd.12396
Subject(s) - candida albicans , antimicrobial , escherichia coli , peptide , antimicrobial peptides , corpus albicans , biology , secretion , potency , toad , bacteria , staphylococcus aureus , stereochemistry , biochemistry , microbiology and biotechnology , chemistry , in vitro , genetics , gene , ecology
Feleucins‐ BV 1 and ‐ BV 2 are recently described prototypes of a novel antimicrobial non‐apeptide ( AMP ) family identified in the skin secretion of the bombinid toad, Bombina variegata . They are encoded on different precursors that also encode a novel bombinin. Here we describe the identification of feleucin‐ BO 1 ( FLGLLGSLL amide) which is co‐encoded with a different novel bombinin, named feleucin precursor‐associated bombinin ( FPA ‐bombinin‐ BO ), from the skin secretion of Bombina orientalis . Synthetic feleucin‐ BO 1 displayed activity against a reference Gram‐positive bacterium. Staphylococcus aureus ( MIC 34  μ m ) but was inactive (> 250  μ m ) against the Gram‐negative bacterium, Escherichia coli , and the yeast, Candida albicans . This pattern of activity was similar to that of the prototypes. Design and synthesis of a cationicity‐enhanced analogue, feleucin‐ K 3 ( F ‐ K 3), in which the amino acid residues at positions 3 ( G ), 6 ( G ) and 7 ( S ) of feleucin‐ BO 1 were substituted with Lys ( K ) residues, resulted in a peptide with significantly enhanced potency and spectrum of activity. The MIC s of F ‐ K 3 against the reference micro‐organisms were 7  μ m ( S. aureus ), 14  μ m ( E. coli ) and 7  μ m ( C. albicans ). These data indicate that the skin secretions of amphibians can continue to provide novel peptide templates for the rational design of analogues with possible therapeutic utility.

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