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Design of novel analogues of short antimicrobial peptide anoplin with improved antimicrobial activity
Author(s) -
Wang Yang,
Chen Jianbo,
Zheng Xin,
Yang Xiaoli,
Ma Panpan,
Cai Ying,
Zhang Bangzhi,
Chen Yuan
Publication year - 2014
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.2705
Subject(s) - antimicrobial , antimicrobial peptides , peptide , escherichia coli , lytic cycle , chemistry , amphiphile , bacteria , antibiotics , biochemistry , combinatorial chemistry , microbiology and biotechnology , biology , gene , organic chemistry , virology , virus , genetics , copolymer , polymer
Currently, novel antibiotics are urgently required to combat the emergence of drug‐resistant bacteria. Antimicrobial peptides with membrane‐lytic mechanism of action have attracted considerable interest. Anoplin, a natural α‐helical amphiphilic antimicrobial peptide, is an ideal research template because of its short sequence. In this study, we designed and synthesized a group of analogues of anoplin. Among these analogues, anoplin‐4 composed of d ‐amino acids displayed the highest antimicrobial activity due to increased charge, hydrophobicity and amphiphilicity. Gratifyingly, anoplin‐4 showed low toxicity to host cells, indicating high bacterial selectivity. Furthermore, the mortality rate of mice infected with Escherichia coli was significantly reduced by anoplin‐4 treatment relative to anoplin. In conclusion, anoplin‐4 is a novel anoplin analogue with high antimicrobial activity and enzymatic stability, which may represent a potent agent for the treatment of infection. Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd.