Prokaryotic expression and antimicrobial mechanism of XPF‐St7‐derived α‐helical peptides
作者:
Tonghui Yi,
Yibing Huang,
Yuxin Chen,
期刊:
Journal of Peptide Science
(WILEY Available online 2015)
卷期:
Volume 21,
issue 1
页码: 46-52
ISSN:1075-2617
年代: 2015
DOI:10.1002/psc.2722
关键词: XPF‐St7;antimicrobial peptide;α‐helical peptide;ubiquitin‐tag;cell membrane
数据来源: WILEY
摘要:
XPF‐St7 (GLLSNVAGLLKQFAKGGVNAVLNPK) is an antimicrobial peptide isolated fromSilurana tropicalis. We developed an α‐helical segment of XPF‐St7 termed as XPF2. Using the XPF2 as a framework, we increased the positive net charge of XPF2 by amino acid substitutions, and thus obtained two novel antimicrobial peptides XPF4 and XPF6. These were each fused with an ubiquitin tag and successfully expressed inEscherichia coli. This ubiquitin fusion system may present a viable alternative for industrial production of antimicrobial peptides. XPF4 and XPF6 showed much better overall antimicrobial activity against both Gram‐negative and Gram‐positive bacteria than XPF2. The therapeutic index of XPF4 and XPF6 was 5.6‐fold and 6.7‐fold of XPF2, respectively. Bacterial cell membrane permeabilization and genomic DNA interaction assays were utilized to explore the mechanism of action of XPF serial peptides. The results revealed that the target of these antimicrobial peptides was the bacterial cytoplasmic membrane. Copyright © 2014 European Peptide Society and John
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