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Int. J. Mol. Sci. 2016, 17(7), 983; doi:10.3390/ijms17070983

Novel Hybrid Peptide Cecropin A (1–8)-LL37 (17–30) with Potential Antibacterial Activity

Laboratory of Feed Biotechnology, State Key Laboratory of Animal Nutrition, College of Animal Science and Technology, China Agricultural University, Beijing 100193, China
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Academic Editor: Jagdish Singh
Received: 5 April 2016 / Revised: 13 June 2016 / Accepted: 16 June 2016 / Published: 29 June 2016
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology)
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Abstract

Hybridizing different antimicrobial peptides (AMPs) is a particularly successful approach to obtain novel AMPs with increased antimicrobial activity but minimized cytotoxicity. The hybrid peptide cecropin A (1–8)-LL37 (17–30) (C-L) combining the hydrophobic N-terminal fragment of cecropin A (C) with the core antimicrobial fragment of LL37 (L) was designed and synthesized. C-L showed higher antibacterial activity against all indicator strains than C and L, and no hemolytic activity to sheep erythrocytes was observed. C-L kills bacterial cells and causes disruption of surface structure, as determined by scanning electron microscopy. Synergistic effects were observed in the combination of C-L with several antibiotics (chloramphenicol, thiamphenicol, or neomycin sulfate) against Escherichia coli and Staphylococcus aureus. View Full-Text
Keywords: hybrid peptide; cecropin A (1–8)-LL37 (17–30); antibacterial activity; hemolytic activity; synergistic interaction hybrid peptide; cecropin A (1–8)-LL37 (17–30); antibacterial activity; hemolytic activity; synergistic interaction
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Wei, X.-B.; Wu, R.-J.; Si, D.-Y.; Liao, X.-D.; Zhang, L.-L.; Zhang, R.-J. Novel Hybrid Peptide Cecropin A (1–8)-LL37 (17–30) with Potential Antibacterial Activity. Int. J. Mol. Sci. 2016, 17, 983.

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