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Int. J. Mol. Sci. 2016, 17(7), 983;

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
Author to whom correspondence should be addressed.
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)
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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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