4.7 Article

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

Journal

Publisher

MDPI AG
DOI: 10.3390/ijms17070983

Keywords

hybrid peptide; cecropin A (1-8)-LL37 (17-30); antibacterial activity; hemolytic activity; synergistic interaction

Funding

  1. National Natural Science Foundation of China [31272476]
  2. Specialized Research Fund for the Doctoral Program of Higher Education of China [20110008110002]

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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.

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