Abstract
Cecropins, originally found in insects, are a group of cationic antimicrobial peptides. Most cecropins have an amphipathic N-terminal segment and a largely hydrophobic C-terminal segment, and normally form a helix-hinge-helix structure. In this study, we developed the novel 32-residue cecropin-like peptide cecropin DH by deleting the hinge region (Alanine-Glycine-Proline) of cecropin B isolated from Chinese oak silk moth, Antheraea pernyi. Cecropin DH possesses effective antibacterial activity, particularly against Gram-negative bacteria, with very low cytotoxicity against mammalian cells. Interactions between cecropin DH and the highly anionic lipopolysaccharide (LPS) component of the Gram-negative bacterial outer membrane indicate that it is capable of dissociating LPS micelles and disrupting LPS aggregates into smaller assemblies, which may play a vital role in its antimicrobial activity. Using LPS-stimulated mouse macrophage RAW264.7 cells, we found that cecropin DH exerted higher potential anti-inflammatory activity than cecropin B, as demonstrated by the inhibition of pro-inflammatory cytokines nitric oxide production and secretion of tumor necrosis factor-α. In conclusion, cecropin DH has potential as a therapeutic agent for both antibacterial and anti-inflammatory applications.
Highlights
In recent decades, antibiotic resistance has emerged as a major threat to global healthcare and food security (Furuya & Lowy, 2006), and new antibiotics are urgently needed.How to cite this article Wang et al (2018), A novel cecropin B-derived peptide with antibacterial and potential anti-inflammatory properties
The antimicrobial activities of cecropin DH were examined against three representative Gram-negative (E. coli ATCC25922, E. coli DH5a and P. aeruginosa) and three Gram-positive (B. subtilis, S. aureus and M. luteus) bacterial strains (Table 1), and compared with the activities of melittin, which is known to have profound antibacterial activities
The antimicrobial activities of the parent peptide cecropin B are listed for comparison
Summary
Antibiotic resistance has emerged as a major threat to global healthcare and food security (Furuya & Lowy, 2006), and new antibiotics are urgently needed.How to cite this article Wang et al (2018), A novel cecropin B-derived peptide with antibacterial and potential anti-inflammatory properties. AMPs are important immune effectors that are present in a wide variety of organisms including mammals, insects, vertebrates, amphibians, bacteria and plants (Bulet, Stocklin & Menin, 2004; Mishra et al, 2017; Tossi, Sandri & Giangaspero, 2000; Zasloff, 2002) These short 12–100 amino acid residue peptides often contain numerous positively charged arginines and lysines. AMPs can be classified based on secondary structure into a-helical peptides, b-sheet peptides, mixed a/b peptides and random coil peptides (Lakshmaiah Narayana & Chen, 2015) These peptides kill bacteria by disrupting cell membranes and/or interacting with internal targets (Brogden, 2005; Hancock & Sahl, 2006)
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