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- Title
Short Antimicrobial Peptides Exhibiting Antibacterial and Anti-Inflammatory Activities Derived from the N-Terminal Helix of Papiliocin.
- Authors
Jeon, Dasom; Jacob, Binu; Kwak, Chulhee; Kim, Yangmee
- Abstract
Papiliocin is a 37-residue antimicrobial peptide, with Trp2 and Phe5 previously reported as key residues necessary for its antibacterial activity. This study determined the essential length of the N-terminal fragment of papiliocin necessary to retain its biological activity. We designed and synthesized an array of seven peptides from the N-terminal helix (PapN), with longest peptide with 22 residues and the shortest peptide consisting of the first 10 residues. The minimum inhibitory concentration (MIC) values and cytotoxicity measurement revealed that a PapN-12mer containing a three-turn, amphipathic helix was the shortest peptide exhibiting antibacterial activity without cytotoxicity. Additionally, PapN-20mer peptide containing two isoleucines at the C-terminus represented the shortest peptide exhibiting potent anti-inflammatory activities by inhibiting nitric oxide production and inflammatory cytokine production in lipopolysaccharide-stimulated mouse macrophage RAW264.7 cells. These results provided valuable insights into the design of short, potent peptide analogs of papiliocin.
- Subjects
PEPTIDE drugs; HELICAL structure; INFLAMMATION; ANTI-infective agents; INHIBITORY Concentration 50; CYTOKINES
- Publication
Bulletin of the Korean Chemical Society, 2017, Vol 38, Issue 11, p1260
- ISSN
0253-2964
- Publication type
Article
- DOI
10.1002/bkcs.11277