Antibiotic activity of reversed peptides of α-helical antimicrobial peptide, P18

Si Hyung Lee, Dong Gun Lee, Sung Tae Yang, Yangmee Kim, Jae Il Kim, Kyung Soo Hahm, Song Yub Shin

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

P18 (KWKLFKKIPKFLHLAKKF-NH2), an α-helical antimicrobial peptide designed from cecropin A-magainin 2 hybrid, was known to have potent antimicrobial activity against bacteria as well as fungi without hemolytic activity. To find the peptides comparable or superior to the antimicrobiai activity of P18, the two reversed peptides (Rev-1 and Rev-2) of P18 were designed and synthesized. These peptides were found to have similar antimicrobial activity against bacterial and fungal cells without hemolytic activity as compared with P18. Furthermore, a reversed peptide, Rev-2 was shown to have a two-fold higher activity in killing some bacterial cells than P18. Therefore, these results suggested that Rev-2 peptide seems to be an excellent candidate for developing novel peptide antibiotics.

Original languageEnglish
Pages (from-to)395-402
Number of pages8
JournalProtein and Peptide Letters
Volume9
Issue number5
DOIs
StatePublished - 2002

Keywords

  • α-helicity
  • Antimicrobial activity
  • Antimicrobial peptide
  • Hemolytic activity
  • P18
  • Reversed peptide

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