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

Protein Pept Lett. 2002 Oct;9(5):395-402. doi: 10.2174/0929866023408535.

Abstract

P18 (KWKLFKKIPKFLHLAKKF-NH(2)), an a-helical antimicrobial peptide designed from cecropin Amagainin 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 antimicrobial 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antimicrobial Cationic Peptides / chemistry
  • Antimicrobial Cationic Peptides / pharmacology*
  • Bacteria / drug effects
  • Fungi / drug effects
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Structure-Activity Relationship

Substances

  • Antimicrobial Cationic Peptides
  • P18 antimicrobial peptide