Not only the nature of peptide but also the characteristics of cell membrane determine the antimicrobial mechanism of a peptide

Jun F. Liang, S. C. Kim

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

The mechanisms of antimicrobial actions of magainin 2, buforin II and poly L-lysine against various Escherichia coli strains were studied. Poly L- lysine inhibited BL21, AD 434 and GroE+/DnaK+ growth without lysing the cell. Magainin 2 had a pore-forming activity on BL 21 and AD 434 membrane but could not inhibit the GroE+/DnaK+ growth in a nutrient-rich medium. Buforin II, which killed BL21 and AD 434 without cell membrane damage, lysed GroE+/DnaK+ to death. Once they were introduced into the cell by electroporation, all three peptides were able to inhibit cell growth at concentrations of 10 times lower than their MICs. These results indicate that the nature of the peptide and also the characteristics of the cell membrane determine the antimicrobial actions of a peptide.

Original languageEnglish
Pages (from-to)518-522
Number of pages5
JournalJournal of Peptide Research
Volume53
Issue number5
DOIs
StatePublished - 1999

Keywords

  • Antimicrobial
  • Electroporation
  • Escherichia coli
  • Mechanism
  • Peptide

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