Inhibitory action of a truncated derivative of the amphibian skin peptide Dermaseptin s3 on Saccharomyces cerevisae

Peter John Coote, CD Holyoak, D Bracey, DP Ferdinando, other 1

Research output: Contribution to journalArticlepeer-review

44 Citations (Scopus)

Abstract

The inhibitory activity of a truncated derivative of the natural amphibian skin peptide dermaseptin s3-(1-16)-NH2 [DS s3 (1-16)] against Saccharomyces cerevisiae was studied. Significant growth inhibition was observed after exposure to 3.45 mu g of the peptide per mi at pH 6.0 and 7.0, with complete growth inhibition occurring at 8.63 mu g of peptide per mi for all pH values tested. Using confocal scanning laser microscopy, we have shown that DS s3 (1-16) disrupted the yeast cell membrane resulting in the gross permeabilization of the cell to the nuclear stain ethidium bromide, However, the principal inhibitory action of the peptide was not due to disruption of intracellular pH homeostasis. Instead, growth inhibition by the peptide correlated with the efflux of important cellular constituents such as ADP, ATP, RNA, and DNA into the surrounding medium. The combination of DS s3 (1-16) with mild heating temperatures as low: as 35 degrees C significantly enhanced the inhibitory effect of the peptide (8.63 mu g/ml), and at 45 degrees C greater than 99% of the population was killed in 10 min. In summary, a derivative of a natural antimicrobial peptide has potential, either alone or in combination with mild heating, to prevent the growth of or kill spoilage yeast.

Original languageEnglish
Pages (from-to)2160-2170
Number of pages11
JournalAntimicrobial Agents and Chemotherapy
Volume42
Issue number9
Publication statusPublished - Sept 1998

Keywords

  • MEMBRANE H+-ATPASE
  • ANTIMICROBIAL PEPTIDES
  • CATIONIC PEPTIDES
  • SEQUENCE
  • THERMOTOLERANCE
  • MAGAININ-2
  • DEFENSINS
  • PH

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