Fuscopeptins, antimicrobial lipodepsipeptides from Pseudomonas fuscovoginoe, are channel forming peptides active on biological and model membranes

M. Coraiola, R. Paletti, A. Fiore, V. Fogliano, Dalla Serra

Research output: Contribution to journalArticleAcademicpeer-review

12 Citations (Scopus)

Abstract

FP-A and FP-B are LDPs produced by the plant pathogen Pseudomonas fuscovaginae. As expected from their primary structure, they shared a similar mechanism of action with the better characterized SPs, synthesized by strains of Pseudomonas syringae pv. syringae. Indeed, they displayed hemolytic activity on human erythrocytes and were able to induce calcein release from LUVs: the effect was dependent on the concentration of the FPs and the lipid composition of the liposome and, in particular, it increased with the SM content of the membrane. The permeabilizing activity was further investigated on PLMs. FPs were able to open pores on pure POPC membranes. Pore opening was strongly voltage dependent: by switching the potential from negative to positive values, an increase in the absolute amplitude of transmembrane current was induced with simultaneous closure of pores. In 0.1 m KCl both FPs' pores had a conductance of 4 and 9 pS at - 140 mV and + 140 mV, respectively. Studies on ion selectivity indicated that FPs formed cation-selective channels.

Original languageEnglish
Pages (from-to)496-502
Number of pages7
JournalJournal of Peptide Science
Volume14
Issue number4
DOIs
Publication statusPublished - 17 Mar 2008
Externally publishedYes

Keywords

  • Antimicrobial peptide
  • Hemolysis
  • Ion channel
  • Lipid bilayer
  • Lipodepsipeptlde
  • Liposome
  • Pseudomonas fuscovaginae
  • Voltage gating

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