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

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

*Corresponding author for this work

Research output: Contribution to journalConference article

7 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 - Apr 2008
Externally publishedYes
Event2nd Workshop on Biophysics of Membrane-Active Peptides - Science Museum, Lisbon, Portugal
Duration: 1 Apr 20073 Apr 2007
Conference number: 2

Cite this

@article{48740b930c7a4c2ca11bac13e57db3d7,
title = "Fuscopeptins, antimicrobial lipodepsipeptides from Pseudomonas fuscovaginae, are channel forming peptides active on biological and model membranes",
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.",
author = "M. Coraiola and R. Paletti and A. Fiore and V. Fogliano and {Dalla Serra}, M.",
year = "2008",
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doi = "10.1002/psc.970",
language = "English",
volume = "14",
pages = "496--502",
journal = "Journal of Peptide Science",
issn = "1075-2617",
publisher = "Wiley-Blackwell",
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Fuscopeptins, antimicrobial lipodepsipeptides from Pseudomonas fuscovaginae, are channel forming peptides active on biological and model membranes. / Coraiola, M.; Paletti, R.; Fiore, A.; Fogliano, V.; Dalla Serra, M.

In: Journal of Peptide Science, Vol. 14, No. 4, 04.2008, p. 496-502.

Research output: Contribution to journalConference article

TY - JOUR

T1 - Fuscopeptins, antimicrobial lipodepsipeptides from Pseudomonas fuscovaginae, are channel forming peptides active on biological and model membranes

AU - Coraiola, M.

AU - Paletti, R.

AU - Fiore, A.

AU - Fogliano, V.

AU - Dalla Serra, M.

PY - 2008/4

Y1 - 2008/4

N2 - 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.

AB - 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.

U2 - 10.1002/psc.970

DO - 10.1002/psc.970

M3 - Conference article

VL - 14

SP - 496

EP - 502

JO - Journal of Peptide Science

JF - Journal of Peptide Science

SN - 1075-2617

IS - 4

ER -