Abstract
Lipodepsipeptides (LPDs) are a group of cyclic, acylated peptides produced by several Pseudomonas species. They are usually divided in two groups, mycins and peptins, on the basis of the size of the amino acidic part of the molecule. Mycins have a ring of 9 amino acids closed between the first and the last residue, peptins contain a more complex peptide moiety of up to 25 amino acids, partially cyclized. Both mycins and peptins attack the plasma membrane, but may have different target organisms. Comparing the mode of action of these two classes of LDPs on natural and model membranes we observed that all peptides induced red blood cell haemolysis and leakage of tonoplasts and liposornes by the formation of pores. The haemolytic activity of the smaller mycins was higher than that of the bigger peptins and proportional to the amphipathic index of the molecule. The extent of permeabilization was dependent also on the composition of the lipid membrane. In particular, mycins show a preference for sterols, whereas peptins are more active on phospholipids, especially sphingomyelin. These differences may have physiological implications. The formation of discrete ion channels, with anionic selectivity, was directly demonstrated by electrophysiological experiments performed on planar lipid bilayers or sugar beet vacuoles. The channels show sub-states and their properties in vacuoles and in planar lipid membranes were remarkably similar.
| Original language | English |
|---|---|
| Title of host publication | Pseudomonas syringae and related pathogens |
| Subtitle of host publication | biology and genetic |
| Editors | Nicola Sante Iacobellis, Alan Collmer, Steven W. Hutcheson, John W. Mansfield, Cindy E. Morris, Jesus Murillo, Norman W. Schaad, David E. Stead, Giuseppe Surico, Matthias S. Ullrich |
| Place of Publication | Dordrecht |
| Publisher | Springer |
| Pages | 185-198 |
| Number of pages | 14 |
| ISBN (Electronic) | 9789401701334 |
| ISBN (Print) | 9781402012273, 9789048162673 |
| DOIs | |
| Publication status | Published - 2003 |
| Externally published | Yes |
| Event | 6th International Conference on Pseudomonas Syringae Pathovars and Related Pathogens - Maratea, Italy Duration: 15 Sep 2002 → 19 Sep 2002 Conference number: 6 |
Conference
| Conference | 6th International Conference on Pseudomonas Syringae Pathovars and Related Pathogens |
|---|---|
| Country | Italy |
| City | Maratea |
| Period | 15/09/02 → 19/09/02 |
Cite this
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Antimicrobial lipodepsipeptides from Pseudomonas spp : a comparison of their activity on model membranes. / Menestrina, G; Coraiola, M; Fogliano, V.; Fiore, A; Grgurina, I.; Carpaneto, A; Gambale, F; Serra, MD.
Pseudomonas syringae and related pathogens: biology and genetic. ed. / Nicola Sante Iacobellis; Alan Collmer; Steven W. Hutcheson; John W. Mansfield; Cindy E. Morris; Jesus Murillo; Norman W. Schaad; David E. Stead; Giuseppe Surico; Matthias S. Ullrich. Dordrecht : Springer, 2003. p. 185-198.Research output: Chapter in Book/Report/Conference proceeding › Conference contribution
TY - GEN
T1 - Antimicrobial lipodepsipeptides from Pseudomonas spp
T2 - a comparison of their activity on model membranes
AU - Menestrina, G
AU - Coraiola, M
AU - Fogliano, V.
AU - Fiore, A
AU - Grgurina, I.
AU - Carpaneto, A
AU - Gambale, F
AU - Serra, MD
PY - 2003
Y1 - 2003
N2 - Lipodepsipeptides (LPDs) are a group of cyclic, acylated peptides produced by several Pseudomonas species. They are usually divided in two groups, mycins and peptins, on the basis of the size of the amino acidic part of the molecule. Mycins have a ring of 9 amino acids closed between the first and the last residue, peptins contain a more complex peptide moiety of up to 25 amino acids, partially cyclized. Both mycins and peptins attack the plasma membrane, but may have different target organisms. Comparing the mode of action of these two classes of LDPs on natural and model membranes we observed that all peptides induced red blood cell haemolysis and leakage of tonoplasts and liposornes by the formation of pores. The haemolytic activity of the smaller mycins was higher than that of the bigger peptins and proportional to the amphipathic index of the molecule. The extent of permeabilization was dependent also on the composition of the lipid membrane. In particular, mycins show a preference for sterols, whereas peptins are more active on phospholipids, especially sphingomyelin. These differences may have physiological implications. The formation of discrete ion channels, with anionic selectivity, was directly demonstrated by electrophysiological experiments performed on planar lipid bilayers or sugar beet vacuoles. The channels show sub-states and their properties in vacuoles and in planar lipid membranes were remarkably similar.
AB - Lipodepsipeptides (LPDs) are a group of cyclic, acylated peptides produced by several Pseudomonas species. They are usually divided in two groups, mycins and peptins, on the basis of the size of the amino acidic part of the molecule. Mycins have a ring of 9 amino acids closed between the first and the last residue, peptins contain a more complex peptide moiety of up to 25 amino acids, partially cyclized. Both mycins and peptins attack the plasma membrane, but may have different target organisms. Comparing the mode of action of these two classes of LDPs on natural and model membranes we observed that all peptides induced red blood cell haemolysis and leakage of tonoplasts and liposornes by the formation of pores. The haemolytic activity of the smaller mycins was higher than that of the bigger peptins and proportional to the amphipathic index of the molecule. The extent of permeabilization was dependent also on the composition of the lipid membrane. In particular, mycins show a preference for sterols, whereas peptins are more active on phospholipids, especially sphingomyelin. These differences may have physiological implications. The formation of discrete ion channels, with anionic selectivity, was directly demonstrated by electrophysiological experiments performed on planar lipid bilayers or sugar beet vacuoles. The channels show sub-states and their properties in vacuoles and in planar lipid membranes were remarkably similar.
U2 - 10.1007/978-94-017-0133-4_20
DO - 10.1007/978-94-017-0133-4_20
M3 - Conference contribution
SN - 9781402012273
SN - 9789048162673
SP - 185
EP - 198
BT - Pseudomonas syringae and related pathogens
A2 - Iacobellis, Nicola Sante
A2 - Collmer, Alan
A2 - Hutcheson, Steven W.
A2 - Mansfield, John W.
A2 - Morris, Cindy E.
A2 - Murillo, Jesus
A2 - Schaad, Norman W.
A2 - Stead, David E.
A2 - Surico, Giuseppe
A2 - Ullrich, Matthias S.
PB - Springer
CY - Dordrecht
ER -