Structure and dynamics of the antifungal molecules Syringotoxin-B and Syringopeptin-25A from molecular dynamics simulation

The phytopathogen Pseudomonas syringae pv. syringae produces toxic cyclic lipodepsipeptides (CLPs): nona-peptides and syringopeptins. All CLPs inhibit the growth of many fungal species, including human pathogens, although different fungi display different degrees of sensitivity. The best studied CLP...

Full description

Saved in:
Bibliographic Details
Published in:European biophysics journal 2008-04, Vol.37 (4), p.495-502
Main Authors: Mátyus, E., Blaskó, K., Fidy, J., Tieleman, D. P.
Format: Article
Language:English
Subjects:
Antifungal Agents - pharmacology
Biochemistry
Biological and Medical Physics
Biomedical and Life Sciences
Biophysics
Biophysics - methods
Cell Biology
Computer Simulation
Fungal Proteins - chemistry
Fungi
Life Sciences
Lipid Bilayers - chemistry
Lipids
Lipids - chemistry
Magnetic Resonance Spectroscopy
Membrane Biology
Models, Chemical
Molecular biology
Molecular Conformation
Nanotechnology
Neurobiology
Original Paper
Peptides
Peptides - chemistry
Peptides, Cyclic - chemistry
Protein Conformation
Pseudomonas syringae - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The phytopathogen Pseudomonas syringae pv. syringae produces toxic cyclic lipodepsipeptides (CLPs): nona-peptides and syringopeptins. All CLPs inhibit the growth of many fungal species, including human pathogens, although different fungi display different degrees of sensitivity. The best studied CLPs are Syringomycin-E (SR-E), Syringotoxin-B (ST-B) and Syringopeptin-25A (SP-25A). Their biological activity is affected by membrane composition and their structural differences. We previously (Matyus et al. in Eur Biophys J 35:459–467, 2006 ) reported the molecular features and structural preferences of SR-E in water and octane environments. Here we investigate in atomic detail the molecular features of the two other main CLP components, ST-B and SP-25A, in water and octane by 200 ns molecular dynamics simulations (MD), using distance restraints derived from NMR NOE data (Ballio et al. in Eur J Biochem 234:747–758, 1995 ). We have obtained three-dimensional models of ST-B and SP-25A CLPs in different environments. These models can now be used as a basis to investigate the interactions of ST-B and SP-25A with lipid membranes an important further step towards a better understanding of the antifungal and antibacterial activity of these peptides.
ISSN:0175-7571
1432-1017
DOI:10.1007/s00249-007-0242-3