Characterisation of antibiotic moenomycin A interaction with phospholipid model membranes.
Using a combination of physico-chemical techniques (MAS NMR, DSC, freeze-fracture electron microscopy, molecular modelling) the antibiotic moenomycin A was found to be anchored by its hydrophobic chain into multilamellar POPC membranes. The lamellar phase structure of the modified membrane is retained, while moenomycin A in water at different concentrations does not form any other but isotropic phase structures. The mobility of POPC molecule segments is reduced with increasing moenomycin A concentrations. Freeze-fracture electron microscopy images show ripple like structures for low moenomycin A concentrations, which are rare for high concentrations. A sugar-group network of the antibiotic seems to cover the whole membrane surface for molar ratios moenomycin A/POPC of 1:2, which is supported by 13C-MAS (Magic Angle Spinning) 31P-NMR, and molecular modelling.
Volke
F
F
Universität Leipzig, Fakultät für Physik und Geowissenschaften, Leipzig, Germany. volke@rz.uni-leipzig.de
Waschipky
R
R
Pampel
A
A
Donnerstag
A
A
Lantzsch
G
G
Pfeiffer
H
H
Richter
W
W
Klose
G
G
Welzel
P
P
D001455:Bambermycins / Q000737:chemistry* / Q000378:metabolism*; D002152:Calorimetry, Differential Scanning; D008081:Liposomes / Q000737:chemistry / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008563:Membrane Lipids / Q000737:chemistry / Q000378:metabolism; D008854:Microscopy, Electron; D008958:Models, Molecular; D015394:Molecular Structure; D010713:Phosphatidylcholines / Q000378:metabolism; D010743:Phospholipids / Q000737:chemistry / Q000378:metabolism*; D013696:Temperature
D008081:Liposomes; D008563:Membrane Lipids; D010713:Phosphatidylcholines; D010743:Phospholipids; D001455:Bambermycins