Domain formation by a Rhodococcus sp. biosurfactant trehalose lipid incorporated into phosphatidylcholine membranes

• Published in: Biochimica et biophysica acta 2007-10, Vol.1768 (10), p.2596-2604
• Main Authors: Aranda, Francisco J., Teruel, José A., Espuny, María J., Marqués, Ana, Manresa, Ángeles, Palacios-Lidón, Elisa, Ortiz, Antonio
• Format: Article
• Language: English
• Subjects: Biosurfactant; Calorimetry, Differential Scanning; Glycolipids - chemistry; Lipid Bilayers - chemistry; Membrane domain; Phosphatidylcholines - chemistry; Phospholipid membrane; Rhodococcus - chemistry; Spectroscopy, Fourier Transform Infrared; Surface-Active Agents - chemistry; Trehalose - chemistry; Trehalose lipid; X-Ray Diffraction
• ISSN: 0005-2736; 0006-3002; 1879-2642
• DOI: 10.1016/j.bbamem.2007.06.016

The study of the interaction of biosurfactants with biological membranes is of great interest in order to gain insight into the molecular mechanisms of their biological actions. In this work we report on the interaction of a bacterial trehalose lipid produced by Rhodococcus sp. with phosphatidylcholine membranes. Differential scanning calorimetry measurements show a good miscibility of the glycolipid in the gel state and immiscibility in the fluid state, suggesting domain formation. These domains have been visualized and characterized, for the first time, by scanning force microscopy. Incorporation of trehalose lipid into phosphatidylcholine membranes produces a small shift of the antisymmetric stretching band toward higher wavenumbers, as shown by FTIR, which indicates a weak increase in fluidity. The C O stretching band shows that incorporation of trehalose lipid increases the proportion of the dehydrated component in mixtures with the three phospholipids at temperatures below and above the gel to liquid–crystalline phase transition. This dehydration effect is also supported by data on the phospholipid P O stretching bands. Small-angle X-ray diffraction measurements show that in the samples containing trehalose lipid the interlamellar repeat distance is larger than in those of pure phospholipids. These results are discussed within the frame of trehalose lipid domain formation, trehalose lipid/phospholipid interactions and its relevance to membrane-related biological actions.