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Interaction of a bacterial monorhamnolipid secreted by Pseudomonas aeruginosa MA01 with phosphatidylcholine model membranes
Authors:Habib Abbasi  Kambiz Akbari Noghabi  Antonio Ortiz
Institution:1. Department of Chemical Engineering, Jundi-Shapur University of Technology, Dezful, Iran;2. Department of Molecular Genetics, National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Iran;3. Department of Biochemistry and Molecular Biology-A, Veterinary Faculty, University of Murcia, E-30100 Murcia, Spain
Abstract:This work presents a biophysical study on the interactions of a monorhamnolipid (monoRL) produced by Pseudomonas aeruginosa MA01 with model phosphatidylcholine membranes. The molecular characterization of the biological activities, including the modulation of phospholipid membranes structure, of this monoRL biosurfactant is of importance for the validation of this particular Pseudomonas aeruginosa strain as a useful biosurfactant producer. The marked amphiphilic structure of monoRL is expected to result in strong interactions with the phospholipid constituents of membrane bilayers. Incorporation of monoRL into DMPC completely abolished the pretransition, and the main gel to liquid-crystalline phase transition was progressively broadened and shifted to lower temperatures, as observed by differential scanning calorimetry. Partial phase diagrams for DPPC and DSPC indicated near-ideal behavior. However, the DMPC diagram indicated fluid phase immiscibility. X-ray diffraction showed and apparent increase in d-value for DPPC containing monoRL, which might be the result of an effective increase in the bilayer thickness, or in the thickness of the hydration layer between bilayers. FTIR indicated that interaction of monoRL with the phospholipid acyl chains did not result in a large additional disordering of the acyl chain region of the fluid bilayer. Analysis of the Cdouble bondO stretching band of DPPC indicated an important effect of monoRL on the interfacial region of phosphatidylcholine bilayers, which might contribute to explain some of the biological activities of this glycolipid.
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