Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10798241 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2005 | 12 Pages |
Abstract
Mes-Y105 was also studied by polarization modulation infrared reflection absorption spectroscopy (PMIRRAS), alone and in various phospholipid environments, to obtain structural information and to assess lipid perturbations. At nanomolar concentrations close to those required for anti-Listeria activity, Mes-Y105 forms films at the air/water interface and inserts into negatively charged lipid monolayers. In situ infrared data show that Mes-Y105 binding only affects the polar head group vibrations while the lipid order of the acyl chains remains unaffected. The PMIRRAS show that Mes-Y105 folds into an N-terminal antiparallel β-sheet followed by an α-helix, both structures being tilted (40°) compared to the normal at the interface, which is in agreement with the thickness estimated by Brewster angle microscopy (BAM). All these data support the proposal of a new model for Mes-Y105 at the membrane interface.
Keywords
TFEdimyristoyl-phosphatidylglycerolpolarization modulation infrared reflection absorption spectroscopyPMIRRASPeptide orientationdimyristoyl-phosphatidylcholineDPPGDMPGtrifluoroethanolPoPCdMPCEPCFluorescence resonance energy transferFRETBacteriocinBAMegg phosphatidylcholinecircular dichroismPhosphatidylserineFluorescence
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Authors
Sabine Castano, Bernard Desbat, Antoine Delfour, Jean Marie Dumas, Alexandra da Silva, Jean Dufourcq,