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Biophys J, February 2002, p. 843-851, Vol. 82, No. 2

Thermotropic Phase Behavior of Monoglyceride-Dicetylphosphate Dispersions and Interactions with Proteins: A 2H and 31P NMR Study

V. Chupin, J. W. P. Boots, J. A. Killian, R. A. Demel, and B. de Kruijff

Department Biochemistry of Membranes, Centre for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands

The phase behavior of a 1-[2H35]-stearoyl-rac-glycerol ([2H35]-MSG)/dicetylphosphate (DCP) mixture and its interaction with beta -lactoglobulin and lysozyme were studied by 2H and 31P nuclear magnetic resonance (NMR). The behavior of the lipids was monitored by using deuterium-labeled [2H35]-MSG as a selective probe for 2H NMR and DCP for 31P NMR. Both 2H and 31P NMR spectra exhibit characteristic features representative of different phases. In the lamellar phases, 31P NMR spectra of DCP are different from the spectra of natural phospholipids, which is attributable to differences in the intramolecular motions and the orientation of the shielding tensor of DCP compared with phospholipids. The presence of the negatively charged amphiphile DCP has a large effect on the phase behavior of [2H35]-MSG. At low temperature, the presence of DCP inhibits crystallization of the gel phase into the coagel. Upon increasing the temperature, the gel phase of [2H35]-MSG transforms in the liquid-crystalline lamellar phase. In the presence of DCP, the gel phase directly transforms into an isotropic phase. The negatively charged beta -lactoglobulin and the positively charged lysozyme completely neutralize the destabilizing effect of DCP on the monoglyceride liquid-crystalline phase and they even stabilize this phase. Without DCP the proteins do not seem to interact with the monoglyceride. These results suggest that interaction is facilitated by electrostatic interactions between the negatively charged DCP and positively charged residues in the proteins. In addition, the nonbilayer-forming DCP creates insertion sites for proteins in the bilayer.

Biophys J, February 2002, p. 843-851, Vol. 82, No. 2
© 2002 by the Biophysical Society   0006-3495/02/02/843/09  $2.00


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V. Chupin, J. A. Killian, and B. de Kruijff
Effect of Phospholipids and a Transmembrane Peptide on the Stability of the Cubic Phase of Monoolein: Implication for Protein Crystalization from a Cubic Phase
Biophys. J., April 1, 2003; 84(4): 2373 - 2381.
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