Effect of glycophorin on lipid polymorphism: A 31P-NMR study |
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Authors: | TF Taraschi B de Kruijff A Verkleij CJA van Echteld |
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Institution: | 1. Laboratory of Biochemistry, State University of Utrecht, Padualaan 8, NL 3584 CII Utrecht The Netherlands;2. Institute of Molecular Biology, State University of Utrecht, Padualaan 8, NL 3584 CII Utrecht The Netherlands |
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Abstract: | (1) The effect of glycophorin, a major intrinsic glycoprotein of the human erythrocyte membrane, on lipid polymorphism has been investigated by 31P-NMR (at 36.4 MHz) and by freeze-fracture electron microscopy. (2) Incorporation of glycophorin into vesicles of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) results in the formation of unilamellar vesicles (1000–5000 Å diameter) which exhibit 31P-NMR bilayer spectra over a wide range of temperature. A reduction in the chemical shift anisotropy (Δσcsaeff) and an increase in spectral linewidth in comparison to dioleoylphosphatidylcholine liposomes may suggest a decrease in phospholipid headgroup order. (3) 1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE), in the presence of excess water, undergoes a bilayer to hexagonal (HII) phospholipid arrangement as the temperature is increased above 0°C. Incorporation of glycophorin into this system stabilizes the bilayer configuration, prohibiting the formation of the HII phase. (4) Cosonication of glycophorin with DOPE in aqueous solution (pH 7.4) produces small, stable unilamellar vesicles (300–1000 Å diameter), unlike DOPE alone which is unstable and precipitates from solution. (5) The current study demonstrates the bilayer stabilizing capacity of an intrinsic membrane protein, glycophorin, most likely by means of a strong hydrophobic interaction between the membrane spanning portion of glycophorin and the hydrophobic region of the phospholipid. |
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Keywords: | Glycophorin Lipid polymorphism DOPC DOPE effective phosphorus-31 chemical shift anisotropy linewidth at half maximum spectral intensity |
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