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31P and19F NMR studies of glycophorin-reconstituted membranes: Preferential interaction of glycophorin with phosphatidylserine

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Summary

Glycophorin A, a major glycoprotein of the erythrocyte membrane, has been incorporated into small unilamellar vesicles composed of a variety of pure and mixed phospholipids. Nuclear spin labels including31P and19F have been used at natural abundance or have been synthetically incorporated in lipids to act as probes of lipid-protein interaction. Interactions produce broadening of resonances in several cases and it can be used to demonstrate preferential interaction of certain lipids with glycophorin.31P and19F probes show a strong preferential interaction of glycophorin with phosphatidylserine over phosphatidylcholine. There is some evidence that interactions are more pronounced at the inner surface of the bilayer and these results are rationalized in terms of the asymmetric distribution of protein and lipid.

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  1. Richard L. Ong

    Present address: Division of Endocrinology and Metabolism, The University of Alabama in Birmingham Medical Center, 35294, Birmingham, Alabama

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  1. Department of Chemistry, Yale University, 06511, New Haven, Connecticut

    Richard L. Ong

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Ong, R.L. 31P and19F NMR studies of glycophorin-reconstituted membranes: Preferential interaction of glycophorin with phosphatidylserine. J. Membrain Biol. 78, 1–7 (1984). https://doi.org/10.1007/BF01872526

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  • DOI: https://doi.org/10.1007/BF01872526

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