31P and 19F NMR studies of glycophorin-reconstituted membranes: preferential interaction of glycophorin with phosphatidylserine.
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 including 31P and 19F 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 and 19F 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.
D005461:Fluorine; D006021:Glycophorins / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008567:Membranes, Artificial; D010713:Phosphatidylcholines / Q000378:metabolism; D010714:Phosphatidylethanolamines / Q000378:metabolism; D010718:Phosphatidylserines / Q000378:metabolism*; D010761:Phosphorus Radioisotopes; D011868:Radioisotopes; D012795:Sialoglycoproteins / Q000378:metabolism*
D006021:Glycophorins; D008567:Membranes, Artificial; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D010718:Phosphatidylserines; D010761:Phosphorus Radioisotopes; D011868:Radioisotopes; D012795:Sialoglycoproteins; D005461:Fluorine