Partitioning of Gramicidin A’ Between Coexisting Phases within Phospholipid Bilayers

  • Andrew R. G. Dibble
  • Mark D. Yeager
  • Gerald W. Feigenson


We investigated the partitioning behavior of gramicidin A′ in various binary phospholipid mixtures in which gel and liquid crystalline phase coexistence had been induced. The quenching of the gramicidin A′ tryptophanyl fluorescence by a spin-labeled phosphatidylcholine was used to determine the equilibrium ratio of gramicidin A′ concentration in the liquid crystalline phase to that in the gel phase (i.e. the partition coefficient, KP). Three multilamellar vesicular systems, differing in the order and rigidity of the gel phase, were compared. The phospholipid content of the gel phase was rich in dipalmitoylphosphatidylcholine or distearoylphosphatidylcholine, or was entirely Ca(dioleoylphosphatidylserine)2. In all cases the gel phase was depleted of gramicidin A′, with KP = 10 ± 2, 25 ± 5, and ≥30, respectively. These data suggest that the more ordered the gel phase, the less it can accommodate a transmembrane polypeptide.


Electron Paramagnetic Resonance Mole Fraction Coat Protein Fluorescence Quenching Liquid Crystalline Phase 
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  1. Caffrey, M., and Feigenson, G.W. (1981) Biochemistry 20, 1949–1961.PubMedCrossRefGoogle Scholar
  2. Datema, K.P., Spruijt, R.B., Wolfs, C.J.A.M., and Hemminga, M.A. (1988) Biochim. Biophys. Acta 944, 507–515.PubMedCrossRefGoogle Scholar
  3. Engelman, D.M. (1970) J. Mol. Biol. 47, 115–117.PubMedCrossRefGoogle Scholar
  4. Florine, K.I., and Feigenson, G.W. (1987a) Biochemistry 26, 1757–1768.CrossRefGoogle Scholar
  5. Florine, K.I., and Feigenson, G.W. (1987b) Biochemistry 26, 2978–2983.CrossRefGoogle Scholar
  6. Huang, N., Florine-Casteel, K., Feigenson, G.W., and Spink, C. (1988) Biochim.Biophys. Acta 939, 124–130.PubMedCrossRefGoogle Scholar
  7. Kingsley, P.B., and Feigenson, G.W. (1979) Chem. Phys. Lipids 24, 135–147.CrossRefGoogle Scholar
  8. Kleeman, W., and McConnell, H.M. (1976) Biochim. Biophys. Acta 419, 206–222.CrossRefGoogle Scholar
  9. London, E., and Feigenson, G.W. (1981a) Biochemistry 20, 1932–1938.CrossRefGoogle Scholar
  10. London, E., and Feigenson, G.W. (1981b) Biochim. Biophys. Acta 649, 89–97.CrossRefGoogle Scholar
  11. Portis, A., Newton, C., Pangborn, W., and Papahadjopoulos, D. (1979) Biochemistry 18, 780–790.PubMedCrossRefGoogle Scholar
  12. Steim, J.M., Tourtellotte, M.E., Reinert, J.C., McElhaney, R.N., and Rader, R.L. (1969) Proc. Natl. Acad. Sci. U.S.A. 63, 104–109.PubMedCrossRefGoogle Scholar
  13. Thilo, L., Trauble, H., and Overath, P. (1977) Biochemistry 26, 1283–1290.CrossRefGoogle Scholar
  14. Urry, D.W. (1971) Proc. Natl. Acad. Sci. U.S.A. 68, 672–676.PubMedCrossRefGoogle Scholar
  15. Urry, D.W., Goodall, M.C., Glickson, J.D., and Mayers, D.F. (1971) Proc. Natl. Acad. Sci. U.S.A. 68,1907–1911.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1991

Authors and Affiliations

  • Andrew R. G. Dibble
    • 1
  • Mark D. Yeager
    • 1
  • Gerald W. Feigenson
    • 1
  1. 1.Section of BiochemistryMolecular and Cell Biology Cornell UniversityIthacaUSA

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