, Volume 5, Issue 7, pp 636–649 | Cite as

Lipid monolayers: Mechanisms of protein penetration with regard to membrane models

  • Giuseppe Colacicco


The influence of lipid and protein on the properties of the air-water interface is analyzed with the view to formulate a mechanism of interaction of protein with lipid monolayers. The increase in surface pressure (ΔΠ) and the quantity of protein incorporated in the lipid film after injection of protein under lipid monolayers were studied as a function of both lipid structure and protein structure. With rabbit γ-globulin, the values of ΔΠ were cholesterol > phosphatidyl choline > sphingomyelin. Similar results were obtained with ribonuclease, lysozyme and serum albumin. The quantities of protein found in films of either cholesterol or phosphatidyl choline (egg lecithin) were much larger than those calculated from a geometric model in which a protein monolayer occupies the area made available by the compressed lipid. Arguments are produced against penetration based on simple mechanisms of compressibility of the lipid film. The mechanisms operating in the incorporation of protein into lipid monolayers are grouped into three categories: (a) free penetration, typical of lecithin; (b) binding-mediated penetration, typical of cholesterol and some glycosphingolipids; and (c) binding-inhibited penetration, typical of the albumin-ganglioside system and a specific lipid hapten-antibody system. A model is described in which nonspecific protein interacts with polymeric lecithin structures (surface micelles). In the sequence of events X»Y»Z, the globular protein X is activated into the expanded or extended form Y by contact with the lipid and then restructured into a compact form Z with release of water and free energy. The resulting lipid-protein assembly has a mosaic structure in which lipid and protein polar surfaces are exposed to water. Accessibility of lecithin to phospholipase A is consistent with the model and with current views on the state of protein in biological membranes; according to such views, protein is more likely structured inside the lipid milieu and not simply denatured on the lipid-water interface.


Lecithin Phosphatidyl Choline Lipid Film Lipid Monolayer Film Pressure 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Colacicco, G., and M. M. Rapport, J. Lipid Res. 7:258–263 (1966).PubMedGoogle Scholar
  2. 2.
    Shah, D. O., and J. H. Schulman, J. Colloid Interface Sci. 25:107–119 (1967).CrossRefGoogle Scholar
  3. 3.
    Bangham, A. D., and R. M. C. Dawson, Biochem. J. 75:133–138 (1960).PubMedGoogle Scholar
  4. 4.
    Colacicco, G., M. M. Rapport and D. Shapiro, J. Colloid Interface Sci. 25:5–15 (1967).CrossRefGoogle Scholar
  5. 5.
    Colacicco, G., and M. M. Rapport, Adv. Chem. Series 84:157–168 (1968).Google Scholar
  6. 6.
    Doty, P., and J. H. Schulman, Discuss. Faraday Soc. 6:21–27 (1949).CrossRefGoogle Scholar
  7. 7.
    Eley, D. D., and D. G. Hedge, Ibid. 21:221–228 (1956).CrossRefGoogle Scholar
  8. 8.
    Eley, D. D., and D. G. Hedge, J. Colloid Sci. 11:445–450 (1956).CrossRefGoogle Scholar
  9. 9.
    Khaiat, A., and I. R. Miller, Biochim. Biophys. Acta 183:309–319 (1969).PubMedCrossRefGoogle Scholar
  10. 10.
    Colacicco, G., J. Colloid Interface Sci. 29:345–364 (1969).PubMedCrossRefGoogle Scholar
  11. 11.
    Camejo, G., G. Colacicco and M. M. Rapport, J. Lipid Res. 9:562–569 (1968).PubMedGoogle Scholar
  12. 12.
    Danielli, J. F., and H. A. Davson, J. Cell. Comp. Physiol. 5:495–508 (1935).CrossRefGoogle Scholar
  13. 13.
    Sjostrand, F. A., Nature 199:1262–1264 (1963).CrossRefGoogle Scholar
  14. 14.
    Benson, A. A., JAOCS 43:265–270 (1966).PubMedGoogle Scholar
  15. 15.
    Lenard, J., and S. J. Singer, Proc. Natl. Acad. Sci. U.S.A. 56:1828–1835 (1966).PubMedCrossRefGoogle Scholar
  16. 16.
    Robertson, J. D., Progr. Biophysics 10:343–418 (1960).Google Scholar
  17. 17.
    Colacicco, G., “Membrane Models.” Read before the Third International Conference on Biological Membranes. Stresa, Italy, June 1969.Google Scholar
  18. 18.
    Ledeen, R., JAOCS 43:57–66 (1966).PubMedGoogle Scholar
  19. 19.
    Satake, M., Y. Murata and T. Suzuki, J. Biochem. Tokyo 53:438–447 (1963).PubMedGoogle Scholar
  20. 20.
    Hughes, A., Biochem. J. 29:437–444 (1935).PubMedGoogle Scholar
  21. 21.
    Schulman, J. H., and E. K. Rideal, Ibid. 27:1581–1597 (1933).PubMedGoogle Scholar
  22. 22.
    Yamashita, T., and H. B. Bull, J. Colloid Interface Sci. 24:310–316 (1967).PubMedCrossRefGoogle Scholar
  23. 23.
    Eley, D. D., and D. G. Hedge, J. Colloid Sci. 12:419–429 (1957).CrossRefGoogle Scholar
  24. 24.
    Colacicco, G., “Concentration of Protein by Gibbs Equation and by Protein Analysis.” Read before the 156th Meeting of the American Chemical Society, Atlantic City, September 1968, Paper No. Coll 030.Google Scholar
  25. 25.
    Camejo, G., Biochim. Biophys. Acta 175:290–300 (1969).PubMedGoogle Scholar
  26. 26.
    Schulman, J. H., Discuss. Faraday Soc. 21:272–273 (1956).CrossRefGoogle Scholar
  27. 27.
    Eley, D. D., and G. Miller, “Proceedings of the Third International Congress on Surface Activity,” Vol. 2, Section B, Verlag Druckerei Universitaet Main GMB, Cologne, 1960, p. 157–160Google Scholar
  28. 28.
    Pethica, B. A., and J. H. Schulman, Biochem. J. 53:177–185 (1952).Google Scholar
  29. 29.
    Shah, D. O., and J. H. Schulman, J. Lipid Res. 6:341–349 (1965).PubMedGoogle Scholar
  30. 30.
    Shah, D. O., and J. H. Schulman, Lipids 2:21–27 (1967).PubMedGoogle Scholar
  31. 31.
    Colacicco, G., “Lipid Monolayers: Surface Potentials of Lecithin and Sphingomyelin With Regard to Ca+ + Binding.” Read before the Third International Biophysics Congress, Cambridge, Massachusetts, August 1969, Paper 11G9.Google Scholar
  32. 32.
    Colacicco, G., “Lipid Monolayers: Influence of Chemical Structure on Surface Properties.” Read before the AOCS 60th Annual Meeting, San Francisco, April 1969, Paper No. 63.Google Scholar
  33. 33.
    Benhamou, N., and J. Guastalla, J. Chim. Phys. Physiocochim. Biol. 57:745–751 (1960).Google Scholar
  34. 34.
    Trurnit, H., J. Colloid Sci. 15:1–3 (1960).CrossRefGoogle Scholar
  35. 35.
    Colacicco, G., and S. Fleischer, “Surface Activity of Mitochondrial Structural Protein.” Read before the 52nd Federation Meeting, Atlantic City, April 1968, Paper 1378.Google Scholar
  36. 36.
    Matalon, R., and J. H. Schulman, Discuss. Faraday Soc. 6:27–39 (1949).Google Scholar
  37. 37.
    Lenard, J., and S. J. Singer, Science 159:738–739 (1968).CrossRefPubMedGoogle Scholar
  38. 38.
    Zahler, W. L., A. Saito and S. Fleischer, Biochem. Biophys. Res. Comm. 32:512–518 (1968).PubMedCrossRefGoogle Scholar
  39. 39.
    Sessa, G., J. H. Freer, G. Colacicco and G. Weissmann, J. Biol. Chem. 244:3575–3582 (1969).PubMedGoogle Scholar
  40. 40.
    Colacicco, G., “Lipid Monolayers: Effect of Lipid Structure on the Interaction With Protein.” Read before the 155th Meeting of the American Chemical Society, San Francisco, April 1968, Paper H90.Google Scholar
  41. 41.
    Miller, I. R., and D. Bach, J. Colloid Interface Sci. 29:250–260 (1969).PubMedCrossRefGoogle Scholar
  42. 42.
    Finean, J. B., Experientia 9:17–19 (1953).PubMedCrossRefGoogle Scholar
  43. 43.
    Shah, D. O., J. H. Schulman, Advan. Chem. Ser. 84:189–209 (1968).CrossRefGoogle Scholar
  44. 44.
    Condrea, E., A. De Vries and J. Mager, Biochim. Biophys. Acta 84:60–73 (1964).PubMedGoogle Scholar
  45. 45.
    Quarles, R. H., and R. M. C. Dawson, Biochem. J. 113:697–705 (1969).PubMedGoogle Scholar
  46. 46.
    Zull, J. E., and C. G. Sciotto, Biochim. Biophys. Acta 173:409–418 (1969).PubMedCrossRefGoogle Scholar
  47. 47.
    Colacicco, G., in “Horizons in Surface Science: Biological Applications,” Edited by L. M. Prince and D. F. Sears, Appleton-Century-Crofts, New York, in press.Google Scholar
  48. 48.
    Chapman, D., Lipids 4:251–260 (1969).PubMedGoogle Scholar
  49. 49.
    Chapman, D., R. B. Leslie, R. Hirz and A. M. Scanu, Nature 221:260–261 (1969).PubMedCrossRefGoogle Scholar
  50. 50.
    Steim, J. M., O. D. Edner and F. G. Bargoot, Science 162:909–911 (1968).PubMedCrossRefGoogle Scholar
  51. 51.
    Bangham, A. D., and D. Papahadjopoulos, Biochim. Biophys. Acta 126:181–184 (1966).PubMedGoogle Scholar
  52. 52.
    Quinn, P. J., and R. M. C. Dawson, Biochem. J. 115:65–75 (1969).PubMedGoogle Scholar

Copyright information

© American Oil Chemists’ Society 1969

Authors and Affiliations

  • Giuseppe Colacicco
    • 1
  1. 1.Department of BiochemistryAlbert Einstein College of MedicineBronx

Personalised recommendations