Skip to main content
SpringerLink
Log in

Gramicidin A-phospholipid model systems

  • Mini-Review
  • Published:
Journal of Bioenergetics and Biomembranes Aims and scope Submit manuscript

Abstract

Gramicidin A forms ion-conducting channels which can traverse the hydrocarbon core of lipid bilayer membranes. The structures formed by gramicidin A are among the best characterized of all membrane-bound polypeptides or proteins. In this review a brief summary is given of the occurrence, conformation, and synthesis of gramicidin A, and of its use as a model for ion transport and the interaction of proteins and lipids in biological membranes.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Apell, H. J., Bamberg, E., Alpes, H., and Lauger, P. (1977).J. Membr. Biol. 31, 171–188.

    Google Scholar 

  • Arseniev, A. S., Bystrov, V. F., Ivanov, V. T., and Ovchinnikov, Yu. A. (1984).FEBS Lett. 165, 51–56.

    Google Scholar 

  • Arseniev, A. S., Barsukov, I. L., and Bystrov, V. F. (1985a).FEBS Lett. 180, 33–39.

    Google Scholar 

  • Arseniev, A. S., Barsukov, I. L., Bystrov, V. F., Lomize, A. L., and Ovchinnikov, Yu. A. (1985b).FEBS Lett. 186, 168–174.

    Google Scholar 

  • Arseniev, A. S., Barsukov, I. L., and Bystrov, V. F. (1986). InChemistry of Peptides and Proteins (Voelter, W., Bayer, E., Ovchinnikov, Y. A., and Ivanov, V. T., eds.), Vol. 3, Walter de Gruyter, Berlin and New York, pp. 127–158.

    Google Scholar 

  • Aslanian, D., Negrerie, M., and Chambert, R. (1986).Eur. J. Biochem. 160, 395–400.

    Google Scholar 

  • Bamberg, E., and Lauger, P. (1973).J. Membr. Biol. 11, 177–194.

    Google Scholar 

  • Bamberg, E., and Janko, K. (1977).Biochim. Biophys. Acta 465, 486–499

    Google Scholar 

  • Bamberg, E., Apell, H. J., and Alpes, H. (1977).Proc. Natl. Acad. Sci. USA 74, 2402–2406.

    Google Scholar 

  • Barrett Russell, E. W., Weiss, L. B., Navetta, F. I., Koeppe, R. E., II, and Andersen, O. S. (1986).Biophys. J. 49, 673–686.

    Google Scholar 

  • Bauer, K., Roskoski, R., Jr., Kleinkauf, H., and Lipmann, F. (1972).Biochemistry 11, 3266–3271.

    Google Scholar 

  • Brickmann, J., and Fischer, W. (1983).Biophys. Chem. 17, 245–248.

    Google Scholar 

  • Buchet, R., Sandorfy, C., Trapane, T. L., and Urry, D. W. (1985).Biochim. Biophys. Acta 821, 8–16.

    Google Scholar 

  • Busath, D. D., Andersen, O. S., and Koeppe, R. E., II (1987).Biophys. J. 51, 79–88.

    Google Scholar 

  • Chapman, D., Cornell, B. A., Eliasz, A. W., and Perry, A. (1977).J. Mol. Biol. 113, 517–538.

    Google Scholar 

  • Cornell, B. A. (1986).Biophys. J. 49, 192a.

  • Cornell, B. A., and Keniry, M. (1983).Biochim. Biophys. Acta 732, 705–710.

    Google Scholar 

  • Cornell, B. A., Sacre, M. M., Peel, W. E., and Chapman, D. (1977).FEBS Lett. 90, 29–35.

    Google Scholar 

  • Cornell, B. A., Separovic, F., Smith, R., and Baldossi, A. J. (1987a).Biophys. J. 51, 561a.

  • Cornell, B. A., Separovic, F., Smith, R., and Baldossi, A. J., (1987b).Biophys. J., in press.

  • Cornell, B. A., Weir, L. E., and Separovic, F. (1987c).Eur. Biophys. J., in press.

  • Cortijo, M., and Chapman, D. (1981).FEBS Lett. 131, 245–248.

    Google Scholar 

  • Cortijo, M., Alonso, A., Gomez-Fernandez, J. C., and Chapman, D. (1982).J. Mol. Biol. 157, 597–618.

    Google Scholar 

  • Cowan, P. M., and Hodgkin, D. C. (1953).Proc. R. Soc. London Ser. B 141, 89–92.

    Google Scholar 

  • Cross, T. A. (1986).Biophys. J. 49, 124–126.

    Google Scholar 

  • Datema, K. P., Pauls, K. P., and Bloom, M. (1986).Biochemistry 25, 3796–3803.

    Google Scholar 

  • Davion-van Mau, N., Daumas, P., Lelievre, D., Trudelle, Y., and Heitz, F. (1987).Biophys. J. 51, 843–845.

    Google Scholar 

  • Durkin, J. T., Andersen, O. S., Blout, E. R., Heitz, F., Koeppe, R. E., II, and Trudelle, Y. (1986).Biophys. J. 49, 118–121.

    Google Scholar 

  • Durkin, J. T., Andersen, O. S., Heitz, F., and Koeppe, R. E., II (1987).Biophys. J. 51, 451a.

  • Elliott, J. R., Needham, D., Dilger, J. P., and Haydon, D. A. (1983).Biochim. Biophys. Acta 735, 95–103.

    Google Scholar 

  • Feigenson, G. W., Meers, P. R., and Kingsley, P. B. (1977).Biochim. Biophys. Acta 471, 487–491.

    Google Scholar 

  • Finkelstein, A., and Andersen, O. S. (1981).J. Membr. Biol. 59, 155–171.

    Google Scholar 

  • Fischer, W., Brickmann, J., and Lauger, P. (1981).Biophys. Chem. 13, 105–116.

    Google Scholar 

  • Fornili, S. L., Vercauteren, D. P., and Clementi, E. (1984).Biochim. Biophys. Acta 771, 151–164.

    Google Scholar 

  • Fossel, E. T., Veatch, W. R., Ovchinnikov, Y. A., and Blout, E. R. (1974).Biochemistry 13, 5264–5275.

    Google Scholar 

  • Glickson, J. D., Mayers, D. F., Settine, J. M., and Urry, D. W. (1972).Biochemistry 11, 477–486.

    Google Scholar 

  • Haigh, E. A., Thulborn, K. R., and Sawyer, W. H. (1979).Biochemistry 18, 3525–3532.

    Google Scholar 

  • Hawkes, G. E., Lian, L. Y., and Randall, E. W. (1984).J. Magn. Reson. 56, 539–542.

    Google Scholar 

  • Hedman, B., Hodgson, K. O., Helliwell, J. R., Liddington, R., and Papiz, M. Z. (1985).Proc. Natl. Acad. Sci. USA 82, 7604–7607.

    Google Scholar 

  • Heitz, F., and Gavach, C. (1983).Biophys. Chem. 18, 153–163.

    Google Scholar 

  • Heitz, F., Spach, G., Cary, P. D., and Crane-Robinson, C. (1979).Eur. J. Biochem. 93, 135–179.

    Google Scholar 

  • Henze, R., Neher, E., Trapane, T. L., and Urry, D. W. (1982).J. Membr. Biol. 64, 233–239.

    Google Scholar 

  • Hinton, J. F., Young, G., and Millett, F. S. (1982).Biochemistry 21, 651–654.

    Google Scholar 

  • Hinton, J. F., Metz, K. R., Turner, G. L., Bennett, T. L., and Millett, F. S. (1985).J. Magn. Reson. 64, 120–123.

    Google Scholar 

  • Hladky, S. B., and Haydon, D. A. (1972).Biochim. Biophys. Acta 274, 294–312.

    Google Scholar 

  • Huang, H. W. (1986).Biophys. J. 50, 1061–1070.

    Google Scholar 

  • James, T. L., and Noggle, J. H. (1969).Proc. Natl. Acad. Sci. USA 62, 644–649.

    Google Scholar 

  • Jordan, P. C. (1984).J. Membr. Biol. 78, 91–102.

    Google Scholar 

  • Jordan, P. C., and Vayl, I. S. (1985).Biochim. Biophys. Acta 818, 416–420.

    Google Scholar 

  • Katz, E., and Demain, A. L. (1977).Bacteriol. Rev. 41, 449–474.

    Google Scholar 

  • Killian, J. A., and de Kruijff, B. (1985a).Biochemistry 24, 7881–7890.

    Google Scholar 

  • Killian, J. A., and de Kruijff, B. (1985b).Biochemistry 24, 7890–7898.

    Google Scholar 

  • Killian, J. A., and de Kruijff, B. (1986).Chem. Phys. Lipids 40, 259–284.

    Google Scholar 

  • Killian, J. A., de Kruijff, B., van Echteld, C. J. A., Verkleij, A. J., Leunissen-Bijvelt, J., and de Gier, J. (1983).Biochim. Biophys. Acta 728, 141–144.

    Google Scholar 

  • Killian, J. A., Timmermans, J. W., Keur, S., and de Kruijff, B. (1985a).Biochim. Biophys. Acta 820, 154–156.

    Google Scholar 

  • Killian, J. A., Verkleij, A. J., Leunissen-Bijvelt, J., and de Kruijff, B. (1985b).Biochim. Biophys. Acta 812, 21–26.

    Google Scholar 

  • Killian, J. A., Borle, F., de Kruijff, B., and Seelig, J. (1986a).Biochim. Biophys. Acta 854, 133–142.

    Google Scholar 

  • Killian, J. A., van den Berg, C. W., Tournois, H., Keur, S., Slotboom, A. J., van Scharrenburg, G. J. M., and de Kruijff, B. (1986b).Biochim. Biophys. Acta 857, 13–27.

    Google Scholar 

  • Killian, J. A., Burger, K. N. J., and de Kruijff, B. (1987).Biochim. Biophys. Acta 897, 269–284.

    Google Scholar 

  • Kim, K. S., and Clementi, E. (1985).J. Am. Chem. Soc. 107, 5504–5513.

    Google Scholar 

  • Kim, K. S., Nguyen, H. L., Swaminathan, P. K., and Clementi, E. (1985).J. Phys. Chem. 89, 2870–2876.

    Google Scholar 

  • Koeppe, R. E., II, and Schoenborn, B. P. (1984).Biophys. J. 45, 503–507.

    Google Scholar 

  • Koeppe, R. E., II, Hodgson, K. O., and Stryer, L. (1978).J. Mol. Biol. 121, 41–54.

    Google Scholar 

  • Koeppe, R. E., II, Berg, J. M., Hodgson, K. O., and Stryer, L. (1979).Nature (London)279, 723–725.

    Google Scholar 

  • Koeppe, R. E., II, Hinton, J. F., Fernandez, J., Shungu, D., Whaley, W. L., and Millett, F. S. (1987).Biophys. J. 51, 303a.

  • Lauger, P. (1982).Biophys. Chem. 15, 89–100.

    Google Scholar 

  • Lee, D. C., Durrani, A. A., and Chapman, D. (1984).Biochim. Biophys. Acta 769, 49–56.

    Google Scholar 

  • Levitt, D. G. (1978).Biophys. J. 22, 209–219.

    Google Scholar 

  • Lorenzi, G. P., Gerber, C., and Jackle, H. (1984).Biopolymers 23, 1905–1916.

    Google Scholar 

  • Mackay, D. J., Berens, P. H., Wilson, K. R., and Hagler, A. T. (1984).Biophys. J. 46, 229–248.

    Google Scholar 

  • Mazet, J.-L., Andersen, O. S., and Koeppe, R. E., II (1984).Biophys. J. 45, 263–276.

    Google Scholar 

  • Merck Index (1983). (Windholz, M., ed.), 10th edn., Merck & Co., Inc., Rathway, New Jersey, p. 651.

    Google Scholar 

  • Merrifield, R. B. (1963).J. Am. Chem. Soc. 85, 2149–2154.

    Google Scholar 

  • Moll, F., Nicholson, L. K., LoGrasso, P. V., Lay, J. L., Guy, C. A., Petefish, J., Fields, G. B., van Wart, H. E., and Cross, T. A. (1987).Biophys. J. 51, 73a.

    Google Scholar 

  • Monoi, H. (1983).J. Theor. Biol. 102, 69–99.

    Google Scholar 

  • Morrow, J. S., Veatch, W. R., and Stryer, L. (1979).J. Mol. Biol. 132, 733–738.

    Google Scholar 

  • Myers, V. B., and Haydon, D. A. (1972).Biochim. Biophys. Acta 27, 313–322.

    Google Scholar 

  • Naik, V. M., and Krimm, S. (1984).Biochem. Biophys. Res. Commun. 125, 919–925.

    Google Scholar 

  • Naik, V. M., and Krimm, S. (1986a).Biophys. J. 49, 1131–1145.

    Google Scholar 

  • Naik, V. M., and Krimm, S. (1986b).Biophys. J. 49, 1147–1154.

    Google Scholar 

  • Noda, K., and Gross, E. (1972). InChemistry and Biology of Peptides (Meienhofer, J., ed.), Ann Arbor Science Publishers, Ann Arbor, Michigan, pp. 241–250.

    Google Scholar 

  • Parsegian, V. A. (1975).Ann. N.Y. Acad. Sci. 264, 161–174.

    Google Scholar 

  • Pauls, K. P., MacKay, A. L., Soderman, O., Bloom, M., Tanjea, A. K., and Hodges, R. S. (1985).Eur. Biophys. J. 12, 1–11.

    Google Scholar 

  • Phonphok, N., Doane, J. W., and Westerman, P. W. (1984).Biophys. J. 47, 113a.

    Google Scholar 

  • Pink, D. A., Georgallas, A., and Chapman, D. (1981).Biochemistry 20, 7152–7157.

    Google Scholar 

  • Pope, C. G., Urban, B. W., and Haydon, D. A. (1982).Biochim. Biophys. Acta 668, 279–283.

    Google Scholar 

  • Prasad, K. U., Trapane, T. L., Busath, D., Szabo, G., and Urry, D. W. (1982).J. Protein Chem. 1, 191–202.

    Google Scholar 

  • Prasad, K. U., Alonso-Romanowski, S., Venkatachalam, C. M., Trapane, T. L., and Urry, D. W. (1986).Biochemistry 25, 456–463.

    Google Scholar 

  • Pullman, A., and Etchebest, C. (1983).FEBS Lett. 163, 199–202.

    Google Scholar 

  • Rajan, S., Kang, S.-Y., Gutowsky, H. S., and Oldfield, E. (1981).J. Biol. Chem. 256, 1160–1166.

    Google Scholar 

  • Ramachandran, L. K. (1963).Biochemistry 2, 1138–1142.

    Google Scholar 

  • Reference Data for Radio Engineers. (1982). (Howard W. Sams Engineering Staff, eds.), 6th edn., Howard W. Sams & Co., Inc., Indianapolis, Indiana pp. 4–21 and 4–28.

    Google Scholar 

  • Rice, D., and Oldfield, E. (1979).Biochemistry 18, 3272–3279.

    Google Scholar 

  • Ring, A. (1986).Biochim. Biophys. Acta 865, 646–653.

    Google Scholar 

  • Sarges, R., and Witkop, B. (1964).J. Am. Chem. Soc. 86, 1861–1862.

    Google Scholar 

  • Sarges, R., and Witkop, B. (1965a).J. Am. Chem. Soc. 87, 2020–2027.

    Google Scholar 

  • Sarges, R., and Witkop, B. (1965b).J. Am. Chem. Soc. 87, 2027–2030.

    Google Scholar 

  • Sarges, R., and Witkop, B. (1965c).Biochemistry 4, 2491–2494.

    Google Scholar 

  • Sarges, R., and Witkop, B. (1965d).Biochemistry 4, 2495–2501.

    Google Scholar 

  • Short, K. W., Wallace, B. A., Myers, R. A., Fodor, S. P. A., and Dunker, A. K. (1987).Biochemistry 26, 557–562.

    Google Scholar 

  • Smith, R., and Cornell, B. A. (1986).Biophys. J. 49, 117–118.

    Google Scholar 

  • Spisni, A., Pasquali-Ronchetti, K., Casali, E., Lindner, L., Cavatorta, P., Masotti, L., and Urry, D. W. (1983).Biochim. Biophys. Acta 732, 58–68.

    Google Scholar 

  • Sychev, S. V., and Ivanov, V. T. (1982). InMembranes and Transport (Martonosi, A. N., ed.), Vol. 2, Plenum Press, New York, pp. 301–307.

    Google Scholar 

  • Sychev, S. V., Nevskaya, N. A., Jordanov, S., Shepel, E. N., Miroshnikov, A. I., and Ivanov, V. T. (1980).Bioorg. Chem. 9, 121–151.

    Google Scholar 

  • Tanaka, H., and Freed, J. H. (1985).J. Phys. Chem. 89, 350–360.

    Google Scholar 

  • Tanford, C. (1973).The Hydrophobic Effect: Formation of Micelles and Biological Membranes. Wiley, New York, pp. 45–59.

    Google Scholar 

  • Tank, D. W., Wu, E. S., Meers, P. R., and Webb, W. W. (1982).Biophys. J. 40, 129–135.

    Google Scholar 

  • Turner, G. L., Hinton, J. F., and Millett, F. S. (1982).Biochemistry 21, 646–651.

    Google Scholar 

  • Urban, B. W., Hladky, S. B., and Haydon, D. A. (1978).Fed. Proc. 37, 2628–2632.

    Google Scholar 

  • Urbaneja, M.-A., Alonso, A., and Goni, F. M. (1985).J. Biochem. Biophys. Methods 11, 341–345.

    Google Scholar 

  • Urry, D. W. (1971).Proc. Natl. Acad. Sci. USA 68, 672–676.

    Google Scholar 

  • Urry, D. W. (1972).Biochim. Biophys. Acta 265, 115–168.

    Google Scholar 

  • Urry, D. W. (1984). InSpectroscopy of Biological Molecules. (Sandorfy, C., and Theophanides, T., eds.), D. Reidel, Dordrecht, Holland, pp. 511–538.

    Google Scholar 

  • Urry, D. W., Long, M. M., Jacobs, M., and Harris, R. D. (1975).Ann. N.Y. Acad. Sci. 264, 203–220.

    Google Scholar 

  • Urry, D. W., Venkatachalam, C. M., Spisni, A., Bradley, R. J., Trapane, T. L., and Prasad, K. U. (1980a).J. Membr. Biol. 55, 29–51.

    Google Scholar 

  • Urry, D. W., Venkatachalam, C. M., Spisni, A., Lauger, P., and Khaled, M. A. (1980b).Proc. Natl. Acad. Sci. USA 77, 2028–2032.

    Google Scholar 

  • Urry, D. W., Walker, J. T., and Trapane, T. L. (1982).J. Membr. Biol. 69, 225–231.

    Google Scholar 

  • Urry, D. W., Shaw, R. G., Trapane, T. L., and Prasad, K. U. (1983a).Biochem. Biophys. Res. Commun. 114, 373–379.

    Google Scholar 

  • Urry, D. W., Trapane, T. L., and Prasad, K. U. (1983b).Science 221, 1064–1067.

    Google Scholar 

  • Urry, D. W., Trapane, T. L., Romanowski, S., Bradley, R. J., and Prasad, K. U. (1983c).Int. J. Peptide Protein Res. 21, 16–23.

    Google Scholar 

  • Urry, D. W., Trapane, T. L., Venkatachalam, C. M., and Prasad, K. U. (1983d).J. Phys. Chem. 87, 2918–2923.

    Google Scholar 

  • Urry, D. W., Alonso-Romanowski, S., Venkatachalam, C. M., Trapane, T. L., Harris, R. D., and Prasad, K. U. (1984a).Biochim. Biophys. Acta 775, 115–119.

    Google Scholar 

  • Urry, D. W., Alonso-Romanowski, S., Venkatachalam, C. M., Trapane, T. L., and Prasad, K. U. (1984b).Biophys. J. 46, 259–266.

    Google Scholar 

  • Urry, D. W., Trapane, T. L., Brown, R. A., Venkatachalam, C. M., and Prasad, K. U. (1985a).J. Magn. Reson. 65, 43–61.

    Google Scholar 

  • Urry, D. W., Trapane, T. L., Venkatachalam, C. M., and Prasad, K. U. (1985b).Can. J. Chem. 63, 1976–1981.

    Google Scholar 

  • Urry, D. W., Trapane, T. L., and Venkatachalam, C. M. (1986).J. Membr. Biol. 89, 107–111.

    Google Scholar 

  • van Echteld, C. J. A., van Stigt, R., de Kruijff, B., Leunissen-Bijvelt, J., Verkleij, A. J., and de Gier, J. (1981).Biochim. Biophys. Acta 648, 287–291.

    Google Scholar 

  • van Echteld, C. J. A., de Kruijff, B., Verkleij, A. J., Leunissen-Bijvelt, J., and de Gier, J. (1982).Biochim. Biophys. Acta 692, 126–138.

    Google Scholar 

  • Veatch, W. R., and Blout, E. R. (1974).Biochemistry 13, 5257–5264.

    Google Scholar 

  • Veatch, W. R., and Stryer, L. (1977).J. Mol. Biol. 113, 89–102.

    Google Scholar 

  • Veatch, W. R., Fossel, E. T., and Blout, E. R. (1974).Biochemistry 13, 5249–5257.

    Google Scholar 

  • Veatch, W. R., Mathies, R., Eisenberg, M., and Stryer, C. (1975).J. Mol. Biol. 99, 76–92.

    Google Scholar 

  • Wallace, B. A. (1983).Biopolymers 22, 397–402.

    Google Scholar 

  • Wallace, B. A. (1984).Biophys. J. 45, 114–116.

    Google Scholar 

  • Wallace, B. A. (1986).Biophys. J. 49, 295–306.

    Google Scholar 

  • Wallace, B. A., and Hendrickson, W. A. (1984).Acta Crystallogr. Sect. A 40, c49.

    Google Scholar 

  • Wallace, B. A., Veatch, W. R., and Blout, E. R. (1981).Biochemistry 20, 5754–5760.

    Google Scholar 

  • Weinstein, S., Wallace, B. A., Blout, E. R., Morrow, J. S., and Veatch, W. (1979).Proc. Natl. Acad. Sci. USA 76, 4230–4234.

    Google Scholar 

  • Weinstein, S., Wallace, B. A., Morrow, J. S., and Veatch, W. R. (1980).J. Mol. Biol. 143, 1–19.

    Google Scholar 

  • Weinstein, S., Durkin, J. T., Veatch, W. R., and Blout, E. R. (1985).Biochemistry 24, 4374–4382.

    Google Scholar 

  • Yonezawa, H., Yutani, K., Aoyagi, H., and Izumiya, N. (1976).Mem. Fac. Sci. Kyushu Univ. Ser. C 10, 43–49.

    Google Scholar 

  • Zwolinski, B. I., Eyring, H., and Polissar, M. I. (1949).J. Phys. Chem. 53, 1426–1453.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Commonwealth Scientific and Industrial Research Organization, P.O. Box 52, 2113, North Ryde, N.S.W., Australia

    Bruce Cornell

Authors
  1. Bruce Cornell
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Cornell, B. Gramicidin A-phospholipid model systems. J Bioenerg Biomembr 19, 655–676 (1987). https://doi.org/10.1007/BF00762301

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00762301

Key words

Search

Navigation