Skip to main content
NCBI home page
Biophysical Journal logoLink to Biophysical Journal
. 1987 May;51(5):843–845. doi: 10.1016/S0006-3495(87)83412-4

Linear gramicidins at the air-water interface.

N D Mau, P Daumas, D Lelièvre, Y Trudelle, F Heitz
PMCID: PMC1329973  PMID: 2439137

Abstract

The behavior of four linear gramicidins, which differ by the nature of their 9, 11, 13, and 15 aromatic residues, together with a covalent "head to tail" retro GA-DAla-GA dimer, has been examined at the air-water interface. It is shown that all four "monomers" have almost the same molecular area, which is compatible with either a single-stranded or a double-stranded helical model, whereas it is suggested that retro GA-DAla-GA could adopt another conformation. The surface potential measurements agree with those of different groups of molecules characterized by their single-channel behaviors.

Full text

PDF
843

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Heitz F., Gavach C., Spach G., Trudelle Y. Analysis of the ion transfer through the channel of 9,11,13,15-phenylalanylgramicidin A. Biophys Chem. 1986 Jul;24(2):143–148. doi: 10.1016/0301-4622(86)80007-2. [DOI] [PubMed] [Google Scholar]
  2. Heitz F., Spach G., Trudelle Y. Single channels of 9, 11, 13, 15-destryptophyl-phenylalanyl-gramicidin A. Biophys J. 1982 Oct;40(1):87–89. doi: 10.1016/S0006-3495(82)84462-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Hladky S. B., Haydon D. A. Ion transfer across lipid membranes in the presence of gramicidin A. I. Studies of the unit conductance channel. Biochim Biophys Acta. 1972 Aug 9;274(2):294–312. doi: 10.1016/0005-2736(72)90178-2. [DOI] [PubMed] [Google Scholar]
  4. Kemp G., Jacobson K. A., Wenner C. E. Solution and interfacial properties of gramicidin pertinent to its effect on membranes. Biochim Biophys Acta. 1972 Feb 11;255(2):493–501. doi: 10.1016/0005-2736(72)90153-8. [DOI] [PubMed] [Google Scholar]
  5. Kemp G., Wenner C. Solution, interfacial, and membrane properties of gramicidin A. Arch Biochem Biophys. 1976 Oct;176(2):547–555. doi: 10.1016/0003-9861(76)90198-3. [DOI] [PubMed] [Google Scholar]
  6. Mazet J. L., Andersen O. S., Koeppe R. E., 2nd Single-channel studies on linear gramicidins with altered amino acid sequences. A comparison of phenylalanine, tryptophane, and tyrosine substitutions at positions 1 and 11. Biophys J. 1984 Jan;45(1):263–276. doi: 10.1016/S0006-3495(84)84153-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Russell E. W., Weiss L. B., Navetta F. I., Koeppe R. E., 2nd, Andersen O. S. Single-channel studies on linear gramicidins with altered amino acid side chains. Effects of altering the polarity of the side chain at position 1 in gramicidin A. Biophys J. 1986 Mar;49(3):673–686. doi: 10.1016/S0006-3495(86)83694-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. SARGES R., WITKOP B. GRAMICIDIN A. V. THE STRUCTURE OF VALINE- AND ISOLEUCINE-GRAMICIDIN A. J Am Chem Soc. 1965 May 5;87:2011–2020. doi: 10.1021/ja01087a027. [DOI] [PubMed] [Google Scholar]
  9. Urban B. W., Hladky S. B. Ion transport in the simplest single file pore. Biochim Biophys Acta. 1979 Jul 5;554(2):410–429. doi: 10.1016/0005-2736(79)90381-x. [DOI] [PubMed] [Google Scholar]
  10. Urry D. W., Goodall M. C., Glickson J. D., Mayers D. F. The gramicidin A transmembrane channel: characteristics of head-to-head dimerized (L,D) helices. Proc Natl Acad Sci U S A. 1971 Aug;68(8):1907–1911. doi: 10.1073/pnas.68.8.1907. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Urry D. W. The gramicidin A transmembrane channel: a proposed pi(L,D) helix. Proc Natl Acad Sci U S A. 1971 Mar;68(3):672–676. doi: 10.1073/pnas.68.3.672. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Veatch W. R., Fossel E. T., Blout E. R. The conformation of gramicidin A. Biochemistry. 1974 Dec 17;13(26):5249–5256. doi: 10.1021/bi00723a001. [DOI] [PubMed] [Google Scholar]
  13. Wallace B. A. Structure of gramicidin A. Biophys J. 1986 Jan;49(1):295–306. doi: 10.1016/S0006-3495(86)83642-6. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES