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PMID: 2432948 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Deformation free energy of bilayer membrane and its effect on gramicidin channel lifetime.

Biophysical journal ·Vol. 50 ·No. 6 ·1986-12-00 ·Pages 1061-70

Huang HW

Abstract

The deformation free energy of a lipid bilayer is presented based on the principle of a continuum theory. For small deformations, the free energy consists of a layer-compression term, a splay-distortion term, and a surface-tension term, equivalent to the elastic free energy of a two-layer smectic liquid crystal with surface tension. Minimization of the free energy leads to a differential equation that, with boundary conditions, determines the elastic deformation of a bilayer membrane. When a dimeric gramicidin channel is formed in a membrane of thickness greater than the length of the channel, the membrane deformation reduces the stability of the channel. Previously this effect was studied by comparing the variation of channel lifetime with the surface tension of bilayers (Elliott, J. R., D. Needham, J. P. Dilger, and D. A. Hayden, 1983, Biochim. Biophys. Acta, 735:95-103). The tension was assumed to pull a dimer for a distance z before the channel loses ion conductivity. To account for the data, z was found to be 18 A. With the deformation free energy, the data can be accounted for with z less than or approximately to 1 A, which is consistent with the breaking of hydrogen bonds in a dimer dissociation. Increasing the strength of lipid-protein interactions is not the only consequence of the complete free energy compared with the previous discussions. It also changes the shape of membrane deformation around an embedded channel from convex to concave, and increases the range of deformation from less than 10 A to greater than 20 A. Clearly these will be important factors in the general considerations of lipid-protein interactions and membrane-mediated interactions between proteins. In addition, thermal fluctuations of a membrane are calculated; in particular, we calculate the relations between the intrinsic thickness and the experimentally measured values. The experimental parameters of monoolein-squalene membranes are used for quantitative analyses.

MeSH Terms
Gramicidin Ion Channels/physiology Lipid Bilayers Mathematics Models, Biological Molecular Conformation Thermodynamics
Chemicals
Ion Channels Lipid Bilayers Gramicidin
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Huang H W
References (24)
24 references, click to expand
  1. Optical properties of black lecithin films.
    J Mol Biol. 1969 Feb 28;40(1):19-32 PMID: 5363346
  2. Mattress model of lipid-protein interactions in membranes.
    Biophys J. 1984 Aug;46(2):141-53 PMID: 6478029
  3. Ion transport across thin lipid membranes: a critical discussion of mechanisms in selected systems.
    Q Rev Biophys. 1972 May;5(2):187-282 PMID: 4559448
  4. Channel formation kinetics of gramicidin A in lipid bilayer membranes.
    J Membr Biol. 1973;11(2):177-94 PMID: 4131309
  5. Elastic properties of lipid bilayers: theory and possible experiments.
    Z Naturforsch C. 1973 Nov-Dec;28(11):693-703 PMID: 4273690
  6. The equivalence of fluctuation analysis and chemical relaxation measurements: a kinetic study of ion pore formation in thin lipid membranes.
    Biophys Chem. 1974 Oct;2(3):197-207 PMID: 4139982
  7. Influence of membrane thickness and ion concentration on the properties of the gramicidin a channel. Autocorrelation, spectral power density, relaxation and single-channel studies.
    Biochim Biophys Acta. 1977 Jan 4;464(1):127-41 PMID: 64260
  8. The influence of phospholipid polar groups on gramicidin channels.
    Biochim Biophys Acta. 1977 Jan 4;464(1):37-44 PMID: 64261
  9. Neutron diffraction studies on selectively deuterated phospholipid bilayers.
    Nature. 1978 Jan 12;271(5641):182-4 PMID: 579650
  10. Theoretical study of protein--lipid interactions in bilayer membranes.
    Proc Natl Acad Sci U S A. 1978 Apr;75(4):1616-9 PMID: 273895
  11. Formation of "solvent-free" black lipid bilayer membranes from glyceryl monooleate dispersed in squalene.
    Biophys J. 1978 Sep;23(3):337-47 PMID: 698340
  12. The blockage of the electrical conductance in a pore-containing membrane by the n-alkanes.
    Biochim Biophys Acta. 1978 Oct 19;513(1):106-16 PMID: 82449
  13. Theory of protein-lipid and protein-protein interactions in bilayer membranes.
    Proc Natl Acad Sci U S A. 1979 Oct;76(10):4750-4 PMID: 291895
  14. The dependence of the conductance and lifetime of gramicidin channels on the thickness and tension of lipid bilayers.
    Biochim Biophys Acta. 1981 Mar 20;642(1):196-202 PMID: 6164394
  15. A mean-field model of the alkane-saturated lipid bilayer above its phase transition. I. Development of the model.
    Biophys J. 1981 Feb;33(2):149-66 PMID: 6894396
  16. A mean-field model of the alkane-saturated lipid bilayer above its phase transition. II. Results and comparison with experiment.
    Biophys J. 1981 Feb;33(2):167-87 PMID: 7225504
  17. The thickness of monoolein lipid bilayers as determined from reflectance measurements.
    Biochim Biophys Acta. 1981 Jul 20;645(2):357-63 PMID: 7272294
  18. Measurement of the lateral compressibility of several phospholipid bilayers.
    Biophys J. 1982 Mar;37(3):667-72 PMID: 7074192
  19. Thickness fluctuations in black lipid membranes.
    Biophys J. 1982 Jun;38(3):251-8 PMID: 7104437
  20. Tensions and free energies of formation of "solventless" lipid bilayers. Measurement of high contact angles.
    Biophys J. 1983 Mar;41(3):251-7 PMID: 6838967
  21. The effects of bilayer thickness and tension on gramicidin single-channel lifetime.
    Biochim Biophys Acta. 1983 Oct 26;735(1):95-103 PMID: 6194820
  22. Gramicidin channels.
    Annu Rev Physiol. 1984;46:531-48 PMID: 6201133
  23. Energetics of fluctuation in lipid bilayer thickness.
    Biophys J. 1984 Mar;45(3):643-6 PMID: 6713074
  24. 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 PMID: 5048999
Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1986-12-00
Pages
1061-70
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1329780
Subset
IM
Grants
NHLBI NIH HHS · HL-32593 · United States
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