Abstract
The helical polypeptide, gramicidin A has been widely studied as a model for the interactions of hydrophobic proteins with lipid bilayer membranes. Many reports are now available of the physical effects of mixing gramicidin A with phospholipid membranes, however, the interpretation of these data remains unclear. The purpose of this communication is to examine the controversial claim that high concentrations of gramicidin A′ cause disorder within the L α phase of phosphatidylcholine-water dispersions. Solid-state nuclear magnetic resonance (NMR), density gradient and X-ray diffraction techniques are used to confirm the existence of such an effect and mechanisms are discussed which account for the known effects of gramicidin A on lipid bilayers.
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Arseniev AS, Barsukov IL, Bystrov VF, Lomize AL, Ovchinnikov YuA (1985) 1H-NMR study of gramicidin A transmembrane ion channel. FEBS Lett 186:168–174
Chapman D, Cornell BA, Eliasz AW, Perry A (1977) Interactions of helical polypeptide segments which span the hydrocarbon region of lipid bilayers. Studies of the gramicidin A lipidwater system. J Mol Biol 113:517–538
Cornell BA, Keniry MA (1983) A proton-enhanced carbon-13 NMR study of the effect of cholesterol and gramicidin A on the dynamics of phospholipid bilayers. Biochim Biophys Acta 732:705–710
Cortijo M, Chapman D (1981) A comparison of the interactions of cholesterol and gramicidin A with lipid bilayers using an infrared data station. FEBS Lett 131:245–248
Cortijo M, Alonso A, Gomez-Fernandez JC, Chapman D (1982) Intrinsic protein-lipid interactions: infrared spectroscopic studies of gramicidin A, bacteriorhodopsin and Ca2+-ATPase in biomembranes and reconstituted systems. J Mol Biol 157:597–618
Etchebest C, Pullman A, Ranganathan S (1985) The gramicidin A channel: theoretical energy profile computed for single occupancy by a divalent cation, Ca2+. Biochim Biophys Acta 818:23–30
Hawkes GE, Lian LY, Randall EW (1984) Conformational analysis of gramicidin A by 15N NMR at natural abundance. J Magn Reson 56:539–542
Janiak MJ, Small DM, Shipley GG (1979) Temperature and compositional dependence of the structure of hydrated dimyristoyl lecithin. J Biol Chem 254:6068–6078
Killian JA, Timmermans JW, Keur S, de Kruijff B (1985a). The tryptophans of gramicidin are essential for the lipid structure modulating effect of the peptide. Biochim Biophys Acta 820: 154–156
Killian JA, Verkleij AJ, Leunissen, Bijvelt J, de Kruijff B (1985 b) External addition of gramicidin induces the hexagonal HII phase in dioleoylphosphatidylcholine model membranes. Biochim Biophys Acta 812:21–26
Kim KS, Clementi E (1985) Energetics and hydration structures of a solvated gramicidin A transmembrane channel for K+ and Na+ cations. J Am Chem Soc 107:5504–5513
Kim KS, Nguyen HL, Swaminathan PK, Clementi E (1985) Na+ and K+ ion transport through a solvated gramicidin A transmembrane channel: molecular dynamics study using parallel processors. J Phys Chem 89:2870–2876
Koeppe II RE, Hodgson KO, Stryer L (1978) Helical channels in crystals of gramicidin A and of cesium-gramicidin A complex: an X-ray diffraction study. J Mol Biol 121:41–54
Lee DC, Durrani AA, Chapman D (1984) A difference infrared spectroscopic study of gramicidin A, alamethicin and bacteriorhodopsin in perdeuterated dimyristoylphosphatidylcholine. Biochim Biophys Acta 769:49–56
Nagle JF, Wilkinson DA (1978) Lecithin bilayers: density measurements and molecular interactions. Biophys J 23:159–175
Pines A, Gibby MG, Waugh JS (1973) Proton-enhanced NMR of dilute spins in solids. J Chem Phys 59:569–590
Pink DA, Georgallas A, Chapman D (1981) Intrinsic proteins and their effect upon lipid hydrocarbon chain order. Biochemistry 20:7152–7157
Prasad KU, Alonso-Romanowski S, Venkatachalam CM, Trapane TL, Urry DW (1986) Synthesis, characterization, and black lipid membrane studies of (7-l-alanine) gramicidin A. Biochemistry 25:456–463
Rajan S, Kang S-Y, Gutowsky HS, Oldfield E (1981) Phosphorus nuclear magnetic resonance study of membrane structure. J Biol Chem 256:1160–1166
Rice D, Oldfield E (1979) Deuterium nuclear magnetic resonance studies of the interaction between dimyristoylphosphatidylcholine and gramicidin A. Biochemistry 18:3272–3279
Sychev SV, Ivanov VT (1984) Conformations of the transmembrane channel formed by gramicidin A. In: Voelter W, Bayer E, Ovchinnikov YA, Wunsch E (eds) Chemistry of peptides and proteins, vol 2. Walter de Gruyter, Berlin, pp 291–299
Tanaka H, Freed JH (1985) Electron spin resonance studies of lipid-gramicidin-interactions utilizing oriented multibilayers. J Phys Chem 89:350–360
Veatch WR, Fossel, ET, Blout ER (1974) The conformation of gramicidin A. Biochemistry 13:5249–5256
Wallace BA, Veatch WR, Blout ER (1981) Conformation of gramicidin A in phospholipid vesicles: circular dichroism studies of effects of ion binding, chemical modification, and lipid structure. Biochemistry 20:5754–5760
Weinstein S, Durkin JT, Veatch WR, Blout ER (1985) Conformation of the gramicidin A channel in phospholipid vesicles: A fluorine-19 nuclear magnetic resonance study. Biochemistry 24:4374–4382
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Cornell, B.A., Weir, L.E. & Separovic, F. The effect of gramicidin A on phospholipid bilayers. Eur Biophys J 16, 113–119 (1988). https://doi.org/10.1007/BF00255521
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DOI: https://doi.org/10.1007/BF00255521