Proton transfer in gramicidin channels is modulated by the thickness of monoglyceride bilayers.
The thickness of monoglyceride planar bilayers has significant effects on the transfer of protons in both native gramicidin A (gA) and in covalently linked SS- and RR-dioxolane-linked gA proteins. Planar bilayers with various thicknesses were formed from an appropriate combination of monoglyceride with various fatty acid lengths and solvent. Bilayer thicknesses ranged from 25 A (monoolein in squalene) to 54 A (monoeicosenoin in decane). Single-channel conductances to protons (g(H)) were measured in the concentration range of 10-5000 mM HCl. In native gA as well as in RR channels, the shape of the log(g(H))-log([H(+)]) relationships was nonlinear and remained basically unaltered in monoglyceride bilayers with various thicknesses. For both native gA and RR channels, g(H) values were systematically and significantly larger in thin than in thick bilayers. By contrast, the shape of the log(g(H))-log([H(+)]) relationships in the SS channel was linear (with a slope considerably smaller than 1) in thick (>37 A) bilayers. However, in thin (<37 A) bilayers these plots became nonlinear and g(H) values approached those obtained in native gA channels. The linearization of the log-log plots in the SS channel in thick bilayers is a consequence of a dramatic increase (instead of a decrease as in native gA and RR channels) of g(H) in these bilayers in [H(+)] <1 M. The gating characteristics of the various gA channels as a function of bilayer thickness followed the same pattern as described previously. It was noticed, however, that in the thickest monoglyceride bilayer used in this study, both the SS- and RR-dioxolane-linked channels opened in a mode of bursting activity instead of remaining in the open state as in thin bilayers. It is proposed that the thickness of monoglyceride bilayers modulates proton transfer in native gA channels by a combination of factors including the access resistances of channels to H(+), and fluctuations in both the structure of the lipid bilayer and in the distance between gA monomers. The differential effects of relatively thick monoglyceride bilayers on proton transfer in both dioxolane-linked gA channels must relate to distinct interactions between the bilayers and the SS and RR dioxolanes.
Chernyshev
Anatoly
A
Dept. of Physiology, Loyola University Medical Center, Maywood, Illinois 60153, USA.
Armstrong
Kathryn M
KM
Cukierman
Samuel
S
D025802:Electric Capacitance; D004553:Electric Conductivity; D004735:Energy Transfer; D005989:Glycerides / Q000737:chemistry*; D006096:Gramicidin / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D015640:Ion Channel Gating; D007473:Ion Channels / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D008560:Membrane Fluidity; D008564:Membrane Potentials; D008567:Membranes, Artificial; D008968:Molecular Conformation; D011487:Protein Conformation; D011522:Protons; D012997:Solvents / Q000737:chemistry; D013499:Surface Properties; D014867:Water / Q000737:chemistry
D005989:Glycerides; D007473:Ion Channels; D008051:Lipid Bilayers; D008567:Membranes, Artificial; D011522:Protons; D012997:Solvents; D014867:Water; D006096:Gramicidin