Literature DB >> 12524278

Proton transfer in gramicidin channels is modulated by the thickness of monoglyceride bilayers.

Anatoly Chernyshev1, Kathryn M Armstrong, Samuel Cukierman.   

Abstract

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.

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Year:  2003        PMID: 12524278      PMCID: PMC1302606          DOI: 10.1016/S0006-3495(03)74845-0

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  62 in total

1.  On the role of the K-proton transfer pathway in cytochrome c oxidase.

Authors:  M Brändén; H Sigurdson; A Namslauer; R B Gennis; P Adelroth; P Brzezinski
Journal:  Proc Natl Acad Sci U S A       Date:  2001-04-10       Impact factor: 11.205

2.  Membrane dipole potential modulates proton conductance through gramicidin channel: movement of negative ionic defects inside the channel.

Authors:  Tatyana I Rokitskaya; Elena A Kotova; Yuri N Antonenko
Journal:  Biophys J       Date:  2002-02       Impact factor: 4.033

3.  Calculation of deformation energies and conformations in lipid membranes containing gramicidin channels.

Authors:  P Helfrich; E Jakobsson
Journal:  Biophys J       Date:  1990-05       Impact factor: 4.033

4.  Brief closures of gramicidin A channels in lipid bilayer membranes.

Authors:  A Ring
Journal:  Biochim Biophys Acta       Date:  1986-04-25

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Authors:  Anatoly Chernyshev; Samuel Cukierman
Journal:  Biophys J       Date:  2002-01       Impact factor: 4.033

6.  Transmembrane channels based on tartaric acid-gramicidin A hybrids.

Authors:  C J Stankovic; S H Heinemann; J M Delfino; F J Sigworth; S L Schreiber
Journal:  Science       Date:  1989-05-19       Impact factor: 47.728

7.  Proton conductance by the gramicidin water wire. Model for proton conductance in the F1F0 ATPases?

Authors:  M Akeson; D W Deamer
Journal:  Biophys J       Date:  1991-07       Impact factor: 4.033

8.  Modulation of proton transfer in the water wire of dioxolane-linked gramicidin channels by lipid membranes.

Authors:  C M de Godoy; S Cukierman
Journal:  Biophys J       Date:  2001-09       Impact factor: 4.033

9.  On the origin of closing flickers in gramicidin channels: a new hypothesis.

Authors:  Kathryn M Armstrong; Samuel Cukierman
Journal:  Biophys J       Date:  2002-03       Impact factor: 4.033

10.  Permeation characteristics of gramicidin conformers.

Authors:  D Busath; G Szabo
Journal:  Biophys J       Date:  1988-05       Impact factor: 4.033

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  4 in total

1.  The pH-dependent induction of lipid membrane ionic permeability by N-terminally lysine-substituted analogs of gramicidin A.

Authors:  Tatyana I Rokitskaya; Alexandra I Sorochkina; Sergey I Kovalchuk; Natalya S Egorova; Elena A Kotova; Sergey V Sychev; Yuri N Antonenko
Journal:  Eur Biophys J       Date:  2011-11-01       Impact factor: 1.733

2.  Ultrafast proton transport in sub-1-nm diameter carbon nanotube porins.

Authors:  Ramya H Tunuguntla; Frances I Allen; Kyunghoon Kim; Allison Belliveau; Aleksandr Noy
Journal:  Nat Nanotechnol       Date:  2016-04-04       Impact factor: 39.213

3.  Proton transfer in gramicidin water wires in phospholipid bilayers: attenuation by phosphoethanolamine.

Authors:  Anatoly Chernyshev; Samuel Cukierman
Journal:  Biophys J       Date:  2006-04-14       Impact factor: 4.033

4.  N-terminally glutamate-substituted analogue of gramicidin A as protonophore and selective mitochondrial uncoupler.

Authors:  Alexandra I Sorochkina; Egor Y Plotnikov; Tatyana I Rokitskaya; Sergei I Kovalchuk; Elena A Kotova; Sergei V Sychev; Dmitry B Zorov; Yuri N Antonenko
Journal:  PLoS One       Date:  2012-07-24       Impact factor: 3.240

  4 in total

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