Literature DB >> 65181

The action of a carbonsuboxide dimerized gramicidin A on lipid bilayer membranes.

E Bamberg, K Janko.   

Abstract

Gramicidin A was dimerized with carbonsuboxide as bifunctional reagent. The effect of the resulting malonyl-bis-desformylgramicidin on lipid bilayer membranes was investigated and compared with the effect of the monomer gramicidin. It was found that the single channel conductance and the ion selectivity are very similar to the behaviour of the monomer molecule, whereas the channel forming kinetics and the life time of the single channel of the malonyl-bis-desformylgramicidin differ strongly from the behaviour of the monomer gramicidin. The electrical relaxations are very small and possibly associated with some structural changes of the membrane after a voltage jump. The single channel lifetime of the malonyl-bis-desformylgramicidin is measured in minutes, whereas for the same lipid system the single channel lifetime in the case of the monomer gramicidin is restricted to 1-2 s. It is concluded that the malonyl-bis-desformylgramicidin-molecule itself (as a single molecule) forms an ionic channel without further association.

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Year:  1977        PMID: 65181     DOI: 10.1016/0005-2736(77)90267-x

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  28 in total

1.  Covalently linked gramicidin channels: effects of linker hydrophobicity and alkaline metals on different stereoisomers.

Authors:  K M Armstrong; E P Quigley; P Quigley; D S Crumrine; S Cukierman
Journal:  Biophys J       Date:  2001-04       Impact factor: 4.033

2.  The conduction of protons in different stereoisomers of dioxolane-linked gramicidin A channels.

Authors:  E P Quigley; P Quigley; D S Crumrine; S Cukierman
Journal:  Biophys J       Date:  1999-11       Impact factor: 4.033

3.  Dimer versus tetramer.

Authors:  O S Andersen; R E Koeppe
Journal:  Biophys J       Date:  1992-02       Impact factor: 4.033

4.  On the supramolecular organization of gramicidin channels. The elementary conducting unit is a dimer.

Authors:  A S Cifu; R E Koeppe; O S Andersen
Journal:  Biophys J       Date:  1992-01       Impact factor: 4.033

5.  Arguments in favor of an aggregational model of the gramicidin channel: a reply.

Authors:  G Stark
Journal:  Biophys J       Date:  1992-02       Impact factor: 4.033

6.  Gramicidin channels are internally gated.

Authors:  Tyson L Jones; Riqiang Fu; Frederick Nielson; Timothy A Cross; David D Busath
Journal:  Biophys J       Date:  2010-04-21       Impact factor: 4.033

Review 7.  Temperature-jump and voltage-jump experiments at planar lipid membranes support an aggregational (micellar) model of the gramicidin A ion channel.

Authors:  G Stark; M Strässle; Z Takácz
Journal:  J Membr Biol       Date:  1986       Impact factor: 1.843

8.  Thermodynamic view of activation energies of proton transfer in various gramicidin A channels.

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

9.  Dicarboxylic acid analogs of gramicidin A: dimerization kinetics and single channel properties.

Authors:  H J Apell; E Bamberg; H Alpes
Journal:  J Membr Biol       Date:  1979-11-30       Impact factor: 1.843

10.  Attenuation of proton currents by methanol in a dioxolane-linked gramicidin A channel in different lipid bilayers.

Authors:  E P Quigley; A J Emerick; D S Crumrine; S Cukierman
Journal:  Biophys J       Date:  1998-12       Impact factor: 4.033

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