Membrane-Mediated Lateral Interactions Regulate the Lifetime of Gramicidin Channels
The lipid matrix of cellular membranes is an elastic liquid crystalline medium. Its deformations regulate the functionality and interactions of membrane proteins,f membrane-bound peptides, lipid and protein-lipid domains. Gramicidin A (gA) is a peptide, which incorporates into membrane leaflets as a...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-11-01
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| Series: | Membranes |
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| Online Access: | https://www.mdpi.com/2077-0375/10/12/368 |
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| author | Oleg V. Kondrashov Timur R. Galimzyanov Rodion J. Molotkovsky Oleg V. Batishchev Sergey A. Akimov |
| author_facet | Oleg V. Kondrashov Timur R. Galimzyanov Rodion J. Molotkovsky Oleg V. Batishchev Sergey A. Akimov |
| author_sort | Oleg V. Kondrashov |
| collection | DOAJ |
| description | The lipid matrix of cellular membranes is an elastic liquid crystalline medium. Its deformations regulate the functionality and interactions of membrane proteins,f membrane-bound peptides, lipid and protein-lipid domains. Gramicidin A (gA) is a peptide, which incorporates into membrane leaflets as a monomer and may form a transmembrane dimer. In both configurations, gA deforms the membrane. The transmembrane dimer of gA is a cation-selective ion channel. Its electrical response strongly depends on the elastic properties of the membrane. The gA monomer and dimer deform the membrane differently; therefore, the elastic energy contributes to the activation barriers of the dimerization and dissociation of the conducting state. It is shown experimentally that channel characteristics alter if gA molecules have been located in the vicinity of the conducting dimer. Here, based on the theory of elasticity of lipid membranes, we developed a quantitative theoretical model which allows explaining experimentally observed phenomena under conditions of high surface density of gA or its analogues, i.e., in the regime of strong lateral interactions of gA molecules, mediated by elastic deformations of the membrane. The model would be useful for the analysis and prediction of the gA electrical response in various experimental conditions. This potentially widens the possible applications of gA as a convenient molecular sensor of membrane elasticity. |
| first_indexed | 2024-03-10T14:33:45Z |
| format | Article |
| id | doaj.art-287b3160f37645c697a8f7d3f955ea74 |
| institution | Directory Open Access Journal |
| issn | 2077-0375 |
| language | English |
| last_indexed | 2024-03-10T14:33:45Z |
| publishDate | 2020-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Membranes |
| spelling | doaj.art-287b3160f37645c697a8f7d3f955ea742023-11-20T22:19:35ZengMDPI AGMembranes2077-03752020-11-01101236810.3390/membranes10120368Membrane-Mediated Lateral Interactions Regulate the Lifetime of Gramicidin ChannelsOleg V. Kondrashov0Timur R. Galimzyanov1Rodion J. Molotkovsky2Oleg V. Batishchev3Sergey A. Akimov4Laboratory of Bioelectrochemistry, A.N. Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, 31/4 Leninskiy Prospekt, 119071 Moscow, RussiaLaboratory of Bioelectrochemistry, A.N. Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, 31/4 Leninskiy Prospekt, 119071 Moscow, RussiaLaboratory of Bioelectrochemistry, A.N. Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, 31/4 Leninskiy Prospekt, 119071 Moscow, RussiaLaboratory of Bioelectrochemistry, A.N. Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, 31/4 Leninskiy Prospekt, 119071 Moscow, RussiaLaboratory of Bioelectrochemistry, A.N. Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, 31/4 Leninskiy Prospekt, 119071 Moscow, RussiaThe lipid matrix of cellular membranes is an elastic liquid crystalline medium. Its deformations regulate the functionality and interactions of membrane proteins,f membrane-bound peptides, lipid and protein-lipid domains. Gramicidin A (gA) is a peptide, which incorporates into membrane leaflets as a monomer and may form a transmembrane dimer. In both configurations, gA deforms the membrane. The transmembrane dimer of gA is a cation-selective ion channel. Its electrical response strongly depends on the elastic properties of the membrane. The gA monomer and dimer deform the membrane differently; therefore, the elastic energy contributes to the activation barriers of the dimerization and dissociation of the conducting state. It is shown experimentally that channel characteristics alter if gA molecules have been located in the vicinity of the conducting dimer. Here, based on the theory of elasticity of lipid membranes, we developed a quantitative theoretical model which allows explaining experimentally observed phenomena under conditions of high surface density of gA or its analogues, i.e., in the regime of strong lateral interactions of gA molecules, mediated by elastic deformations of the membrane. The model would be useful for the analysis and prediction of the gA electrical response in various experimental conditions. This potentially widens the possible applications of gA as a convenient molecular sensor of membrane elasticity.https://www.mdpi.com/2077-0375/10/12/368lipid membranegramicidinlateral dimerelastic deformationstheory of elasticitychannel lifetime |
| spellingShingle | Oleg V. Kondrashov Timur R. Galimzyanov Rodion J. Molotkovsky Oleg V. Batishchev Sergey A. Akimov Membrane-Mediated Lateral Interactions Regulate the Lifetime of Gramicidin Channels Membranes lipid membrane gramicidin lateral dimer elastic deformations theory of elasticity channel lifetime |
| title | Membrane-Mediated Lateral Interactions Regulate the Lifetime of Gramicidin Channels |
| title_full | Membrane-Mediated Lateral Interactions Regulate the Lifetime of Gramicidin Channels |
| title_fullStr | Membrane-Mediated Lateral Interactions Regulate the Lifetime of Gramicidin Channels |
| title_full_unstemmed | Membrane-Mediated Lateral Interactions Regulate the Lifetime of Gramicidin Channels |
| title_short | Membrane-Mediated Lateral Interactions Regulate the Lifetime of Gramicidin Channels |
| title_sort | membrane mediated lateral interactions regulate the lifetime of gramicidin channels |
| topic | lipid membrane gramicidin lateral dimer elastic deformations theory of elasticity channel lifetime |
| url | https://www.mdpi.com/2077-0375/10/12/368 |
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