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Gramicidin A in Asymmetric Lipid Membranes.

Biomolecules

December 2024

Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, 31/4 Leninskiy Prospekt, 119071 Moscow, Russia.

Gramicidin A is a natural antimicrobial peptide produced by . Its transmembrane dimer is a cation-selective ion channel. The channel is characterized by the average lifetime of the conducting state and the monomer-dimer equilibrium constant.

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Article Synopsis
  • The study explores how mitochondrial potassium channels and the peptide Gramicidin affect ion transport and electrical properties in lipid membranes attached to gold electrodes.
  • Techniques like chronoamperometry and impedance spectroscopy were used to analyze how the potassium channel's transport abilities can be altered using the ATP-Mg complex inhibitor, and how Gramicidin's function changes when sodium replaces potassium.
  • The findings show two different current-time responses, which reflect ion movement and changes in the lipid membrane, and were further validated through experiments with self-assembled monolayers on gold surfaces.
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Mitochondrial uncoupling by small-molecule protonophores is generally accepted to proceed via transmembrane proton shuttling. The idea of facilitating this process by the adenine nucleotide translocase ANT originated primarily from the partial reversal of the DNP-induced mitochondrial uncoupling by the ANT inhibitor carboxyatractyloside (CATR). Recently, the sensitivity to CATR was also observed for the action of such potent OxPhos uncouplers as BAM15, SF6847, FCCP and niclosamide.

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Proton transport across lipid membranes is one of the most fundamental reactions that make up living organisms. In vitro, however, the study of proton transport reactions can be very challenging due to limitations imposed by proton concentrations, compartment size, and unstirred layers as well as buffer exchange and buffer capacity. In this study, we have developed a proton permeation assay based on the microfluidic trapping of giant vesicles enclosing the pH-sensitive dye pyranine to address some of these challenges.

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Gramicidin A (gA) is a short hydrophobic β-helical peptide that forms cation-selective channels in lipid membranes in the course of transbilayer dimerization. The length of the gA helix is smaller than the thickness of a typical lipid monolayer. Consequently, elastic deformations of the membrane arise in the configurations of gA monomers, conducting dimer, and the intermediate state of coaxial pair, where gA monomers from opposing membrane monolayers are located one on top of the other.

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