Biochimica et Biophysica Acta (BBA) - Biomembranes
Temperature-dependent properties of gramicidin A channels
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Molecular Mechanism for Gramicidin Dimerization and Dissociation in Bilayers of Different Thickness
2019, Biophysical JournalCitation Excerpt :The bilayer-spanning gramicidin channel forms by transmembrane dimerization of two nonconducting monomers (1,2), and the antiparallel dimer structure is stabilized by six hydrogen bonds at the formyl-N-termini (3–5). Each hydrogen bond contributes ∼4 kBT to the channel stability (6–9), indicating that gramicidin channel dissociation occurs on a timescale far beyond microseconds. The measured gramicidin channel lifetimes are sensitive to the lipid bilayer thickness: dependent on the lipid composition, the channel lifetimes may vary by an order of magnitude in response to subnanometer changes of lipid bilayer thickness (10,11).
pH-Dependent properties of ion channels formed by N-terminally glutamate substituted gramicidin A in planar lipid bilayers
2017, Biochimica et Biophysica Acta - BiomembranesLipid bilayer technologies in ion channel recordings and their potential in drug screening assay
2013, Sensors and Actuators, B: ChemicalCitation Excerpt :Most of the LOC devices developed for lipid bilayer formation use the pore forming antibiotic gramicidin or bacterial toxin α-haemolysin to demonstrate proof-of-concept [46,51,56,57,60,66,75,77–80]. Gramicidin and α-haemolysin are usually preferred because of their well characterized ion channel functions [86–89]. In addition, insertion of these proteins into lipid bilayer membranes is relatively easier as compared to eukaryotic ion channels.
The Gramicidin Dimer Shows Both EX1 and EX2 Mechanisms of H/D Exchange
2009, Journal of the American Society for Mass SpectrometryFluorometric immunoassay based on pH-sensitive dye-encapsulating liposomes and gramicidin channels
2007, Analytical BiochemistryCitation Excerpt :Consequently, the small amount of gramicidin in an open state and/or the use of multilamellar liposomes are responsible for the slow attainment of the steady fluorescence intensity. The gramicidin channel is permeable to monovalent cations, such as H+ and Na+, but is not permeable to divalent cations [38,42]. The effect of monovalent and divalent cations on fluorescence of BCECF (1.0 mM) entrapped in biotin–liposomes at pH 5.5 was investigated.
Sensitized photoinactivation of minigramicidin channels in bilayer lipid membranes
2007, Biochimica et Biophysica Acta - Biomembranes