Mechanosensitive (MS) ion channels are molecular sensors that detect and transduce signals across prokaryotic and eukaryotic cell membranes arising from external mechanical stimuli or osmotic gradients. They play an integral role in mechanosensory responses including touch, hearing, and proprioception by opening or closing in order to facilitate or prevent the flow of ions and organic osmolytes. In this study we use a linear force model of MS channel gating to determine the gating membrane tension (γ) and the gating area change (ΔA) associated with the energetics of MscS channel gating in giant spheroplasts and azolectin liposomes. Analysis of Boltzmann distribution functions describing the dependence of MscS channel gating on membrane tension indicated that the gating area change (ΔA) was the same for MscS channels recorded in both preparations. The comparison of the membrane tension (γ) gating the channel, however, showed a significant difference between the MscS channel activities in these two preparations.
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http://dx.doi.org/10.4161/chan.28366 | DOI Listing |
Biomech Model Mechanobiol
January 2025
CNR Istituto Officina Dei Materiali, Area Science Park Basovizza, S.S. 14, Km 163,5, 34149, Trieste, Italy.
The organization and dynamics of the spectrin-actin membrane cytoskeleton play a crucial role in determining the mechanical properties of red blood cells (RBC). RBC are subjected to various forces that induce deformation during blood microcirculation. Such forces also regulate membrane tension, leading to Piezo1 channel activation, which is functionally linked to RBC dehydration through calcium influx and subsequent activation of Gardos channels, ultimately resulting in variations in RBC volume.
View Article and Find Full Text PDFLangmuir
January 2025
Department of Chemical and Environmental Engineering, University of Cincinnati, Cincinnati, Ohio 45220, United States.
Solvent toxicity limits -butanol fermentation titer, increasing the cost and energy consumption for subsequent separation processes and making biobased production more expensive and energy-intensive than petrochemical approaches. Amphiphilic solvents such as -butanol partition into the cell membrane of fermenting microorganisms, thinning the transverse structure, and eventually causing a loss of membrane potential and cell death. In this work, we demonstrate the deleterious effects of -butanol partitioning upon the lateral dimension of the membrane structure, called membrane domains or lipid rafts.
View Article and Find Full Text PDFACS Appl Mater Interfaces
January 2025
University Clinic of Navarra Centre for Applied Medical Research, 31008 Pamplona, Spain.
Experimental reproducibility in organ-on-chip (OOC) devices is a challenging issue, mainly caused by cell adhesion problems, as OOC devices are made of bioinert materials not suitable for natural cellularization of their surfaces. To improve cell adhesion, several surface functionalization techniques have been proposed, among which the simple use of an intermediate layer of adsorbed proteins has become the preferred one by OOC users. This way, the cells use surface receptors to adhere to the adsorbed proteins, which are in turn attached to the surface.
View Article and Find Full Text PDFBiomolecules
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.
View Article and Find Full Text PDFSoft Matter
January 2025
Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, Moscow, Russia.
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