Search arXivSearch

arXiv · 1907.05643

A Teflon-based system for applying multidirectional voltages to lipid bilayers as a novel platform for membrane proteins

Abstract

Artificial bilayer lipid membranes (BLMs), along with patch-clamped membranes, are frequently used for functional analyses of membrane proteins. In both methods, the electric properties of membranes are characterized by only one parameter, namely, transmembrane potential. Here the construction of a novel BLM system was reported, in which membrane voltages can be controlled in a lateral direction in addition to conventional transmembrane direction. A microaperture was fabricated in a Teflon film and Ti electrodes were evaporated around the aperture. BLMs were reproducibly formed in the aperture without being affected by the presence of the electrodes. The application of a lateral voltage induced no significant changes in the electric properties of the BLMs, such as baseline current, transmembrane resistance, and transmembrane capacitance. In contrast, lateral voltages clearly affected the activities of biological ion channels, suggesting that the lateral voltage might be a useful parameter for analyzing channel activities. The present Teflon-based system in which multidirectional voltages can be applied to BLMs represent a promising platform for the analysis of underlying functional properties of membrane proteins.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Maki Komiya, Kensaku Kanomata, Ryo Yokota, Yusuke Tsuneta, Madoka Sato, Daichi Yamaura, Daisuke Tadaki, Teng Ma, Hideaki Yamamoto, Yuzuru Tozawa, Albert Marti, Jordi Madrenas, Shigeru Kubota, Fumihiko Hirose, Michio Niwano, Ayumi Hirano-Iwata. 2019-07-12. A Teflon-based system for applying multidirectional voltages to lipid bilayers as a novel platform for membrane proteins. https://arxiv.org/abs/1907.05643

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related papers

Tracking and distinguishing slime mold solutions to traveling salesperson problems through synchronized amplification in the non-equilibrium steady state

The plasmodium of the true slime mold Physarum polycephalum-an ancient, unicellular, aneural organism-serves as a platform for studying the information-processing capacities of active matter. Previous experiments used Physarum's intricate morphological dynamics and photoavoidance in stellate chips to solve $N$-city traveling salesperson problems (TSPs) of up to eight cities, scaling linearly in time with TSP size. Optical feedback controlled by a modified Hopfield network illuminated specific lanes at regular intervals, prompting Physarum to elongate or retract selected branches. When the illumination pattern stabilized in a non-equilibrium steady state, branches bifurcated reproducibly into solution and non-solution groups, with the former exhibiting lower-frequency, higher-amplitude, and more synchronized oscillations than the latter across 41 trials with valid TSP solutions. Physarum's synchronization dynamics efficiently predict 100% of selected solutions by the midpoint of the optical-feedback interval, achieving statistically significant (paired t-test, $p<0.005$) discrimination from alternate tours well before the non-equilibrium steady state. Observed frequency downconversions and synchronized power amplifications scale linearly and quadratically, respectively, for small-to-moderate TSP size, as captured by a toy model of energy redistribution with saturating optical absorption. Tuning these features in native biomolecular chromophore networks may thus improve both the quality and efficiency of TSP solutions from Physarum-based biocomputers, which exploit the effects of organismal-scale coherence.

physics.bio-ph

How do incorrect ligands help detect a correct ligand?

Intrigued by the response of T cell receptors to the presence of a few agonist ligands, we propose a minimal model that can achieve similar performance. The model consists of a small cluster of immobile receptors that bind reversibly to two types (correct/incorrect) of ligands in the environment, with slightly weaker binding strength for the incorrect one. It features binding-state coupling between nearest-neighbor receptors, and receptors in the bound/free states are activated/deactivated by specific enzymes, with rates that allow kinetic proofreading. It is found that, for a range of binding-state coupling strength, incorrect ligands alone cannot activate the receptors, but the binding of merely one correct ligand to a receptor is sufficient to promote the activation of other receptors via induced binding to incorrect ligands. Both response time and signal amplification increase as the receptor binding-state coupling strength increases until it reaches an optimal range to achieve the most rapid and sensitive response. These results suggest a possible mechanism for a speedy and specific response of receptors to very few correct ligands in biological and artificial systems at the subcellular scale.

physics.bio-ph

Signature of mechanically induced cell extrusions in cell size distribution

How a growing tissue organizes its own homeostatic state is a central question in the physics of living matter. We show that when a growing epithelial sheet counteracts increasing cell density by mechanically squeezing cells out of its plane, a homeostatic in-plane pressure emerges as a generalization of a yield stress. We find that in the quasistatic growth limit the homeostatic state is marginally stable, with a pseudogap in the distribution of local distances to the extrusion threshold pressure. Because such mechanically induced extrusions arise from an instability of individual cells, the pseudogap is imprinted in the distribution of cell areas. This provides an image-based way to test for presence of mechanically induced extrusions and we identify this signature in the developing wing epithelium of \textit{D.~melanogaster}. We expect the same principles to apply to confined three-dimensional tissues.

physics.bio-ph