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

## TL;DR

This paper introduces a novel Teflon-based bilayer lipid membrane system capable of applying multidirectional voltages, enabling advanced analysis of membrane protein functions, especially ion channel activities, beyond traditional transmembrane potential measurements.

## Contribution

The study presents a new BLM platform that allows for lateral voltage application without disrupting membrane properties, offering a novel tool for membrane protein research.

## Key findings

- Lateral voltage application does not affect BLM electric properties.
- Lateral voltages influence biological ion channel activities.
- The system enables multidirectional voltage control in BLMs.

## 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.

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Source: https://tomesphere.com/paper/1907.05643