Investigation of transmembrane protein fused in lipid bilayer membranes supported on porous silicon

Abstract

This article investigates a device made from a porous silicon structure supporting a lipid bilayer membrane (LBM)fused with Epithelial Sodium Channel protein. The electrochemically-fabricated porous silicon template had pore diameters in the range 0.2~2 µm. Membranes were composed of two synthetic phospholipids: 1,2-diphytanoyl-sn-glycero-3-phosphoserine and 1,2-diphytanoyl-sn-glycero-3-phosphoethanolamine. The LBMwas formed by means of the Langmuir-Blodgett and Langmuir-Schaefer techniques, at a monolayer surface tension of 26 m Nm⁻¹ in room temperature and on a deionized water subphase, which resulted in an average molecular area of 0.68–0.73 nm². Fusion of transmembrane protein was investigated using Atomic Force Microscopy. Initial atomic force microscopy results demonstrate the ability to support lipid bilayers fused with transmembrane proteins across a porous silicon substrate. However, more control of the membrane’s surface tension using traditional membrane fusion techniques is required to optimize protein incorporation.

Keywords::

• Porous silicon
• Lipid bilayer membranes
• Transmembrane protein

Declaration of interest: This work was funded by the Alabama EPSCoR Graduate Research Scholars Program and supported by the Office of the Vice President for Research.