Investigation of transmembrane protein fused in lipid bilayer membranes supported on porous silicon. (January 2013)

• Record Type: Journal Article
• Authors: Tantawi, Khalid Hasan; Cerro, Ramon; Berdiev, Bakhrom; Martin, M. Elena Diaz; Montes, Francisco Javier; Patel, Darayas; Williams, John D.
• Is Part Of: Journal of medical engineering & technology. Volume 37:Number 1(2013)
• Page Start: 28
• Page End: 34
• Publication Date: 2013-01
• Subjects: Biomedical engineering -- Periodicals; Medical technology -- Periodicals; 610.28
• DOI: 10.3109/03091902.2012.733056
• Languages: English
• ISSNs: 0309-1902

Abstract

<abstract> <title> <x xml:space="preserve">Abstract</x> </title> <p>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-<italic>sn</italic>-glycero-3-phosphoserine and 1, 2-diphytanoyl-<italic>sn</italic>-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.</p> </abstract>