TY - JOUR
T1 - Investigation of transmembrane protein fused in lipid bilayer membranes supported on porous silicon
AU - Tantawi, Khalid Hasan
AU - Cerro, Ramon
AU - Berdiev, Bakhrom
AU - Martin, M. Elena Diaz
AU - Montes, Francisco Javier
AU - Patel, Darayas
AU - Williams, John D.
PY - 2013/1
Y1 - 2013/1
N2 - 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 nm 2. 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.
AB - 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 nm 2. 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.
KW - Lipid bilayer membranes
KW - Porous silicon
KW - Transmembrane protein
UR - http://www.scopus.com/inward/record.url?scp=84871901887&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84871901887&partnerID=8YFLogxK
U2 - 10.3109/03091902.2012.733056
DO - 10.3109/03091902.2012.733056
M3 - Article
C2 - 23276154
AN - SCOPUS:84871901887
VL - 37
SP - 28
EP - 34
JO - Journal of Medical Engineering and Technology
JF - Journal of Medical Engineering and Technology
SN - 0309-1902
IS - 1
ER -