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. 1998 Sep;123(1):37-44.
doi: 10.1006/jsbi.1998.4007.

Reconstitution and imaging of a membrane protein in a nanometer-size phospholipid bilayer

T H Bayburt  1 , J W Carlson, S G Sligar
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Reconstitution and imaging of a membrane protein in a nanometer-size phospholipid bilayer

T H Bayburt et al. J Struct Biol. 1998 Sep.

Abstract

A phospholipid bilayer of nanometer dimension has been used as a support for the study of reconstituted functional single-membrane proteins. This nanobilayer consists of an approximately 10-nm-diameter circular phospholipid domain stabilized by apolipoprotein A1. As a demonstration of this methodology, we formed the nanobilayers in the presence of hepatic microsomal NADPH-cytochrome P450 reductase. Incubation of a solution of enzyme-containing nanobilayers with a freshly cleaved mica substrate resulted in the spontaneous formation of a fully oriented supported monolayer of discoidal phospholipid domains. The P450-reductase in the oriented monolayer retains its catalytic activity. Characterization by scanning force microscopy revealed isolated single-membrane proteins that could be stably imaged over time. These results define a novel technique for the study of single-membrane proteins in a bilayer environment.

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