Distribution and stability of membrane proteins in lipid membranes on solid supports

被引：36

作者：

Puu, G ^{[1
]}

Artursson, E ^{[1
]}

Gustafson, I ^{[1
]}

Lundström, M ^{[1
]}

Jass, J ^{[1
]}

机构：

[1] Def Res Estab, S-90182 Umea, Sweden

来源：

BIOSENSORS & BIOELECTRONICS | 2000年 / 15卷 / 1-2期

关键词：

atomic force microscopy; bacteriorhodopsin; biotin-streptavidin complex; colloidal gold; nicotinic acetylcholine receptor;

D O I：

10.1016/S0956-5663(00)00050-6

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Bacteriorhodopsin and the nicotinic acetylcholine receptor were biotinylated and reconstituted in lipidic membranes on silicon supports by fusion with proteoliposomes. The presence and distribution of the proteins were studied by binding with streptavidin. Radio-labelled streptavidin was employed for quantifying the amounts of protein remaining in the supported membranes after storage in buffer. The proteins within the membranes remained bound to the surface for weeks. The biological activity of reconstituted unlabelled receptor upon storage showed stability in membranes formed on silicon supports and a reduced stability when formed onto lipid monolayer covered supports. Atomic force microscopy studies on preparations in liquid showed bilayer structures but also attached, partly fused liposomes and membrane particles. In air, the surface was smoother and contained less of liposomes and more of stacked lipid layers. Preparations labelled with streptavidin conjugated to colloidal gold and imaged in air showed the proteins individually distributed, with no protein-rich patches or protein aggregates. (C) 2000 Elsevier Science S.A. All rights reserved.

引用

页码：31 / 41

页数：11

共 27 条

[1] Adhesion-induced domain formation by interplay of long-range repulsion and short-range attraction force: A model membrane study [J].