Channel-forming membrane proteins as molecular sensors

被引:10
作者
Danelon, C
Lindemann, M
Borin, C
Fournier, D
Winterhalter, M [1 ]
机构
[1] CNRS, UMR 5089, IPBS, F-31077 Toulouse, France
[2] Swiss Fed Inst Technol, Lab Phys Chem Polymers & Membranes, CH-1015 Lausanne, Switzerland
[3] Int Univ Bremen, D-28726 Bremen, Germany
关键词
maltoporin; membrane channels; molecular sensors; outer membrane protein F (OmpF);
D O I
10.1109/TNB.2004.824271
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Membrane channels are typically around or less than 1 nm in diameter and a description of the flow through them requires a molecular approach called nanofluidic. The ion current through channels is extremely sensitive to pore sizes. It is tempting to use the ion current to probe conformational changes of the channel or, for a fixed channel conformation, the current can be used to follow binding of molecules to the pore surfaces. Here we show the sensitivity of this method. It is possible to observe the passage of single isolated molecules through the channel and it is possible to discriminate between different passing molecules. Bioengineering allows us to modify channel surfaces and the affinity to different host molecules. Combining engineered proteins with the appropriated detection technique will allow a new type of molecular sensor.
引用
收藏
页码:46 / 48
页数:3
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