期刊
BIOSENSORS & BIOELECTRONICS
卷 203, 期 -, 页码 -出版社
ELSEVIER ADVANCED TECHNOLOGY
DOI: 10.1016/j.bios.2022.114024
关键词
Membranes; Membrane proteins; Ion channels; Electrochemistry; Inset olfaction
类别
资金
- Gesellschaft fur Forschungsforderung Niederosterreich m.b.H. [LSC19-026]
- European Research Council [ERC-StG 663677]
Membrane proteins are crucial drug targets, but studying them is challenging due to the complexity of the cellular membrane. Tethered membrane systems can replicate basic properties of the cellular membrane, making them ideal for studying membrane proteins thanks to their high electrical resistance and stability.
Membrane proteins are among the most important drug targets. To improve drug design, it is critical to study membrane proteins. However, due to the myriad roles fulfilled by the cellular membrane, it is a highly complex environment and challenging to study. Tethered membranes reproduce the basic physicochemical properties of the cellular membrane without its inherent complexity. The high electrical resistance and stability makes them ideal to study membrane proteins, particularly ion channels. However, due to the close proximity of the membrane to the support and the reduced fluidity and high packing density, they are unsuitable to study larger membrane proteins. We present here a tethered membrane system which adresses these challenges, allowing the functional reconstitution of the odorant receptor coreceptor from Drosophila melanogaster, a tetrameric ionotropic receptor was incorporated and its sensitivity to various ligands was examined via electrochemical impedance spectroscopy and atomic force microscopy.
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