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Protein binding to supported lipid membranes: investigation of the cholera toxin-ganglioside interaction by simultaneous impedance spectroscopy and surface plasmon resonance
Open accessAbstract
The specific recognition reaction between cholera toxin (ChTo) and the ganglioside GM1 was investigated in situ on planar supported lipid layers using simultaneous surface plasmon resonance (SPR) and electrochem. impedance measurements. The lipid monolayers contg. different amts. of GM1 were formed on alkanethiol-coated gold surfaces by a new lipid/detergent diln. technique. The formation of the layers was investigated using both SPR and impedance measurements. While the optical properties of the different lipid layers remained unchanged, the layer capacitance was seen to depend on the GM1 to POPC molar ratio. The selective binding of ChTo to these layers was detected with high sensitivity by SPR. The comparatively small impedance changes assocd. with the protein adsorption suggest a high water content of the ChTo layers. The B5 subunit interacts similarly with these supported lipid layers. [on SciFinder (R)]
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Cited by
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Cooper, M. A. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd838 · Cited by 1,015
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Tanaka, M., & Sackmann, E. (2005) · Nature · doi:10.1038/nature04164 · Cited by 915
In Situ Kinetics of Self-Assembly by Surface Plasmon Resonance Spectroscopy
Peterlinz, K. A., & Georgiadis, R. (1996) · Langmuir · doi:10.1021/la9508452 · Cited by 461
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Rose, L., & Jenkins, A. T. A. (2007) · Bioelectrochemistry · doi:10.1016/j.bioelechem.2006.05.009 · Cited by 81
Metadata
- Authors
- Terrettaz, S., Stora, T., Duschl, C., & Vogel, H.
- Venue
- Langmuir
- Publisher
- American Chemical Society (ACS)
- Published
- 1993-05
- Volume
- 9
- Issue
- 5
- Pages
- 1361-1369
- ISSN
- 0743-7463 (ISSN-L)
- 1520-5827
- OpenAlex
- W1974858284
- Cited by
- 223
- References
- 0
- FWCI
- 2.75
- Type
- journal article
- Language
- en
- Open access
- green
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