Protein-protein interactions at the cell surface are important in the activity of bacterial toxins such as colicins. We have developed methods to study these events using tethered lipid bilayers, which can be probed by impedance spectroscopy and surface plasmon resonance. Recently we have attached the receptor proteins directly to gold electrodes and this offers new possibilities for measuring protein-protein interactions on solid supports.

Keywords:
colicin, impedance spectroscopy, porin, surface plasmon resonance, ITC, isothermal titration microcalorimetry, SPR, surface plasmon resonance, octyl-POE, octyl-polyoxy-ethylene, T-domain, translocation domain, R-domain, receptor-binding domain, P-domain, toxic domain
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© 2001 Biochemical Society
2001
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