Electrochemical and PM-IRRAS characterization of cholera toxin binding at a model biological membrane

A mixed phospholipid-cholestrol bilayer, with cholera toxin B (CTB) units attached to the monosialotetrahexosylganglioside (GM1) binding sites in the distal leaflet, was deposited on a Au(111) electrode surface. Polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) measureme...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 29(2013), 3 vom: 22. Jan., Seite 965-76
1. Verfasser: Leitch, J Jay (VerfasserIn)
Weitere Verfasser: Brosseau, Christa L, Roscoe, Sharon G, Bessonov, Kyrylo, Dutcher, John R, Lipkowski, Jacek
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Gangliosides Gold 7440-57-5 Cholera Toxin 9012-63-9
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520 |a A mixed phospholipid-cholestrol bilayer, with cholera toxin B (CTB) units attached to the monosialotetrahexosylganglioside (GM1) binding sites in the distal leaflet, was deposited on a Au(111) electrode surface. Polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) measurements were used to characterize structural and orientational changes in this model biological membrane upon binding CTB and the application of the electrode potential. The data presented in this article show that binding cholera toxin to the membrane leads to an overall increase in the tilt angle of the fatty acid chains; however, the conformation of the bilayer remains relatively constant as indicated by the small decrease in the total number of gauche conformers of acyl tails. In addition, the bound toxin caused a significant decrease in the hydration of the ester group contained within the lipid bilayer. Furthermore, changes in the applied potential had a minimal effect on the overall structure of the membrane. In contrast, our results showed significant voltage-dependent changes in the average orientation of the protein α-helices that may correspond to the voltage-gated opening and closing of the central pore that resides within the B subunit of cholera toxin 
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700 1 |a Brosseau, Christa L  |e verfasserin  |4 aut 
700 1 |a Roscoe, Sharon G  |e verfasserin  |4 aut 
700 1 |a Bessonov, Kyrylo  |e verfasserin  |4 aut 
700 1 |a Dutcher, John R  |e verfasserin  |4 aut 
700 1 |a Lipkowski, Jacek  |e verfasserin  |4 aut 
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