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Detection of Ganglioside-Specific Toxin Binding with Biomembrane-Based Bioelectronic Sensors. | LitMetric

Detection of Ganglioside-Specific Toxin Binding with Biomembrane-Based Bioelectronic Sensors.

ACS Appl Bio Mater

Robert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, New York 14853, United States.

Published: November 2021

AI Article Synopsis

  • * The research focuses on creating GM1-rich SLBs on conducting polymer electrodes to measure changes in electrical properties when interacting with cholera toxin.
  • * The findings demonstrate the effectiveness of this platform for detecting toxins in complex samples, understanding ganglioside interactions, and finding molecules that could inhibit these interactions.

Article Abstract

Gangliosides, glycolipids that are abundant in the plasma membrane outer leaflet, play an integral role in cellular recognition, adhesion, and infection by interacting with different endogenous molecules, viruses, and toxins. Model membrane systems, such as ganglioside-enriched supported lipid bilayers (SLBs), present a useful tool for sensing, characterizing, and quantifying such interactions. In this work, we report the formation of ganglioside GM1-rich SLBs on conducting polymer electrodes using a solvent-assisted lipid bilayer assembly method to investigate changes in membrane electrical properties upon binding of the B subunit of cholera toxin. The sensing capabilities of our platform were investigated by varying both the receptor and the toxin concentrations in the system as well as using a complex sample (milk contaminated with the toxin) and monitoring the changes in the electrical properties of the membrane. Our work highlights the potential of such conducting polymer-supported biomembrane-based platforms for detecting the toxins within a complex environment, studying ganglioside-specific biomolecular interactions with toxins and screening inhibitory molecules to prevent these interactions.

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Source
http://dx.doi.org/10.1021/acsabm.1c00878DOI Listing

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