Severity: Warning
Message: file_get_contents(https://...@pubfacts.com&api_key=b8daa3ad693db53b1410957c26c9a51b4908&a=1): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 176
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 176
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 250
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3122
Function: getPubMedXML
File: /var/www/html/application/controllers/Detail.php
Line: 575
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 489
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 316
Function: require_once
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.
Download full-text PDF |
Source |
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http://dx.doi.org/10.1021/acsabm.1c00878 | DOI Listing |
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