Electrochemical detection of protein glycosylation using lectin and protein–gold affinity interactions
Literature Information
Publication Date
2016-03-11
DOI
10.1039/C6AN00528D
Impact Factor
4.616
Authors
Laura G. Carrascosa, Abu A. I. Sina, Muhammad J. A. Shiddiky
View Original
Abstract
We report a new method for the electrochemical detection of glycosylation on proteins, which relies on lectin–protein interaction on a bare gold electrode. The target protein isolated by immunoaffinity is directly adsorbed onto a gold surface and its glycosylation status is retrieved by subsequent addition of specific lectins. The adsorption and subsequent recognition process is monitored electrochemically in the presence of [Fe(CN)6]3−/4− redox system. By decoupling target protein capture from glycosylation read-out steps, this approach circumvents unwanted antibody–lectin crosstalk while enabling specific glycosylation detection of a glycoprotein in serum-spiked samples in less than 1 h.
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