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Issue 8, 2016
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Electrochemical detection of protein glycosylation using lectin and protein–gold affinity interactions

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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.

Graphical abstract: Electrochemical detection of protein glycosylation using lectin and protein–gold affinity interactions

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Supplementary files

Article information


Submitted
04 Mar 2016
Accepted
04 Mar 2016
First published
11 Mar 2016

Analyst, 2016,141, 2356-2361
Article type
Communication
Author version available

Electrochemical detection of protein glycosylation using lectin and protein–gold affinity interactions

S. Yadav, L. G. Carrascosa, A. A. I. Sina, M. J. A. Shiddiky, M. M. Hill and M. Trau, Analyst, 2016, 141, 2356
DOI: 10.1039/C6AN00528D

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