Jump to main content
Jump to site search

Issue 8, 2016
Previous Article Next Article

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

Author affiliations

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

Back to tab navigation

Supplementary files

Publication details

The article was received on 04 Mar 2016, accepted on 04 Mar 2016 and first published on 11 Mar 2016


Article type: Communication
DOI: 10.1039/C6AN00528D
Author version
available:
Download author version (PDF)
Analyst, 2016,141, 2356-2361

  •   Request permissions

    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

Search articles by author

Spotlight

Advertisements