4.6 Article

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

期刊

ANALYST
卷 141, 期 8, 页码 2356-2361

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ROYAL SOC CHEMISTRY
DOI: 10.1039/c6an00528d

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资金

  1. John and Mary Kibble Trust
  2. Canine Research Foundation
  3. University of Queensland Postdoctoral Research Fellowship [2012001456]
  4. NHMRC CDF [APP1088966]
  5. National Breast Cancer Foundation of Australia [CG-12-07]
  6. National Breast Cancer Foundation [NC-14-022] Funding Source: researchfish

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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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