Send to

Choose Destination

See 1 citation found by title matching your search:

Bioelectrochemistry. 2017 Oct;117:89-94. doi: 10.1016/j.bioelechem.2017.06.005. Epub 2017 Jun 19.

Label-free chronopotentiometric glycoprofiling of prostate specific antigen using sialic acid recognizing lectins.

Author information

Institute of Chemistry, Slovak Academy of Sciences, Dubravska cesta 9, 845 38 Bratislava, Slovak Republic.
Institute of Biophysics, Czech Academy of Sciences, Kralovopolská 135, 612 65 Brno, Czech Republic.
CEITEC Central European Institute of Technology, Masaryk University, Kamenice 5, Brno 62500, Czech Republic.
Institute of Biophysics, Czech Academy of Sciences, Kralovopolská 135, 612 65 Brno, Czech Republic. Electronic address:


In recent decades, it has become clear that most of human proteins are glycosylated and that protein glycosylation plays an important role in health and diseases. At present, simple, fast and inexpensive methods are sought for clinical applications and particularly for improved diagnostics of various diseases, including cancer. We propose a label- and reagent-free electrochemical method based on chronopotentiometric stripping (CPS) analysis and a hanging mercury drop electrode for the detection of interaction of sialylated protein biomarker a prostate specific antigen (PSA) with two important lectins: Sambucus nigra agglutinin (SNA) and Maackia amurensis agglutinin (MAA). Incubation of PSA-modified electrode with specific SNA lectin resulted in an increase of CPS peak H of the complex as compared to this peak of individual PSA. By adjusting polarization current and temperature, PSA-MAA interaction can be either eliminated or distinguished from the more abundant PSA-SNA complex. CPS data were in a good agreement with the data obtained by complementary methods, namely surface plasmon resonance and fluorescent lectin microarray. It can be anticipated that CPS will find application in glycomics and proteomics.


A prostate specific antigen; Chronopotentiometric analysis; Lectin-glycoprotein interaction; Mercury electrode; Sialylated glycan isomers

[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center