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

0485548 - BFÚ 2018 RIV CH eng J - Článek v odborném periodiku
Belicky, S. - Černocká, Hana - Bertok, T. - Holazova, A. - Réblová, K. - Paleček, Emil - Tkáč, J. - Ostatná, Veronika
Label-free chronopotentiometric glycoprofiling of prostate specific antigen using sialic acid recognizing lectins.
Bioelectrochemistry. Roč. 117, OCT2017 (2017), s. 89-94. ISSN 1567-5394. E-ISSN 1878-562X
Grant CEP: GA ČR(CZ) GA15-15479S
Institucionální podpora: RVO:68081707
Klíčová slova: amalgam electrodes * cancer * glycosylation * interface
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 3.789, rok: 2017

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. (C) 2017 Elsevier B.V. All tights reserved.
Trvalý link: http://hdl.handle.net/11104/0280516