Detailed Information on Publication Record
2017
Label-free chronopotentiometric glycoprofiling of prostate specific antigen using sialic acid recognizing lectins
BELICKY, Stefan, Hana CERNOCKA, Tomas BERTOK, Alena HOLAZOVA, Kamila RÉBLOVÁ et. al.Basic information
Original name
Label-free chronopotentiometric glycoprofiling of prostate specific antigen using sialic acid recognizing lectins
Authors
BELICKY, Stefan (703 Slovakia), Hana CERNOCKA (203 Czech Republic), Tomas BERTOK (703 Slovakia), Alena HOLAZOVA (703 Slovakia), Kamila RÉBLOVÁ (203 Czech Republic, guarantor, belonging to the institution), Emil PALECEK (203 Czech Republic), Jan TKAC (703 Slovakia) and Veronika OSTATNA (203 Czech Republic)
Edition
Bioelectrochemistry, SWITZERLAND, Elsevier Science SA, 2017, 1567-5394
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
Switzerland
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 3.789
RIV identification code
RIV/00216224:14740/17:00098091
Organization unit
Central European Institute of Technology
UT WoS
000407411700013
Keywords in English
A prostate specific antigen; Lectin-glycoprotein interaction; Sialylated glycan isomers; Chronopotentiometric analysis; Mercury electrode
Tags
Tags
International impact, Reviewed
Změněno: 1/3/2018 13:50, Mgr. Pavla Foltynová, Ph.D.
Abstract
V originále
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.
Links
LQ1601, research and development project |
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