J 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
Name: CEITEC 2020 (Acronym: CEITEC2020)
Investor: Ministry of Education, Youth and Sports of the CR