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Immobilization of concanavalin A lectin on a reduced graphene oxide-thionine surface by glutaraldehyde crosslinking for the construction of an impedimetric biosensor

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dc.title Immobilization of concanavalin A lectin on a reduced graphene oxide-thionine surface by glutaraldehyde crosslinking for the construction of an impedimetric biosensor en
dc.contributor.author Filip, Jaroslav
dc.contributor.author Zavahir, Sifani
dc.contributor.author Kluková, Ludmila
dc.contributor.author Tkář, Ján
dc.contributor.author Kasák, Peter
dc.relation.ispartof Journal of Electroanalytical Chemistry
dc.identifier.issn 1572-6657 Scopus Sources, Sherpa/RoMEO, JCR
dc.date.issued 2017
utb.relation.volume 794
dc.citation.spage 156
dc.citation.epage 163
dc.type article
dc.language.iso en
dc.publisher Elsevier
dc.identifier.doi 10.1016/j.jelechem.2017.04.019
dc.relation.uri https://www.sciencedirect.com/science/article/pii/S157266571730259X
dc.subject Affinity biosensor en
dc.subject Reduced graphene oxide en
dc.subject Thionine en
dc.subject Concanavalin A en
dc.subject Invertase en
dc.description.abstract Lectins, which are proteins with selective affinity to glycans or glycoproteins, have been recognized as promising agents for the construction of devices for the detection of specific glycoproteins and for glycoprofiling. This allows for the exploration of new potential biomarkers and for early diagnosis by detection of already known glycosylated biomarkers. In this work, immobilization of Concanavalin A (ConA) lectin on an electrochemically reduced graphene oxide (ErGO)/thionine (Thi) surface via glutaraldehyde (GA) crosslinking is investigated and applied for the impedimetric detection of the glycoprotein invertase (INV). An attachment of ConA/GA aggregates to the ErGO/Thi surface leads to a biosensor with a linear response in the concentration range of 10− 14–10− 8 mol for INV and a sensitivity of 6.1% of RCT change per decade of INV concentration. The sensitivity towards a negative control, i.e., INV with oxidized glycan moieties, is 2.97-fold lower than that towards INV. These findings provide a platform for the development of lectin-based, miniature and cheap biosensors for possible future disease diagnosis. © 2017 Elsevier B.V. en
utb.faculty Faculty of Technology
dc.identifier.uri http://hdl.handle.net/10563/1007354
utb.identifier.obdid 43876691
utb.identifier.scopus 2-s2.0-85018524623
utb.identifier.wok 000403128200022
utb.identifier.coden JECHE
utb.source j-scopus
dc.date.accessioned 2017-09-08T12:14:44Z
dc.date.available 2017-09-08T12:14:44Z
dc.description.sponsorship NPRP-6-381-1-078, QNRF, Qatar National Research Fund
dc.description.sponsorship NPRP grant from the Qatar National Research Fund (Qatar Foundation) [NPRP-6-381-1-078]
utb.contributor.internalauthor Filip, Jaroslav
utb.fulltext.affiliation Jaroslav Filip a,b, Sifani Zavahir a, Ludmila Klukova c, Jan Tkac c, Peter Kasak a⁎ a Center for Advanced Materials, Qatar University, P.O. Box 2713, Doha, Qatar b Department of Environmental Protection Engineering, Faculty of Technology, Tomas Bata University in Zlin, Vavreckova 275, 76001 Zlín, Czech Republic c Slovak Academy of Sciences, Institute of Chemistry, Department of Glycobiotechnology, Dubravska cesta 9, Bratislava SK-84538, Slovakia ⁎ Corresponding author. E-mail address: peter.kasak@qu.edu.qa (P. Kasak).
utb.fulltext.dates Received 12 December 2016 Received in revised form 3 April 2017 Accepted 11 April 2017 Available online 12 April 2017
utb.fulltext.faculty Faculty of Technology
utb.fulltext.ou Department of Environmental Protection Engineering
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