Contact Us | Language: čeština English
Title: | Immobilization of concanavalin A lectin on a reduced graphene oxide-thionine surface by glutaraldehyde crosslinking for the construction of an impedimetric biosensor | ||||||||||
Author: | Filip, Jaroslav; Zavahir, Sifani; Kluková, Ludmila; Tkář, Ján; Kasák, Peter | ||||||||||
Document type: | Peer-reviewed article (English) | ||||||||||
Source document: | Journal of Electroanalytical Chemistry. 2017, vol. 794, p. 156-163 | ||||||||||
ISSN: | 1572-6657 (Sherpa/RoMEO, JCR) | ||||||||||
Journal Impact
This chart shows the development of journal-level impact metrics in time
|
|||||||||||
DOI: | https://doi.org/10.1016/j.jelechem.2017.04.019 | ||||||||||
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. | ||||||||||
Full text: | https://www.sciencedirect.com/science/article/pii/S157266571730259X | ||||||||||
Show full item record |