Number of the records: 1  

Reversible Lectin Binding to Glycan-Functionalized Graphene

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    SYSNO ASEP0551978
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleReversible Lectin Binding to Glycan-Functionalized Graphene
    Author(s) Koukalová, Tereza (MBU-M)
    Kovaříček, P. (CZ)
    Bojarová, Pavla (MBU-M) ORCID
    Guerra, V. L. P. (CZ)
    Vrkoslav, V. (CZ)
    Navara, L. (CZ)
    Jirka, I. (CZ)
    Cebecauer, M. (CZ)
    Křen, Vladimír (MBU-M) RID, ORCID
    Kalbáč, M. (CZ)
    Number of authors10
    Article number6661
    Source TitleInternational Journal of Molecular Sciences. - : MDPI
    Roč. 22, č. 13 (2021)
    Number of pages9 s.
    Languageeng - English
    CountryCH - Switzerland
    Keywordscopper ; graphene ; wheat germ agglutinin ; carbohydrate ; 2D materials ; sensor
    Subject RIVJJ - Other Materials
    OECD categoryNano-materials (production and properties)
    R&D ProjectsLTC20072 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    Method of publishingOpen access
    Institutional supportMBU-M - RVO:61388971
    UT WOS000671186500001
    EID SCOPUS85108207108
    DOI10.3390/ijms22136661
    AnnotationThe monolayer character of two-dimensional materials predestines them for application as active layers of sensors. However, their inherent high sensitivity is always accompanied by a low selectivity. Chemical functionalization of two-dimensional materials has emerged as a promising way to overcome the selectivity issues. Here, we demonstrate efficient graphene functionalization with carbohydrate ligands-chitooligomers, which bind proteins of the lectin family with high selectivity. Successful grafting of a chitooligomer library was thoroughly characterized, and glycan binding to wheat germ agglutinin was studied by a series of methods. The results demonstrate that the protein quaternary structure remains intact after binding to the functionalized graphene, and that the lectin can be liberated from the surface by the addition of a binding competitor. The chemoenzymatic assay with a horseradish peroxidase conjugate also confirmed the intact catalytic properties of the enzyme. The present approach thus paves the way towards graphene-based sensors for carbohydrate-lectin binding.
    WorkplaceInstitute of Microbiology
    ContactEliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
    Year of Publishing2022
    Electronic addresshttps://www.mdpi.com/1422-0067/22/13/6661
Number of the records: 1  

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