Evidence map›Paper›PMID 34206350›Full record

ArticleInternational journal of molecular sciences2021

Reversible Lectin Binding to Glycan-Functionalized Graphene.

Tereza Koukalová, Petr Kovaříček, Pavla Bojarová, Valentino L P Guerra, Vladimír Vrkoslav, Lukáš Navara, Ivan Jirka, Marek Cebecauer, Vladimír Křen, Martin Kalbáč

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 47% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Tereza KoukalováJ. Heyrovsky Institute of Physical Chemistry of the Czech Academy of Sciences, Dolejškova 2155/3, 182 23 Prague, Czech Republic.
Petr KovaříčekJ. Heyrovsky Institute of Physical Chemistry of the Czech Academy of Sciences, Dolejškova 2155/3, 182 23 Prague, Czech Republic.ORCID 0000-0002-4404-3606
Pavla BojarováInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague, Czech Republic.ORCID 0000-0001-7069-0973
Valentino L P GuerraJ. Heyrovsky Institute of Physical Chemistry of the Czech Academy of Sciences, Dolejškova 2155/3, 182 23 Prague, Czech Republic.ORCID 0000-0002-3814-3993
Vladimír VrkoslavInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo Náměstí 542/2, 166 10 Praha, Czech Republic.
Lukáš NavaraJ. Heyrovsky Institute of Physical Chemistry of the Czech Academy of Sciences, Dolejškova 2155/3, 182 23 Prague, Czech Republic.
Ivan JirkaJ. Heyrovsky Institute of Physical Chemistry of the Czech Academy of Sciences, Dolejškova 2155/3, 182 23 Prague, Czech Republic.ORCID 0000-0002-0222-4855
Marek CebecauerJ. Heyrovsky Institute of Physical Chemistry of the Czech Academy of Sciences, Dolejškova 2155/3, 182 23 Prague, Czech Republic.ORCID 0000-0002-4606-1218
Vladimír KřenInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague, Czech Republic.ORCID 0000-0002-1091-4020
Martin KalbáčJ. Heyrovsky Institute of Physical Chemistry of the Czech Academy of Sciences, Dolejškova 2155/3, 182 23 Prague, Czech Republic.ORCID 0000-0001-9574-4368
Czech Academy of Sciences, J. Heyrovský Institute of Physical Chemistry · CZCzech Academy of Sciences · CZCzech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZ

Funding

European Regional Development Fund CZ.02.1.01/0.0/0.0/16_026/0008382Grantová Agentura České Republiky 18-09055YMinisterstvo Školství, Mládeže a Tělovýchovy LTAUSA19001Ministerstvo Školství, Mládeže a Tělovýchovy LTC20072Nadace Experientia Start-up grantVysoká Škola Chemicko-technologická v Praze Dagmar Prochazkova Fund starting grant
6 · The paper itself

Abstract

The 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.

Indexed as

GraphiteHorseradish PeroxidaseLectinsPolysaccharidesProtein BindingProtein Structure, QuaternaryGraphiteHorseradish PeroxidaseLectinsPolysaccharides2D materialscarbohydrategraphenesensorwheat germ agglutinin

Identifiers

PMID34206350
PMCPMC8267698
OpenAlexW3176993405

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.