Evidence map›Paper›PMID 23601864›Full record

ArticleTalanta2013

Label-free detection of glycoproteins by the lectin biosensor down to attomolar level using gold nanoparticles.

Tomas Bertok, Alena Sediva, Jaroslav Katrlik, Pavol Gemeiner, Milan Mikula, Martin Nosko, Jan Tkac

Abstract read
In one paragraph

Article in Talanta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

27 citing papers in PubMed, 91 citations in OpenAlex.

  1. Review
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  11. Lectins, Interconnecting Proteins with Biotechnological/Pharmacological and Therapeutic Applications.Evidence-based complementary and alternative medicine : eCAM · 2017
    Review
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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

7 authors at 2 institutions in 1 country.

Tomas BertokDepartment of Glycobiotechnology, Institute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, 845 38 Bratislava, Slovak Republic.
Alena Sediva
Jaroslav Katrlik
Pavol Gemeiner
Milan Mikula
Martin Nosko
Jan Tkac
Slovak Academy of Sciences · SKSlovak University of Technology in Bratislava · SK

Funding

European Research Council 311532
6 · The paper itself

Abstract

We present here an ultrasensitive electrochemical biosensor based on a lectin biorecognition capable to detect concentrations of glycoproteins down to attomolar (aM) level by investigation of changes in the charge transfer resistance (Rct) using electrochemical impedance spectroscopy (EIS). On polycrystalline gold modified by an aminoalkanethiol linker layer, gold nanoparticles were attached. A Sambucus nigra agglutinin was covalently immobilised on a mixed self-assembled monolayer formed on gold nanoparticles and finally, the biosensor surface was blocked by poly(vinyl alcohol). The lectin biosensor was applied for detection of sialic acid containing glycoproteins fetuin and asialofetuin. Building of a biosensing interface was carefully characterised by a broad range of techniques such as electrochemistry, EIS, atomic force microscopy, scanning electron microscopy and surface plasmon resonance with the best performance of the biosensor achieved by application of HS-(CH2)11-NH2 linker and gold nanoparticles with a diameter of 20 nm. The lectin biosensor responded to an addition of fetuin (8.7% of sialic acid) with sensitivity of (338 ± 11) Ω decade(-1) and to asialofetuin (≤ 0.5% of sialic acid) with sensitivity of (109 ± 10) Ω decade(-1) with a blank experiment with oxidised asialofetuin (without recognisable sialic acid) revealing sensitivity of detection of (79 ± 13) Ω decade(-1). These results suggest the lectin biosensor responded to changes in the glycan amount in a quantitative way with a successful validation by a lectin microarray. Such a biosensor device has a great potential to be employed in early biomedical diagnostics of diseases such as arthritis or cancer, which are connected to aberrant glycosylation of protein biomarkers in biological fluids.

Indexed as

Biosensing TechniquesAsialoglycoproteinsElectrochemistryFetuinsGoldLectinsMetal NanoparticlesN-Acetylneuraminic AcidProtein Array AnalysisasialofetuinAsialoglycoproteinsFetuinsGoldLectinsN-Acetylneuraminic Acid

Identifiers

PMID23601864
PMCPMC4881810
OpenAlexW2053231021

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.