Evidence map›Paper›PMID 28248511›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2017

Optimization of the Small Glycan Presentation for Binding a Tumor-Associated Antibody: Application to the Construction of an Ultrasensitive Glycan Biosensor.

Filip Kveton, Anna Blšáková, Andras Hushegyi, Pavel Damborsky, Ola Blixt, Bo Jansson, Jan Tkac

Open access · greenAbstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Glycan Nanobiosensors.Nanomaterials (Basel, Switzerland) · 2020
    Review
  3. Article
  4. 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

7 authors at 3 institutions in 3 countries.

Filip KvetonDepartment of Glycobiotechnology, Institute of Chemistry, Slovak Academy of Sciences , Dubravska cesta 9, 845 38 Bratislava, Slovakia.
Anna BlšákováDepartment of Glycobiotechnology, Institute of Chemistry, Slovak Academy of Sciences , Dubravska cesta 9, 845 38 Bratislava, Slovakia.
Andras HushegyiDepartment of Glycobiotechnology, Institute of Chemistry, Slovak Academy of Sciences , Dubravska cesta 9, 845 38 Bratislava, Slovakia.
Pavel DamborskyDepartment of Glycobiotechnology, Institute of Chemistry, Slovak Academy of Sciences , Dubravska cesta 9, 845 38 Bratislava, Slovakia.
Ola BlixtDepartment of Chemistry, University of Copenhagen , 1871 Frederiksberg, Copenhagen, Denmark.ORCID 0000-0003-4143-6276
Bo JanssonDivision of Oncology and Pathology, Department of Clinical Sciences, Lund, Lund University , Lund, SE 221 85 Sweden.
Jan TkacDepartment of Glycobiotechnology, Institute of Chemistry, Slovak Academy of Sciences , Dubravska cesta 9, 845 38 Bratislava, Slovakia.ORCID 0000-0002-0765-7262
Institute of Chemistry of the Slovak Academy of Sciences · SKLund University · SEUniversity of Copenhagen · DK

Funding

European Research Council 311532
6 · The paper itself

Abstract

The main aim of the study was to optimize the interfacial presentation of a small antigen-a Tn antigen (N-acetylgalactosamine)-for binding to its analyte anti-Tn antibody. Three different methods for the interfacial display of a small glycan are compared here, including two methods based on the immobilization of the Tn antigen on a mixed self-assembled monolayer (SAM) (2D biosensor) and the third one utilizing a layer of a human serum albumin (HSA) for the immobilization of a glycan forming a 3D interface. Results showed that the 3D interface with the immobilized Tn antigen is the most effective bioreceptive surface for binding its analyte. The 3D impedimetric glycan biosensor exhibited a limit of detection of 1.4 aM, a wide linear range (6 orders of magnitude), and high assay reproducibility with an average relative standard deviation of 4%. The buildup of an interface was optimized using various techniques with the visualization of the glycans on the biosensor surface by atomic force microscopy. The study showed that the 3D biosensor is not only the most sensitive compared to other two biosensor platforms but that the Tn antigen on the 3D biosensor surface is more accessible for antibody binding with better kinetics of binding (t

Indexed as

Biosensing TechniquesAntibodiesKineticsMicroscopy, Atomic ForcePolysaccharidesAntibodiesPolysaccharides

Identifiers

PMID28248511
PMCPMC5659382
OpenAlexW2592067375

What OpenQuestion holds

Textmetadata
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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.