Evidence map›Paper›PMID 30669262›Full record

ReviewBiosensors2019

Suppressing Non-Specific Binding of Proteins onto Electrode Surfaces in the Development of Electrochemical Immunosensors.

Jesús E Contreras-Naranjo, Oscar Aguilar

Abstract readReview
In one paragraph

Review in Biosensors, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Development of Functional Biointerface Using Mixed Zwitterionic Silatranes.Langmuir : the ACS journal of surfaces and colloids · 2024
    Article
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  7. Review
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  11. 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

2 authors.

Jesús E Contreras-NaranjoTecnologico de Monterrey, Escuela de Ingeniería y Ciencias. Ave. Eugenio Garza Sada 2501, Monterrey 64849, N.L., Mexico. a00825447@itesm.mx.
Oscar AguilarTecnologico de Monterrey, Escuela de Ingeniería y Ciencias. Ave. Eugenio Garza Sada 2501, Monterrey 64849, N.L., Mexico. alex.aguilar@tec.mx.ORCID 0000-0002-5352-9579

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Electrochemical immunosensors, EIs, are systems that combine the analytical power of electrochemical techniques and the high selectivity and specificity of antibodies in a solid phase immunoassay for target analyte. In EIs, the most used transducer platforms are screen printed electrodes, SPEs. Some characteristics of EIs are their low cost, portability for point of care testing (POCT) applications, high specificity and selectivity to the target molecule, low sample and reagent consumption and easy to use. Despite all these attractive features, still exist one to cover and it is the enhancement of the sensitivity of the EIs. In this review, an approach to understand how this can be achieved is presented. First, it is necessary to comprise thoroughly all the complex phenomena that happen simultaneously in the protein-surface interface when adsorption of the protein occurs. Physicochemical properties of the protein and the surface as well as the adsorption phenomena influence the sensitivity of the EIs. From this point, some strategies to suppress non-specific binding, NSB, of proteins onto electrode surfaces in order to improve the sensitivity of EIs are mentioned.

Indexed as

AntibodiesBiosensing TechniquesElectrochemical TechniquesElectrodesHumansImmunoassayNanostructuresProstate-Specific AntigenProteinsAntibodiesProstate-Specific AntigenProteinsEI sensitivity enhancementelectrochemical immunosensors (EIs)non-specific binding (NSB)protein adsorption

Identifiers

PMID30669262
PMCPMC6468902

What OpenQuestion holds

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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.