Evidence map›Paper›PMID 34063512›Full record

ArticlePolymers2021

Effect of Spherical Elements of Biosensors and Bioreactors on the Physicochemical Properties of a Peroxidase Protein.

Yuri D Ivanov, Vadim Yu Tatur, Tatyana O Pleshakova, Ivan D Shumov, Andrey F Kozlov, Anastasia A Valueva, Irina A Ivanova, Maria O Ershova, Nina D Ivanova, Victor V Repnikov and 2 more

Open access · goldAbstract read
In one paragraph

Article in Polymers, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

7 citing papers in PubMed, 16 citations in OpenAlex.

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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

12 authors at 3 institutions in 1 country.

Yuri D IvanovInstitute of Biomedical Chemistry, 119121 Moscow, Russia.
Vadim Yu TaturFoundation of Perspective Technologies and Novations, 115682 Moscow, Russia.
Tatyana O PleshakovaInstitute of Biomedical Chemistry, 119121 Moscow, Russia.
Ivan D ShumovInstitute of Biomedical Chemistry, 119121 Moscow, Russia.
Andrey F KozlovInstitute of Biomedical Chemistry, 119121 Moscow, Russia.
Anastasia A ValuevaInstitute of Biomedical Chemistry, 119121 Moscow, Russia.
Irina A IvanovaInstitute of Biomedical Chemistry, 119121 Moscow, Russia.
Maria O ErshovaInstitute of Biomedical Chemistry, 119121 Moscow, Russia.
Nina D IvanovaFoundation of Perspective Technologies and Novations, 115682 Moscow, Russia.
Victor V RepnikovBruker Ltd., 119017 Moscow, Russia.
Igor N StepanovFoundation of Perspective Technologies and Novations, 115682 Moscow, Russia.
Vadim S ZiborovInstitute of Biomedical Chemistry, 119121 Moscow, Russia.
Institute of Biomedical Chemistry · RUJoint Institute for High Temperatures · RUMoscow State Academy of Veterinary Medicine and Biotechnology named after Skryabin · RU

Funding

The Ministry of Science and Higher Education of the Russian Federation within the framework of state support for the creation and development of World-Class Research Centers "Digital bi-odesign and personalized healthcare" 075-15-2020-913
6 · The paper itself

Abstract

External electromagnetic fields are known to be able to concentrate inside the construction elements of biosensors and bioreactors owing to reflection from their surface. This can lead to changes in the structure of biopolymers (such as proteins), incubated inside these elements, thus influencing their functional properties. Our present study concerned the revelation of the effect of spherical elements, commonly employed in biosensors and bioreactors, on the physicochemical properties of proteins with the example of the horseradish peroxidase (HRP) enzyme. In our experiments, a solution of HRP was incubated within a 30 cm-diameter titanium half-sphere, which was used as a model construction element. Atomic force microscopy (AFM) was employed for the single-molecule visualization of the HRP macromolecules, adsorbed from the test solution onto mica substrates in order to find out whether the incubation of the test HRP solution within the half-sphere influenced the HRP aggregation state. Attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR) was employed in order to reveal whether the incubation of HRP solution within the half-sphere led to any changes in its secondary structure. In parallel, spectrophotometry-based estimation of the HRP enzymatic activity was performed in order to find out if the HRP active site was affected by the electromagnetic field under the conditions of our experiments. We revealed an increased aggregation of HRP after the incubation of its solution within the half-sphere in comparison with the control sample incubated far outside the half-sphere. ATR-FTIR allowed us to reveal alterations in HRP's secondary structure. Such changes in the protein structure did not affect its active site, as was confirmed by spectrophotometry. The effect of spherical elements on a protein solution should be taken into account in the development of the optimized design of biosensors and bioreactors, intended for performing processes involving proteins in biomedicine and biotechnology, including highly sensitive biosensors intended for the diagnosis of socially significant diseases in humans (including oncology, cardiovascular diseases, etc.) at early stages.

Indexed as

atomic force microscopybioreactorelectromagnetic fieldhorseradish peroxidaseprotein aggregation

Identifiers

PMID34063512
PMCPMC8155990
OpenAlexW3160392873

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.