Evidence map›Paper›PMID 35197521›Full record

ArticleScientific reports2022

Electric-field induced modulation of amorphous protein aggregates: polarization, deformation, and reorientation.

Kyongok Kang, Florian Platten

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 31% 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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
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  5. Voltage-calibrated, finely tunable protein assembly.Journal of the Royal Society, Interface · 2023
    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

2 authors at 1 institution in 1 country.

Kyongok KangForschungszentrum Jülich, Institute of Biological Information Processing IBI-4, Biomacromolecular Systems and Processes, Jülich, Germany. k.kang@fz-juelich.de.ORCID http://orcid.org/0000-0002-8790-9350
Florian PlattenForschungszentrum Jülich, Institute of Biological Information Processing IBI-4, Biomacromolecular Systems and Processes, Jülich, Germany. florian.platten@hhu.de.ORCID http://orcid.org/0000-0001-5912-1833
Forschungszentrum Jülich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins in their native state are only marginally stable and tend to aggregate. However, protein misfolding and condensation are often associated with undesired processes, such as pathogenesis, or unwanted properties, such as reduced biological activity, immunogenicity, or uncontrolled materials properties. Therefore, controlling protein aggregation is very important, but still a major challenge in various fields, including medicine, pharmacology, food processing, and materials science. Here, flexible, amorphous, micron-sized protein aggregates composed of lysozyme molecules reduced by dithiothreitol are used as a model system. The preformed amorphous protein aggregates are exposed to a weak alternating current electric field. Their field response is followed in situ by time-resolved polarized optical microscopy, revealing field-induced deformation, reorientation and enhanced polarization as well as the disintegration of large clusters of aggregates. Small-angle dynamic light scattering was applied to probe the collective microscopic dynamics of amorphous aggregate suspensions. Field-enhanced local oscillations of the intensity auto-correlation function are observed and related to two distinguishable elastic moduli. Our results validate the prospects of electric fields for controlling protein aggregation processes.

Indexed as

ElectricityProtein AggregatesDithiothreitolDynamic Light ScatteringMicroscopy, PolarizationMuramidaseSuspensionsDithiothreitolMuramidaseProtein AggregatesSuspensions

Identifiers

PMID35197521
PMCPMC8866516
OpenAlexW4214488380

What OpenQuestion holds

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LicenceCC BY
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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.