Evidence map›Paper›PMID 31222107›Full record

ArticleScientific reports2019

Self-assembly of plant protein fibrils interacting with superparamagnetic iron oxide nanoparticles.

Jing Li, Ievgen Pylypchuk, Daniel P Johansson, Vadim G Kessler, Gulaim A Seisenbaeva, Maud Langton

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.7field-weighted citation impact, top 8% 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

11 citing papers in PubMed, 41 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

6 authors at 1 institution in 1 country.

Jing LiThe Department of Molecular Sciences, SLU - Swedish University of Agricultural Sciences, Box 7015, SE-750 07, Uppsala, Sweden. jing.li@slu.se.ORCID http://orcid.org/0000-0001-5007-2705
Ievgen PylypchukThe Department of Molecular Sciences, SLU - Swedish University of Agricultural Sciences, Box 7015, SE-750 07, Uppsala, Sweden.ORCID http://orcid.org/0000-0001-5467-2839
Daniel P JohanssonThe Department of Molecular Sciences, SLU - Swedish University of Agricultural Sciences, Box 7015, SE-750 07, Uppsala, Sweden.
Vadim G KesslerThe Department of Molecular Sciences, SLU - Swedish University of Agricultural Sciences, Box 7015, SE-750 07, Uppsala, Sweden.ORCID http://orcid.org/0000-0001-7570-2814
Gulaim A SeisenbaevaThe Department of Molecular Sciences, SLU - Swedish University of Agricultural Sciences, Box 7015, SE-750 07, Uppsala, Sweden. gulaim.seisenbaeva@slu.se.ORCID http://orcid.org/0000-0003-0072-6082
Maud LangtonThe Department of Molecular Sciences, SLU - Swedish University of Agricultural Sciences, Box 7015, SE-750 07, Uppsala, Sweden. maud.langton@slu.se.ORCID http://orcid.org/0000-0003-1565-6996
Swedish University of Agricultural Sciences · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In situ fibrillation of plant proteins in presence of the superparamagnetic iron oxide nanoparticles (NP) promoted formation of a hybrid nanocomposite. The morphology of NP-fibril composite was revealed using ex-situ atomic force microscopy (AFM) in air. The NP-fibrils were associated into extended multi-fibril structures, indicating that the addition of NPs promoted protein association via β-sheet assembly. Real-time movement of NPs attached to fibrils under an external magnetic field was visualized using in-situ AFM in liquid, revealing that composite structures were stable at low pH, and displaying dipolar property of the NPs in the composite at high pH. Changes in magnetic properties of NPs when interacting with protein fibrils were quantitatively mapped using magnetic force microscopy (MFM). The magnetic moment of the NPs in composite was increased by co-existing with protein at low pH, while their dipolar nature was maintained at high pH. Self-assembly of the protein into fibrils is accelerated with increasing NP concentration within an optimal range, which is attributed to a fibrillation-competent conformation of the peptides. The latter was explained by the formation of favorable hydrogen bonds, electrostatic interactions, and efficient surface energy transfer between NPs and proteins.

Indexed as

MagneticsElectrophoresis, Polyacrylamide GelMagnetite NanoparticlesMicroscopy, Atomic ForcePlant ProteinsProtein BindingSpectroscopy, Fourier Transform InfraredMagnetite NanoparticlesPlant Proteins

Identifiers

PMID31222107
PMCPMC6586877
OpenAlexW2951437120

What Socratic 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 Socratic graph.