Evidence map›Paper›PMID 31952436›Full record

ArticleIranian biomedical journal2020

Affinity Based Nano-Magnetic Particles for Purification of Recombinant Proteins in Form of Inclusion Body

Masoud Seyedinkhorasani, Reza Ahangari Cohan, Saeid Taghavi Fardood, Farzin Roohvand, Dariush Norouzian, Malihe Keramati

Open access · diamondAbstract read
In one paragraph

Article in Iranian biomedical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 45% 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

1 citing paper in PubMed, 7 citations in OpenAlex.

  1. 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

6 authors at 2 institutions in 1 country.

Masoud SeyedinkhorasaniNano-Biotechnology Department, Pasteur Institute of Iran, Tehran, Iran.
Reza Ahangari CohanNano-Biotechnology Department, Pasteur Institute of Iran, Tehran, Iran.
Saeid Taghavi Fardood2Department of Chemistry, University of Zanjan, Zanjan, Iran.
Farzin RoohvandVirology Department, Pasteur Institute of Iran, Tehran, Iran.
Dariush NorouzianNano-Biotechnology Department, Pasteur Institute of Iran, Tehran, Iran.
Malihe KeramatiNano-Biotechnology Department, Pasteur Institute of Iran, Tehran, Iran.
Pasteur Institute of Iran · IRUniversity of Zanjan · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: Protein purification is the most complicated issue in the downstream processes of recombinant protein production; therefore, improved selective purification methods are important. Affinity-based protein purification method using polyhistidine-tag (His-tag) and nickel-nitrilotriacetic acid (Ni-NTA) resins is one of the most common strategies. Magnetic nanoparticles (MNPs) can be used as a beneficial alternative for Ni-NTA resins. However, there is no data on the capability of MNPs for protein purification from inclusion bodies; this issue is studied here. Methods: Recombinant His-tagged proteins of enhanced green fluorescent protein (EGFP)-His and streptokinase (SK)-His were expressed in E. coli BL-21 (DE3) in soluble and inclusion body forms, respectively. MNPs including Fe3O4 magnetic core, SiO2 shell, and Ni2+ on the surface were synthesized by sol-gel and hydrothermal reactions and then characterized by X-ray powder diffraction, vibrating sample magnetometer, and scanning electron microscopy imaging. Both synthesized Fe3O4@NiSiO3 and Fe3O4@NixSiOy MNPs were employed to purify EGEP-His and SK-His under native and denaturing conditions, respectively. The quantity and purity of purified proteins were analyzed by micro-Bradford assay and SDS-PAGE, respectively. Results: Both synthesized MNPs were spherical and well-dispersed with the size ranging from 290 to 415 nm. Synthesized MNPs contained Fe3O4, SiO2 shell, and Ni2+ on their structures with suitable magnetization properties. Using Fe3O4@NiSiO3 and Fe3O4@NixSiOy yielded 192 and 188 µg/mg of SK-His, as compared to 207 and 195 µg/mg of EGFP-His, respectively. Conclusion: MNPs containing magnetic Fe3O4 core, SiO2 shell, and Ni2+on their surface are versatile alternatives for Ni-NTA resins in protein purification for proteins expressed in both soluble and inclusion body forms.

Indexed as

Chromatography, AffinityGreen Fluorescent ProteinsInclusion BodiesMagnetite NanoparticlesRecombinant ProteinsSilicon DioxideX-Ray Diffractionenhanced green fluorescent proteinGreen Fluorescent ProteinsMagnetite NanoparticlesRecombinant ProteinsSilicon DioxideHis-tagInclusion bodyMagnetic nanoparticleProtein purification

Identifiers

PMID31952436
PMCPMC7275627
OpenAlexW3008667797

What OpenQuestion holds

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LicenceCC BY
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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.