Evidence map›Paper›PMID 26864123›Full record

ArticleScientific reports2016

Green fluorescent protein as a scaffold for high efficiency production of functional bacteriotoxic proteins in Escherichia coli.

Nagasundarapandian Soundrarajan, Hye-Sun Cho, Byeongyong Ahn, Minkyung Choi, Le Minh Thong, Hojun Choi, Se-Yeoun Cha, Jin-Hoi Kim, Choi-Kyu Park, Kunho Seo and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.8field-weighted citation impact, top 11% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Effective Healing ofInternational journal of molecular sciences · 2023
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Rediscovery of antimicrobial peptides as therapeutic agents.Journal of microbiology (Seoul, Korea) · 2021
    Review
  10. Article
  11. Article
  12. Fluorescence modeling ofBiomedical optics express · 2019
    Article
  13. Article
  14. Review
  15. 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

11 authors at 3 institutions in 1 country.

Nagasundarapandian SoundrarajanDepartment of Animal Biotechnology, Konkuk University, Seoul 143-701, Korea.
Hye-Sun ChoDepartment of Animal Biotechnology, Konkuk University, Seoul 143-701, Korea.
Byeongyong AhnDepartment of Animal Biotechnology, Konkuk University, Seoul 143-701, Korea.
Minkyung ChoiDepartment of Animal Biotechnology, Konkuk University, Seoul 143-701, Korea.
Le Minh ThongDepartment of Animal Biotechnology, Konkuk University, Seoul 143-701, Korea.
Hojun ChoiDepartment of Animal Biotechnology, Konkuk University, Seoul 143-701, Korea.
Se-Yeoun ChaDepartment of Infectious and Avian Diseases, Chonbuk National University, Iksan 570-752, Korea.
Jin-Hoi KimDepartment of Animal Biotechnology, Konkuk University, Seoul 143-701, Korea.
Choi-Kyu ParkCollege of Veterinary Medicine, Kyungpook National University, Daegu 702-701, Korea.
Kunho SeoCollege of Veterinary Medicine, Konkuk University, Seoul Seoul 143-701, Korea.
Chankyu ParkDepartment of Animal Biotechnology, Konkuk University, Seoul 143-701, Korea.
Konkuk University · KRJeonbuk National University · KRKyungpook National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The availability of simple, robust, and cost-effective methods for the large-scale production of bacteriotoxic peptides such as antimicrobial peptides (AMPs) is essential for basic and pharmaceutical research. However, the production of bacteriotoxic proteins has been difficult due to a high degree of toxicity in bacteria and proteolytic degradation. In this study, we inserted AMPs into the Green fluorescent protein (GFP) in a loop region and expressed them as insoluble proteins in high yield, circumventing the inherent toxicity of AMP production in Escherichia coli. The AMPs inserted were released by cyanogen bromide and purified by chromatography. We showed that highly potent AMPs such as Protegrin-1, PMAP-36, Buforin-2, and Bactridin-1 are produced in high yields and produced AMPs showed similar activities compared to chemically synthesized AMPs. We increased the yield more than two-fold by inserting three copies of Protegrin-1 in the GFP scaffold. The immunogold electron micrographs showed that the expressed Protegrin-1 in the GFP scaffold forms large and small size aggregates in the core region of the inclusion body and become entirely nonfunctional, therefore not influencing the proliferation of E. coli. Our novel method will be applicable for diverse bacteriotoxic peptides which can be exploited in biomedical and pharmaceutical researches.

Indexed as

Antimicrobial Cationic PeptidesCyanogen BromideEscherichia coliGene DosageGene ExpressionGreen Fluorescent ProteinsInclusion BodiesMicrobial Sensitivity TestsMicroscopy, Electron, TransmissionModels, MolecularProtein AggregatesProteinsProtein Structure, SecondaryPseudomonas aeruginosaRecombinant Fusion ProteinsSolubilityAntimicrobial Cationic Peptidesbuforin IICyanogen BromideGreen Fluorescent ProteinsPMAP-36protegrin-1Protein AggregatesProteinsRecombinant Fusion Proteins

Identifiers

PMID26864123
PMCPMC4749965
OpenAlexW2411946388

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.