Evidence map›Paper›PMID 33263333›Full record

ArticleJournal of microbiology and biotechnology2021

Anti-Endotoxin 9-Meric Peptide with Therapeutic Potential for the Treatment of Endotoxemia.

Manigandan Krishnan, Joonhyeok Choi, Sungjae Choi, Yangmee Kim

Open access · bronzeAbstract read
In one paragraph

Article in Journal of microbiology and biotechnology, 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
0.8field-weighted citation impact, top 28% 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, 8 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Antiseptic 9-Meric Peptide with Potency against Carbapenem-ResistantInternational journal of molecular sciences · 2021
    Article
  7. 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

4 authors at 1 institution in 1 country.

Manigandan KrishnanDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 05029, Republic of Korea.
Joonhyeok ChoiDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 05029, Republic of Korea.
Sungjae ChoiDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 05029, Republic of Korea.
Yangmee KimDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 05029, Republic of Korea.
Konkuk University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inflammatory reactions activated by lipopolysaccharide (LPS) of gram-negative bacteria can lead to severe septic shock. With the recent emergence of multidrug-resistant gram-negative bacteria and a lack of efficient ways to treat resulting infections, there is a need to develop novel anti-endotoxin agents. Antimicrobial peptides have been noticed as potential therapeutic molecules for bacterial infection and as candidates for new antibiotic drugs. We previously designed the 9-meric antimicrobial peptide Pro9-3 and it showed high antimicrobial activity against gram-negative bacteria. Here, to further examine its potency as an anti-endotoxin agent, we examined the antiendotoxin activities of Pro9-3 and elucidated its mechanism of action. We performed a dye-leakage experiment and BODIPY-TR cadaverine and limulus amebocyte lysate assays for Pro9-3 as well as its lysine-substituted analogue and their enantiomers. The results confirmed that Pro9-3 targets the bacterial membrane and the arginine residues play key roles in its antimicrobial activity. Pro9-3 showed excellent LPS-neutralizing activity and LPS-binding properties, which were superior to those of other peptides. Saturation transfer difference-nuclear magnetic resonance experiments to explore the interaction between LPS and Pro9-3 revealed that Trp

Indexed as

AnimalsAnti-Infective AgentsAntimicrobial Cationic PeptidesAntisepsisDisease Models, AnimalEndotoxemiaEndotoxinsFemaleGram-Negative BacteriaGram-Negative Bacterial InfectionsImmunoglobulinsLipopolysaccharidesMembrane ProteinsMiceMicrobial Sensitivity TestsShock, SepticAnti-Infective Agentsantilipopolysaccharide antibodiesAntimicrobial Cationic Peptidesendotoxin binding proteinsEndotoxinsImmunoglobulinsLipopolysaccharidesMembrane ProteinsAntimicrobial peptideendotoxemiagram-negative infectionLPSLPS binding assaySTD-NMR

Identifiers

PMID33263333
PMCPMC9705858
OpenAlexW3107274238

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.