Evidence map›Paper›PMID 32445120›Full record

ArticleProbiotics and antimicrobial proteins2020

Design and Synthesis of Lipopolysaccharide-Binding Antimicrobial Peptides Based on Truncated Rabbit and Human CAP18 Peptides and Evaluation of Their Action Mechanism.

Hamid Madanchi, Ramin Ebrahimi Kiasari, Seyed Javad Seyed Mousavi, Behrooz Johari, Ali Akbar Shabani, Soroush Sardari

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Article in Probiotics and antimicrobial proteins, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

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  15. [Antibacterial mechanism of Brevinin-2GHk, an antimicrobial peptide fromNan fang yi ke da xue xue bao = Journal of Southern Medical University · 2021
    Article
  16. Article
  17. 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 4 institutions in 1 country.

Hamid MadanchiDepartment of Biotechnology, School of Medicine, Semnan University of Medical Sciences, Semnan, Iran.
Ramin Ebrahimi KiasariDrug Design and Bioinformatics Unit, Medical Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Seyed Javad Seyed MousaviDrug Design and Bioinformatics Unit, Medical Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Behrooz JohariDepartment of Medical Biotechnology, School of Medicine, Zanjan University of Medical Sciences, Zanjan, Iran.
Ali Akbar ShabaniDepartment of Biotechnology, School of Medicine, Semnan University of Medical Sciences, Semnan, Iran.
Soroush SardariDrug Design and Bioinformatics Unit, Medical Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran. ssardari@hotmail.com.
Pasteur Institute of Iran · IRBiotechnology Research Center · IRSemnan University of Medical Sciences · IRZanjan University of Medical Sciences · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipopolysaccharide (LPS) is a toxic and immunogenic agent for human. Additionally, LPS is a good target for some antimicrobial compounds, including antimicrobial peptides (AMPs). LPS-binding peptides (LBPs) can recognize and neutralize LPS. Rabbit and human cathelicidins are AMPs with LPS-binding activity. In this study, we designed and synthesized two new truncated LBPs from rabbit and human CAP18 peptides by in silico methods. After synthesis of peptides, the antimicrobial properties and LPS-binding activity of these peptides were evaluated. The parental rabbit and human CAP18 peptides were selected as positive controls. Next, the changes in the secondary structure of these peptides before and after treatment with LPS were measured by circular dichroism (CD). Human cytotoxicity of the peptides was evaluated by MTT and red blood cells (RBCs) hemolysis assays. Finally, field emission scanning electron microscopy (FE-SEM), confocal microscopy, and flow cytometry were performed to study the action mechanism of these peptides. Results indicated that the hCap18 and rCap18 had antibacterial activity (at a MIC of 4-128 μg/mL). The results of the quantitative LAL test demonstrated that LPS-binding activity of hCap18 peptide was better than rCap18, while rCap18 peptide had better antimicrobial properties. Furthermore, rCap18 had less cytotoxicity than hCap18. However, both peptides were nontoxic for normal human skin fibroblast cell in MIC range. In conclusion, rCap18 has good antibacterial properties, while hCap18 can be tested as a diagnostic molecule in our future studies.

Indexed as

Drug DesignAcute-Phase ProteinsAmino Acid SequenceAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBacillus subtilisCarrier ProteinsCell LineCell SurvivalComputer SimulationErythrocytesEscherichia coliFibroblastsHemolysisHumansAcute-Phase ProteinsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesCarrier ProteinsLipopolysaccharide-Binding ProteinLipopolysaccharidesMembrane GlycoproteinsAntimicrobial peptidesCap18In silico drug designLipopolysaccharideLPS-binding peptide

Identifiers

PMID32445120
OpenAlexW3028133901

What OpenQuestion holds

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Read underepoch 390

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.