Evidence map›Paper›PMID 32670215›Full record

ArticleFrontiers in microbiology2020

The Critical Role of Tryptophan in the Antimicrobial Activity and Cell Toxicity of the Duck Antimicrobial Peptide DCATH.

Xingjun Feng, Sanjun Jin, Min Wang, Qian Pang, Chunlong Liu, Ruiqi Liu, Yingjie Wang, Hao Yang, Fangju Liu, Yueying Liu

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 57 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

10 authors at 3 institutions in 1 country.

Xingjun FengInstitute of Animal Nutrition, Northeast Agricultural University, Harbin, China.
Sanjun JinInstitute of Animal Nutrition, Northeast Agricultural University, Harbin, China.
Min WangInstitute of Animal Nutrition, Northeast Agricultural University, Harbin, China.
Qian PangInstitute of Animal Nutrition, Northeast Agricultural University, Harbin, China.
Chunlong LiuNortheast Institute of Geography and Agricultural Ecology, Chinese Academy of Sciences, Harbin, China.
Ruiqi LiuInstitute of Animal Nutrition, Northeast Agricultural University, Harbin, China.
Yingjie WangInstitute of Animal Nutrition, Northeast Agricultural University, Harbin, China.
Hao YangInstitute of Animal Nutrition, Northeast Agricultural University, Harbin, China.
Fangju LiuInstitute of Animal Nutrition, Northeast Agricultural University, Harbin, China.
Yueying LiuCollege of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, China.
Northeast Agricultural University · CNNortheast Institute of Geography and Agroecology · CNZhejiang University of Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) have attracted more attention for their potential candidates for new antibiotic drugs. As a novel identified cathelicidin AMP from duck, dCATH owns broad-spectrum antimicrobial activities but with a noticeable toxicity. To explore dCATH-derived AMPs with reduced cell toxicity and improved cell selectivity, a series of truncated and tryptophan-replaced peptides of dCATH were designed. Two truncated peptides containing one of the two tryptophan (Trp) residues at the positions of 4 and 17 (W4 and W17) of dCATH, dCATH(1-16) and dCATH(5-20), showed strong antibacterial activity, but didn't show obvious hemolytic activity and cytotoxicity. The derived peptides not containing Trp didn't possess obvious antimicrobial activity, and their hemolytic and cytotoxic effect was also diminished. Also as evidence by Trp fluorescence experiment that existence of W4 and W17 was crucially important to the antimicrobial activity, hemolysis and cytotoxicity of dCATH, and one of the two Trp residues was competent and necessary to retain its antimicrobial activity. Antibacterial mechanism analysis showed that dCATH(1-16) and dCATH(5-20) killed bacterial cells by increasing permeability and causing a loss of membrane integrity. dCATH(1-16) and dCATH(5-20) possessed insignificant inhibitory activity against levels of IL-6, TNF-α, and NO in RAW 264.7 cells treated with LPS.

Indexed as

antimicrobial mechanismantimicrobial peptidescathelicidincell selectivitylipopolysaccharidemicetryptophan

Identifiers

PMID32670215
PMCPMC7326067
OpenAlexW3032353527

What OpenQuestion holds

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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.