Evidence map›Paper›PMID 32403086›Full record

ArticleEBioMedicine2020

Antimicrobial and antibiofilm activity of the EeCentrocin 1 derived peptide EC1-17KV via membrane disruption.

Lingman Ma, Xinyue Ye, Pengbo Sun, Pengfei Xu, Liping Wang, Zixiang Liu, Xiaowei Huang, Zhaoshi Bai, Changlin Zhou

Open access · goldAbstract read
In one paragraph

Article in EBioMedicine, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 44 citations in OpenAlex.

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  15. Review
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  17. A truncated peptide SpgillcinFrontiers in cellular and infection microbiology · 2022
    Article
  18. Article
  19. Article
  20. 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

9 authors at 2 institutions in 1 country.

Lingman MaSchool of Life Science and Technology, China Pharmaceutical University, Nanjing, Jiangsu 211198, China.
Xinyue YeSchool of Life Science and Technology, China Pharmaceutical University, Nanjing, Jiangsu 211198, China.
Pengbo SunSchool of Life Science and Technology, China Pharmaceutical University, Nanjing, Jiangsu 211198, China.
Pengfei XuSchool of Life Science and Technology, China Pharmaceutical University, Nanjing, Jiangsu 211198, China.
Liping WangSchool of Life Science and Technology, China Pharmaceutical University, Nanjing, Jiangsu 211198, China.
Zixiang LiuSchool of Life Science and Technology, China Pharmaceutical University, Nanjing, Jiangsu 211198, China.
Xiaowei HuangSchool of Life Science and Technology, China Pharmaceutical University, Nanjing, Jiangsu 211198, China.
Zhaoshi BaiJiangsu Cancer Hospital & Jiangsu Institute of Cancer Research & the Affiliated Cancer Hospital of Nanjing Medical University, Nanjing, Jiangsu 210009, China. Electronic address: baizhaoshi23@126.com.
Changlin ZhouSchool of Life Science and Technology, China Pharmaceutical University, Nanjing, Jiangsu 211198, China. Electronic address: cl_zhou@cpu.edu.cn.
China Pharmaceutical University · CNJiangsu Cancer Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe antibiotic resistance and biofilm formation of pathogenic microbes exacerbate the difficulties of anti-infection therapy in the clinic. The structural modification of antimicrobial peptides (AMP) is an effective strategy to develop novel anti-infective agents.

methodSeventeen amino acids (AA) in the longer chain of EeCentrocin 1 (from the edible sea-urchin Echinus esculentus) were truncated and underwent further modification. To produce lead peptides with low toxicity and high efficacy, the antimicrobial activity or cytotoxicity of peptides was evaluated against various multidrug-resistant bacteria/fungi or mammalian cells in vivo/ in vitro. In addition, the stability and modes of action of the lead peptide were investigated.

findingsEC1-17KV displayed potent activity and an expanded antimicrobial spectrum, especially against drug-resistant gram-negative bacteria and fungi, attributable to its enhanced amphiphilicity and net charge. In addition, it exhibits bactericidal/fungicidal activity and effectively increased the animal survival rate and mitigated the histopathological damage induced by multidrug-resistant P. aeruginosa or C. albicans in infected mice or G. mellonella. Moreover, EC1-17KV had a poor ability to induce resistance in bacteria and fungi and exhibited desirable high-salt/high-temperature tolerance properties. In bacteria, EC1-17KV promoted divalent cation release to damage bacterial membrane integrity. In fungi, it changed C. albicans membrane fluidity to increase membrane permeabilization or reduced hyphal formation to suppress biofilm formation.

interpretationEC1-17KV is a promising lead peptide for the development of antimicrobial agents against antibiotic resistant bacteria and fungi.

fundingThis work was funded by the National Natural Science Foundation of China (No. 81673483, 81803591); National Science and Technology Major Project Foundation of China (2019ZX09721001-004-005); National Key Research and Development Program of China (2018YFA0902000); "Double First-Class" University project (CPU2018GF/GY16); Natural Science Foundation of Jiangsu Province of China (No. BK20180563); and A Project Funded by the Priority Academic Program Development of Jiangsu Higher Education Institutions.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsAntimicrobial Cationic PeptidesBiofilmsCandida albicansHumansMiceMicrobial Sensitivity TestsMothsProtein EngineeringPseudomonas aeruginosaPseudomonas InfectionsSea UrchinsStructure-Activity RelationshipSurface-Active AgentsAntimicrobial Cationic PeptidesSurface-Active AgentsAMP structural modificationAntibiofilm effectAntibiotic resistanceAntimicrobial activityEC1-17KVMembrane destruction

Identifiers

PMID32403086
PMCPMC7218270
OpenAlexW3022117017

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.