Evidence map›Paper›PMID 26552969›Full record

ArticleAntimicrobial agents and chemotherapy2016

Antimicrobial Peptide CMA3 Derived from the CA-MA Hybrid Peptide: Antibacterial and Anti-inflammatory Activities with Low Cytotoxicity and Mechanism of Action in Escherichia coli.

Jong-Kook Lee, Chang Ho Seo, Tudor Luchian, Yoonkyung Park

Open access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 14% 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

37 citing papers in PubMed, 1 synthesis or guideline pooled it, 55 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Peptide PN5 fromACS omega · 2025
    Article
  4. Review
  5. Article
  6. Article
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  10. Article
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  12. Article
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  15. Article
  16. Article
  17. Article
  18. Review
  19. Expression of Hybrid Peptide EF-1 inMolecules (Basel, Switzerland) · 2020
    Article
  20. Therapeutic Effect and Mechanisms of the Novel Monosulfactam 0073.Antimicrobial agents and chemotherapy · 2020
    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 3 institutions in 2 countries.

Jong-Kook LeeResearch Center for Proteinaceous Materials (RCPM), Chosun University, Gwangju, Republic of Korea.
Chang Ho SeoDepartment of Bioinformatics, Kongju National University, Kongju, Republic of Korea.
Tudor LuchianDepartment of Physics, Alexandru I. Cuza University, Iasi, Romania.
Yoonkyung ParkResearch Center for Proteinaceous Materials (RCPM), Chosun University, Gwangju, Republic of Korea Department of Biotechnology and BK21-Plus Research Team for Bioactive Control Technology, Chosun University, Gwangju, Republic of Korea y_k_park@chosun.ac.kr.
Chosun University · KRAlexandru Ioan Cuza University · ROKongju National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CA-MA is a hybrid antimicrobial peptide (AMP) derived from two naturally occurring AMPs, cecropin A and magainin 2. CA-MA shows strong antimicrobial activity against Gram-negative and Gram-positive bacteria but also exhibits cytotoxicity toward mammalian cells. Our objective was to identify CA-MA analogues with reduced cytotoxicity by systematic replacement of amino acids with positively charged R groups (His and Lys), aliphatic R groups (Leu), or polar R groups (Glu). Among the CA-MA analogues studied (CMA1 to -6), CMA3 showed the strongest antimicrobial activity, including against drug-resistant Escherichia coli and Pseudomonas aeruginosa strains isolated from hospital patients. CMA3 appeared to act by inducing pore formation (toroidal model) in the bacterial membrane. In cytotoxicity assays, CMA3 showed little cytotoxicity toward human red blood cells (hRBCs) or HaCaT cells. Additionally, no fluorescence was released from small or giant unilamellar vesicles exposed to 60 μM CMA3 for 80 s, whereas fluorescence was released within 35 s upon exposure to CA-MA. CMA3 also exerted strong lipopolysaccharide (LPS)-neutralizing activity in RAW 264.7 cells, and BALB/c mice exposed to LPS after infection by Escherichia coli showed improved survival after administration of one 0.5-mg/kg of body weight or 1-mg/kg dose of CMA3. Finally, in a mouse model of septic shock, CMA3 reduced the levels of proinflammatory factors, including both nitric oxide and white blood cells, and correspondingly reduced lung tissue damage. This study suggests that CMA3 is an antimicrobial/antiendotoxin peptide that could serve as the basis for the development of anti-inflammatory and/or antimicrobial agents with low cytotoxicity.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsAnti-Bacterial AgentsAnti-Inflammatory Agents, Non-SteroidalAntimicrobial Cationic PeptidesCell LineCell MembraneErythrocytesEscherichia coliEscherichia coli InfectionsHumansKeratinocytesLipopolysaccharidesMacrophagesMagaininsAnti-Bacterial AgentsAnti-Inflammatory Agents, Non-SteroidalAntimicrobial Cationic Peptidescecropin ALipopolysaccharidesmagainin 2 peptide, XenopusMagaininsNitric OxideXenopus Proteins

Identifiers

PMID26552969
PMCPMC4704218
OpenAlexW2098670239

What OpenQuestion holds

Textmetadata
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.