Evidence map›Paper›PMID 32576874›Full record

ArticleScientific reports2020

Bee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties.

Su Jin Ko, Eunji Park, Alina Asandei, Jee-Young Choi, Seung-Chul Lee, Chang Ho Seo, Tudor Luchian, Yoonkyung Park

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

30 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. ScymicrosinFrontiers in microbiology · 2025
    Article
  7. Review
  8. Hundreds of antimicrobial peptides create a selective barrier for insect gut symbionts.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Diversity of Antimicrobial Peptides in Silkworm.Life (Basel, Switzerland) · 2023
    Review
  17. Antimicrobial Activity ofAntibiotics (Basel, Switzerland) · 2023
    Article
  18. Unraveling the Role of Antimicrobial Peptides in Insects.International journal of molecular sciences · 2023
    Review
  19. Pharmacological properties and therapeutic potential of honey bee venom.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2023
    Review
  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

8 authors at 4 institutions in 2 countries.

Su Jin KoDepartment of Biomedical Science, Chosun University, Gwangju, 61452, South Korea.
Eunji ParkDepartment of Biomedical Science, Chosun University, Gwangju, 61452, South Korea.
Alina AsandeiInterdisciplinary Research Institute, Sciences Department, Alexandru I. Cuza University, Iasi, 700506, Romania.
Jee-Young ChoiChonnam National University Hospital, Gwangju, Korea.
Seung-Chul LeeDepartments of Dermatology, Chonnam National University Medical School, Gwnagju, Korea.
Chang Ho SeoDepartment of Bioinformatics, Kongju National University, Kongju, 32588, Republic of Korea.
Tudor LuchianDepartment of Physics, Alexandru I. Cuza University, Iasi, Romania. luchian@uaic.ro.ORCID http://orcid.org/0000-0002-9388-7266
Yoonkyung ParkDepartment of Biomedical Science, Chosun University, Gwangju, 61452, South Korea. y_k_park@chosun.ac.kr.ORCID http://orcid.org/0000-0002-8717-3080
Chosun University · KRAlexandru Ioan Cuza University · ROChonnam National University Hospital · KRKongju National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial peptides have attracted attention as alternatives to conventional antibiotics. Previously, a novel antimicrobial peptide, melectin, consisting of 18 amino acids was isolated from the venom of a bee, Melecta albifrons. Here, we investigated the antibacterial activity of melectin against drug-resistant bacteria. Melectin showed broad-spectrum antimicrobial activity but low cytotoxicity and no hemolytic activity. Melectin maintained its antimicrobial activity at physiological salt concentrations. Melectin is an α-helical structure that binds to the bacterial membrane via electrostatic interactions and kills bacteria in a short time by bacterial membrane targeting. Collectively, our results suggest that melectin has antibacterial activity and anti-inflammatory activity.

Indexed as

Anti-Bacterial AgentsAmino AcidsAnti-Inflammatory AgentsAntimicrobial Cationic PeptidesBacteriaBacterial Physiological PhenomenaBee VenomsCell MembraneCells, CulturedDrug Resistance, BacterialFibroblastsHumansProtein BindingProtein Conformation, alpha-HelicalSalt ToleranceSodium ChlorideAmino AcidsAnti-Bacterial AgentsAnti-Inflammatory AgentsAntimicrobial Cationic PeptidesBee VenomsmelectinSodium Chloride

Identifiers

PMID32576874
PMCPMC7311438
OpenAlexW3036773763

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.