Evidence map›Paper›PMID 27529210›Full record

ArticleMolecules (Basel, Switzerland)2016

Influence of Cysteine and Tryptophan Substitution on DNA-Binding Activity on Maize α-Hairpinin Antimicrobial Peptide.

Daniel A Sousa, William F Porto, Maria Z Silva, Tatiane R da Silva, Octávio L Franco

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.8field-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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
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  6. Article
  7. Review
  8. Article
  9. Frontiers in microbiology · 2022
    Article
  10. Review
  11. Review
  12. Nigellothionins from Black Cumin (Antibiotics (Basel, Switzerland) · 2021
    Article
  13. Article
  14. Review
  15. Review
  16. Sarconesin II, a New Antimicrobial Peptide Isolated fromMolecules (Basel, Switzerland) · 2019
    Article
  17. 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

5 authors at 2 institutions in 1 country.

Daniel A SousaPrograma de Pós Graduação em Patologia Molecular, Universidade de Brasília, Brasília, DF 70910-900, Brazil. amarods@gmail.com.
William F PortoCentro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia, Universidade Católica de Brasília, Brasília, DF 70790-160, Brazil. Williamfp7@gmail.com.
Maria Z SilvaCentro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia, Universidade Católica de Brasília, Brasília, DF 70790-160, Brazil. marizaban@gmail.com.
Tatiane R da SilvaCentro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia, Universidade Católica de Brasília, Brasília, DF 70790-160, Brazil. tatyrodrigues8@gmail.com.
Octávio L FrancoPrograma de Pós Graduação em Patologia Molecular, Universidade de Brasília, Brasília, DF 70910-900, Brazil. ocfranco@pos.ucb.br.
Universidade Católica de Brasília · BRUniversidade de Brasília · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For almost four decades, antimicrobial peptides have been studied, and new classes are being discovered. However, for therapeutic use of these molecules, issues related to the mechanism of action must be answered. In this work, the antimicrobial activity of the hairpinin MBP-1 was studied by the synthesis of two variants, one replacing cysteines and one tryptophan with alanine. Antibacterial activity was abolished in both variants. No membrane disturbance, even in concentrations higher than those required to inhibit the bacteria, was observed in SEM microscopy. The gel retardation assay showed that MBP-1 possesses a higher DNA-binding ability than variants. Finally, molecular modelling showed that the lack of cysteines resulted in structure destabilization and lack of tryptophan resulted in a less flexible peptide, with less solvent assessable surface area, both characteristics that could contribute to absence of activity. In summary, the data here reported add more information about the multiple mechanisms of action of α-hairpinins.

Indexed as

Amino Acid SubstitutionAntimicrobial Cationic PeptidesCysteineDNAModels, MolecularMolecular ConformationStructure-Activity RelationshipTryptophanZea maysAntimicrobial Cationic PeptidesCysteineDNATryptophanantimicrobial peptidesDNA-bindingα-hairpinin

Identifiers

PMID27529210
PMCPMC6273665
OpenAlexW2517754321

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.