Evidence map›Paper›PMID 33809374›Full record

ArticleBiomolecules2021

Beneficial Impacts of Incorporating the Non-Natural Amino Acid Azulenyl-Alanine into the Trp-Rich Antimicrobial Peptide buCATHL4B.

Areetha R D'Souza, Matthew R Necelis, Alona Kulesha, Gregory A Caputo, Olga V Makhlynets

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Frontiers in immunology · 2023
    Review
  15. Antimicrobial Peptides: From Design to Clinical Application.Antibiotics (Basel, Switzerland) · 2022
    Review
  16. Review
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.

Areetha R D'SouzaDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.
Matthew R NecelisDepartment of Chemistry & Biochemistry, Rowan University, Glassboro, NJ 08028, USA.
Alona KuleshaDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.ORCID 0000-0003-3844-1242
Gregory A CaputoDepartment of Chemistry & Biochemistry, Rowan University, Glassboro, NJ 08028, USA.ORCID 0000-0002-4510-2815
Olga V MakhlynetsDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.ORCID 0000-0002-2763-7891
Syracuse University · USRowan University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) present a promising scaffold for the development of potent antimicrobial agents. Substitution of tryptophan by non-natural amino acid Azulenyl-Alanine (AzAla) would allow studying the mechanism of action of AMPs by using unique properties of this amino acid, such as ability to be excited separately from tryptophan in a multi-Trp AMPs and environmental insensitivity. In this work, we investigate the effect of Trp→AzAla substitution in antimicrobial peptide buCATHL4B (contains three Trp side chains). We found that antimicrobial and bactericidal activity of the original peptide was preserved, while cytocompatibility with human cells and proteolytic stability was improved. We envision that AzAla will find applications as a tool for studies of the mechanism of action of AMPs. In addition, incorporation of this non-natural amino acid into AMP sequences could enhance their application properties.

Indexed as

3T3 CellsAnimalsAzulenesBacteriaCell Membrane PermeabilityCircular DichroismErythrocytesFibroblastsHemolysisMiceMicrobial Sensitivity TestsPeptide HydrolasesPore Forming Cytotoxic ProteinsSheepSpectrometry, FluorescenceTryptophanAzulenesPeptide HydrolasesPore Forming Cytotoxic ProteinsTryptophanantimicrobial peptidesbuCATHL4Bfluorescencelipid bindingmembrane permeabilizationnon-natural amino acidsprotease resistance

Identifiers

PMID33809374
PMCPMC8001250
OpenAlexW3137265166

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.