Evidence map›Paper›PMID 31692278›Full record

ArticleChemMedChem2019

Proline-Rich Peptides with Improved Antimicrobial Activity against E. coli, K. pneumoniae, and A. baumannii.

Mario Mardirossian, Riccardo Sola, Bertrand Beckert, Dominic W P Collis, Adriana Di Stasi, Federica Armas, Kai Hilpert, Daniel N Wilson, Marco Scocchi

Abstract read
In one paragraph

Article in ChemMedChem, 2019. 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
–field-weighted citation impact
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.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Metabolic Comparison and Molecular Networking of Antimicrobials inInternational journal of molecular sciences · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Mechanisms of aPharmaceutics · 2023
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. The cyclic octapeptide antibiotic argyrin B inhibits translation by trapping EF-G on the ribosome during translocation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Article
  19. Review
  20. Effects of Lipidation on a Proline-Rich Antibacterial Peptide.International journal of molecular sciences · 2021
    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.

Mario MardirossianDepartment of Life Sciences, University of Trieste, 34128, Trieste, Italy.
Riccardo SolaDepartment of Life Sciences, University of Trieste, 34128, Trieste, Italy.
Bertrand BeckertInstitute for Biochemistry and Molecular Biology, University of Hamburg, 20146, Hamburg, Germany.
Dominic W P CollisTiKa Diagnostics Ltd, London, SW17 0RE, UK.
Adriana Di StasiDepartment of Life Sciences, University of Trieste, 34128, Trieste, Italy.
Federica ArmasDepartment of Life Sciences, University of Trieste, 34128, Trieste, Italy.
Kai HilpertSt Georges, University of London, London, SW17 0RE, UK.
Daniel N WilsonInstitute for Biochemistry and Molecular Biology, University of Hamburg, 20146, Hamburg, Germany.
Marco ScocchiDepartment of Life Sciences, University of Trieste, 34128, Trieste, Italy.ORCID 0000-0003-1247-3641

Funding

Deutsche Zentrum für Luft- und Raumfahrt DLR01Kl1820Institute of Infection and Immunity"Made in Trieste" by Area Science Park (Trieste)University of Trieste
6 · The paper itself

Abstract

Proline-rich antimicrobial peptides (PrAMPs) are promising agents to combat multi-drug resistant pathogens due to a high antimicrobial activity, yet low cytotoxicity. A library of derivatives of the PrAMP Bac5(1-17) was synthesized and screened to identify which residues are relevant for its activity. In this way, we discovered that two central motifs -PIRXP- cannot be modified, while residues at N- and C- termini tolerated some variations. We found five Bac5(1-17) derivatives bearing 1-5 substitutions, with an increased number of arginine and/or tryptophan residues, exhibiting improved antimicrobial activity and broader spectrum of activity while retaining low cytotoxicity toward eukaryotic cells. Transcription/translation and bacterial membrane permeabilization assays showed that these new derivatives still retained the ability to strongly inhibit bacterial protein synthesis, but also acquired permeabilizing activity to different degrees. These new Bac5(1-17) derivatives therefore show a dual mode of action which could hinder the selection of bacterial resistance against these molecules.

Indexed as

Acinetobacter baumanniiAnti-Bacterial AgentsCell Line, TumorCell ProliferationCell SurvivalDose-Response Relationship, DrugEscherichia coliHumansKlebsiella pneumoniaeMicrobial Sensitivity TestsMolecular StructurePeptidesProlineStructure-Activity RelationshipAnti-Bacterial AgentsPeptidesProlineAntibioticsmembrane permeabilizationproline-rich peptideprotein synthesis inhibitionsolid-phase synthesis

Identifiers

PMID31692278
PMCPMC6973051

What OpenQuestion holds

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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.