Evidence map›Paper›PMID 28761101›Full record

ArticleScientific reports2017

A short D-enantiomeric antimicrobial peptide with potent immunomodulatory and antibiofilm activity against multidrug-resistant Pseudomonas aeruginosa and Acinetobacter baumannii.

Mohamed F Mohamed, Anna Brezden, Haroon Mohammad, Jean Chmielewski, Mohamed N Seleem

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing 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

53 citing papers in PubMed.

  1. Article
  2. Nanosystems for delivery of indolicidin peptide.Frontiers in medical technology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Advances of Antimicrobial Peptides in the Treatment of Multidrug-Resistant Bacteria.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Going Beyond Host Defence Peptides: Horizons of Chemically Engineered Peptides for Multidrug-Resistant Bacteria.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023
    Review
  19. Review
  20. FightingInternational journal of molecular sciences · 2023
    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.

Mohamed F MohamedDepartment of Comparative Pathobiology, Purdue University, West Lafayette, IN, 47907, USA.
Anna BrezdenDepartment of Chemistry, Purdue University, West Lafayette, IN, 47907, USA.
Haroon MohammadDepartment of Comparative Pathobiology, Purdue University, West Lafayette, IN, 47907, USA.
Jean ChmielewskiDepartment of Chemistry, Purdue University, West Lafayette, IN, 47907, USA.
Mohamed N SeleemDepartment of Comparative Pathobiology, Purdue University, West Lafayette, IN, 47907, USA. mseleem@purdue.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) represent a promising therapeutic alternative for the treatment of antibiotic-resistant bacterial infections. The present study investigates the antimicrobial activity of new, rationally-designed derivatives of a short α-helical peptide, RR. From the peptides designed, RR4 and its D-enantiomer, D-RR4, emerged as the most potent analogues with a more than 32-fold improvement in antimicrobial activity observed against multidrug-resistant strains of Pseudomonas aeruginosa and Acinetobacter baumannii. Remarkably, D-RR4 demonstrated potent activity against colistin-resistant strains of P. aeruginosa (isolated from cystic fibrosis patients) indicating a potential therapeutic advantage of this peptide over several AMPs. In contrast to many natural AMPs, D-RR4 retained its activity under challenging physiological conditions (high salts, serum, and acidic pH). Furthermore, D-RR4 was more capable of disrupting P. aeruginosa and A. baumannii biofilms when compared to conventional antibiotics. Of note, D-RR4 was able to bind to lipopolysaccharide to reduce the endotoxin-induced proinflammatory cytokine response in macrophages. Finally, D-RR4 protected Caenorhabditis elegans from lethal infections of P. aeruginosa and A. baumannii and enhanced the activity of colistin in vivo against colistin-resistant P. aeruginosa.

Indexed as

Acinetobacter baumanniiAnimalsAntimicrobial Cationic PeptidesBiofilmsCaenorhabditis elegansColistinCystic FibrosisDrug DesignDrug Resistance, Multiple, BacterialDrug StabilityHumansMicrobial Sensitivity TestsPseudomonas aeruginosaPseudomonas InfectionsAntimicrobial Cationic PeptidesColistin

Identifiers

PMID28761101
PMCPMC5537347

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.