Evidence map›Paper›PMID 20956602›Full record

ArticleAntimicrobial agents and chemotherapy2011

Structural features governing the activity of lactoferricin-derived peptides that act in synergy with antibiotics against Pseudomonas aeruginosa in vitro and in vivo.

Susana Sánchez-Gómez, Bostjan Japelj, Roman Jerala, Ignacio Moriyón, Mirian Fernández Alonso, José Leiva, Sylvie E Blondelle, Jörg Andrä, Klaus Brandenburg, Karl Lohner and 1 more

Open access · bronzeAbstract read
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Article in Antimicrobial agents and chemotherapy, 2011. 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
2.5field-weighted citation impact, top 12% 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, 54 citations in OpenAlex.

  1. Synergistic Action of Antimicrobial Peptides and Antibiotics.International journal of molecular sciences · 2026
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  12. Antimicrobial Activity of Protein Fraction fromMolecules (Basel, Switzerland) · 2020
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  18. Review
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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

11 authors at 6 institutions in 5 countries.

Susana Sánchez-GómezDepartment of Microbiology and Parasitology, University of Navarra, Pamplona, Spain.
Bostjan Japelj
Roman Jerala
Ignacio Moriyón
Mirian Fernández Alonso
José Leiva
Sylvie E Blondelle
Jörg Andrä
Klaus Brandenburg
Karl Lohner
Guillermo Martínez de Tejada
Universidad de Navarra · ESNational Institute of Chemistry · SIResearch Center Borstel - Leibniz Lung Center · DEAustrian Academy of Sciences · ATClinica Universidad de Navarra · ESTorrey Pines Institute For Molecular Studies · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pseudomonas aeruginosa is naturally resistant to many antibiotics, and infections caused by this organism are a serious threat, especially to hospitalized patients. The intrinsic low permeability of P. aeruginosa to antibiotics results from the coordinated action of several mechanisms, such as the presence of restrictive porins and the expression of multidrug efflux pump systems. Our goal was to develop antimicrobial peptides with an improved bacterial membrane-permeabilizing ability, so that they enhance the antibacterial activity of antibiotics. We carried out a structure activity relationship analysis to investigate the parameters that govern the permeabilizing activity of short (8- to 12-amino-acid) lactoferricin-derived peptides. We used a new class of constitutional and sequence-dependent descriptors called PEDES (peptide descriptors from sequence) that allowed us to predict (Spearman's ρ = 0.74; P < 0.001) the permeabilizing activity of a new peptide generation. To study if peptide-mediated permeabilization could neutralize antibiotic resistance mechanisms, the most potent peptides were combined with antibiotics, and the antimicrobial activities of the combinations were determined on P. aeruginosa strains whose mechanisms of resistance to those antibiotics had been previously characterized. A subinhibitory concentration of compound P2-15 or P2-27 sensitized P. aeruginosa to most classes of antibiotics tested and counteracted several mechanisms of antibiotic resistance, including loss of the OprD porin and overexpression of several multidrug efflux pump systems. Using a mouse model of lethal infection, we demonstrated that whereas P2-15 and erythromycin were unable to protect mice when administered separately, concomitant administration of the compounds afforded long-lasting protection to one-third of the animals.

Indexed as

AnimalsAnti-Bacterial AgentsDrug SynergismFemaleLactoferrinMiceMicrobial Sensitivity TestsPeptidesPseudomonas aeruginosaPseudomonas InfectionsAnti-Bacterial Agentslactoferricin BLactoferrinPeptides

Identifiers

PMID20956602
PMCPMC3019672
OpenAlexW2163561196

What OpenQuestion holds

Textmetadata
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.