Evidence map›Paper›PMID 29265636›Full record

ArticleChemMedChem2018

Co-administration of Antimicrobial Peptides Enhances Toll-like Receptor 4 Antagonist Activity of a Synthetic Glycolipid.

Fabio A Facchini, Helena Coelho, Stefania E Sestito, Sandra Delgado, Alberto Minotti, David Andreu, Jesús Jiménez-Barbero, Francesco Peri

Open access · hybridAbstract read
In one paragraph

Article in ChemMedChem, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

6 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Review
  3. Antimicrobial peptides could antagonize uncontrolled inflammationFrontiers in bioengineering and biotechnology · 2022
    Review
  4. Review
  5. Article
  6. 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

8 authors at 5 institutions in 3 countries.

Fabio A FacchiniDepartment of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza, 2, 20126, Milano, Italy.
Helena CoelhoMolecular Recognition & Host-Pathogen Interactions Programme, CIC bioGUNE, Bizkaia Technology Park, Building 801A, 48170, Derio, Spain.
Stefania E SestitoDepartment of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza, 2, 20126, Milano, Italy.
Sandra DelgadoMolecular Recognition & Host-Pathogen Interactions Programme, CIC bioGUNE, Bizkaia Technology Park, Building 801A, 48170, Derio, Spain.
Alberto MinottiDepartment of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza, 2, 20126, Milano, Italy.
David AndreuDepartment of Experimental and Health Sciences, Pompeu Fabra University, Barcelona Biomedical Research Park, Dr. Aiguader 88, 08003, Barcelona, Spain.
Jesús Jiménez-BarberoMolecular Recognition & Host-Pathogen Interactions Programme, CIC bioGUNE, Bizkaia Technology Park, Building 801A, 48170, Derio, Spain.
Francesco PeriDepartment of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza, 2, 20126, Milano, Italy.ORCID 0000-0002-3417-8224
University of Milano-Bicocca · ITCIC bioGUNE · ESIkerbasque · ESUniversitat Pompeu Fabra · ESUniversity of the Basque Country · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study examines the effect of co-administration of antimicrobial peptides and the synthetic glycolipid FP7, which is active in inhibiting inflammatory cytokine production caused by TLR4 activation and signaling. The co-administration of two lipopolysaccharide (LPS)-neutralizing peptides (a cecropin A-melittin hybrid peptide and a human cathelicidin) enhances by an order of magnitude the potency of FP7 in blocking the TLR4 signal. Interestingly, this is not an additional effect of LPS neutralization by peptides, because it also occurs if cells are stimulated by the plant lectin phytohemagglutinin, a non-LPS TLR4 agonist. Our data suggest a dual mechanism of action for the peptides, not exclusively based on LPS binding and neutralization, but also on a direct effect on the LPS-binding proteins of the TLR4 receptor complex. NMR experiments in solution show that peptide addition changes the aggregation state of FP7, promoting the formation of larger micelles. These results suggest a relationship between the aggregation state of lipid A-like ligands and the type and intensity of the TLR4 response.

Indexed as

Acute-Phase ProteinsAntimicrobial Cationic PeptidesCarrier ProteinsCathelicidinsCell LineCell SurvivalGlycolipidsHumansLigandsLipopolysaccharide-Binding ProteinMelittenMembrane GlycoproteinsProtein BindingProtein ConformationToll-Like Receptor 4Acute-Phase ProteinsAntimicrobial Cationic PeptidesCarrier ProteinsCathelicidinscecropin AGlycolipidsLigandsLipopolysaccharide-Binding ProteinMelittenMembrane GlycoproteinsTLR4 protein, humanToll-Like Receptor 4aggregationantimicrobial peptidesFP7small-molecule antagoniststoll-like receptor 4

Identifiers

PMID29265636
PMCPMC5900894
OpenAlexW2776636298

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.