Evidence map›Paper›PMID 22908164›Full record

ArticleAntimicrobial agents and chemotherapy2012

Identification of peptides derived from the human antimicrobial peptide LL-37 active against biofilms formed by Pseudomonas aeruginosa using a library of truncated fragments.

C Nagant, B Pitts, K Nazmi, M Vandenbranden, J G Bolscher, P S Stewart, J-P Dehaye

Open access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

59 citing papers in PubMed, 113 citations in OpenAlex.

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  7. Anti-Biofilm Agents to OvercomePharmaceuticals (Basel, Switzerland) · 2025
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  16. Antibiofilm properties of cathelicidin LL-37: an in-depth review.World journal of microbiology & biotechnology · 2023
    Review
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  19. 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

7 authors at 4 institutions in 3 countries.

C NagantLaboratoire de Chimie biologique et médicale et de Microbiologie pharmaceutique, Faculté de Pharmacie, Université libre de Bruxelles, Brussels, Belgium. cnagant@ulb.ac.be
B Pitts
K Nazmi
M Vandenbranden
J G Bolscher
P S Stewart
J-P Dehaye
Université Libre de Bruxelles · BEMontana State University · USAcademic Center for Dentistry Amsterdam · NLUniversity of Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Persistent Pseudomonas aeruginosa infections are a major cause of morbidity and mortality in cystic fibrosis (CF) patients and are linked to the formation of a biofilm. The development of new biofilm inhibition strategies is thus a major challenge. LL-37 is the only human antimicrobial peptide derived from cathelicidin. The effects on the P. aeruginosa PAO1 strain of synthetic truncated fragments of this peptide were compared with the effects of the original peptide. Fragments of LL-37 composed of 19 residues (LL-19, LL13-31, and LL7-25) inhibited biofilm formation. The strongest antibiofilm activity was observed with the peptides LL7-37 and LL-31, which decreased the percentage of biomass formation at a very low concentration. Some peptides were also active on the bacteria within an established biofilm. LL7-31, LL-31, and LL7-37 increased the uptake of propidium iodide (PI) by sessile bacteria. The peptide LL7-37 decreased the height of the biofilm and partly disrupted it. The peptides active within the biofilm had an infrared spectrum compatible with an α-helix. LL-37, but not the peptides LL7-31 and LL7-37, showed cellular toxicity by permeabilizing the eukaryotic plasma membrane (uptake of ethidium bromide and release of lactate dehydrogenase [LDH]). None of the tested peptides affected mitochondrial activity in eukaryotic cells. In conclusion, a 25-amino-acid peptide (LL7-31) displayed both strong antimicrobial and antibiofilm activities. The peptide was even active on cells within a preformed biofilm and had reduced toxicity toward eukaryotic cells. Our results also suggest the contribution of secondary structures (α-helix) to the activity of the peptides on biofilms.

Indexed as

Amino Acid SequenceAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBiofilmsCathelicidinsCell MembraneCell Membrane PermeabilityCell SurvivalHumansHuman Umbilical Vein Endothelial CellsL-Lactate DehydrogenaseMicrobial ViabilityMolecular Sequence DataPeptide FragmentsPeptide LibraryPropidiumAnti-Bacterial AgentsAntimicrobial Cationic PeptidesCathelicidinsL-Lactate DehydrogenasePeptide FragmentsPeptide LibraryPropidium

Identifiers

PMID22908164
PMCPMC3486595
OpenAlexW2086368575

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.