Evidence map›Paper›PMID 30760803›Full record

ArticleScientific reports2019

The cyclic peptide labaditin does not alter the outer membrane integrity of Salmonella enterica serovar Typhimurium.

Simone C Barbosa, Thatyane M Nobre, Diogo Volpati, Eduardo M Cilli, Daniel S Correa, Osvaldo N Oliveira

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

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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

6 authors at 4 institutions in 4 countries.

Simone C BarbosaSão Carlos Institute of Physics, University of São Paulo, CP 369, 13560-970, São Carlos-SP, Brazil.
Thatyane M NobreSão Carlos Institute of Physics, University of São Paulo, CP 369, 13560-970, São Carlos-SP, Brazil.
Diogo VolpatiSol Voltaics AB, 223 63, Lund, Sweden.
Eduardo M CilliUniversidade Estadual Paulista (UNESP), Institute of Chemistry, 14800-060, Araraquara-SP, Brazil.
Daniel S CorreaNanotechnology National Laboratory for Agriculture (LNNA), Embrapa Instrumentação, 13560-970, São Carlos, SP, Brazil.ORCID 0000-0002-5592-0627
Osvaldo N OliveiraSão Carlos Institute of Physics, University of São Paulo, CP 369, 13560-970, São Carlos-SP, Brazil. chu@ifsc.usp.br.
Universidade de São Paulo · BRBrazilian Agricultural Research Corporation · BRSol Voltaics (Sweden) · SEUniversidade Estadual Paulista (Unesp) · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial peptides are a promising class of new antibiotics with the ability to kill bacteria by disrupting their cell membrane, which is especially difficult for Gram-negative bacteria whose cell wall contains an outer layer of lipopolysaccharides (LPS). Here we show that the cyclic decapeptide Labaditin (Lo), with proven activity against the Gram-positive Staphylococcus aureus and Streptococcus mutans, is not able to kill the Gram-negative Salmonella enterica serovar Typhimurium (S.e.s. Typhimurium). We found that Lo induced significant changes in the surface pressure isotherms of Langmuir monolayers representing the Salmonella enterica serovar Typhimurium inner membrane (S.e.s. Typhimurium IM), and caused leakage in large unilamellar vesicles made with this IM lipid composition. On the basis of these results one should expect bactericidal activity against S.e.s. Typhimurium. However, Lo could not interact with a monolayer of LPS, causing no significant changes in either the surface pressure isotherms or in the polarization-modulated infrared reflection absorption spectra (PM-IRRAS). Therefore, the failure of Lo to kill S.e.s. Typhimurium is associated with the lack of interaction with LPS from the outer bacteria membrane. Our approach with distinct monolayer compositions and combined techniques to investigate molecular-level interactions is useful for drug design to fight antibiotic-resistant bacteria.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesBacterial Outer MembraneBacterial Outer Membrane ProteinsDrug DesignDrug Resistance, BacterialLipopolysaccharidesMicrobial Sensitivity TestsPeptides, CyclicSalmonella typhimuriumAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBacterial Outer Membrane ProteinslabaditinLipopolysaccharidesPeptides, Cyclic

Identifiers

PMID30760803
PMCPMC6374527
OpenAlexW2914899868

What OpenQuestion holds

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LicenceCC BY
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.