Evidence map›Paper›PMID 24156610›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2013

Interaction between a cationic surfactant-like peptide and lipid vesicles and its relationship to antimicrobial activity.

Ashkan Dehsorkhi, Valeria Castelletto, Ian W Hamley, Jani Seitsonen, Janne Ruokolainen

Open access · hybridAbstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

16 citing papers in PubMed, 63 citations in OpenAlex.

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  16. Self-assembling amphiphilic peptides.Journal of peptide science : an official publication of the European Peptide Society · 2014
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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

5 authors at 2 institutions in 2 countries.

Ashkan DehsorkhiSchool of Chemistry, Pharmacy and Food Biosciences, University of Reading , Whiteknights, Reading, RG6 6AD, United Kingdom.
Valeria Castelletto
Ian W Hamley
Jani Seitsonen
Janne Ruokolainen
Aalto University · FIUniversity of Reading · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We investigate the properties of an antimicrobial surfactant-like peptide (Ala)6(Arg), A6R, containing a cationic headgroup. The interaction of this peptide with zwitterionic (DPPC) lipid vesicles is investigated using a range of microscopic, X-ray scattering, spectroscopic, and calorimetric methods. The β-sheet structure adopted by A6R is disrupted in the presence of DPPC. A strong effect on the small-angle X-ray scattering profile is observed: the Bragg peaks from the DPPC bilayers in the vesicle walls are eliminated in the presence of A6R and only bilayer form factor peaks are observed. All of these observations point to the interaction of A6R with DPPC bilayers. These studies provide insight into interactions between a model cationic peptide and vesicles, relevant to understanding the action of antimicrobial peptides on lipid membranes. Notably, peptide A6R exhibits antimicrobial activity without membrane lysis.

Indexed as

1,2-DipalmitoylphosphatidylcholineAmino Acid SequenceAnti-Infective AgentsEscherichia coli O157OligopeptidesStaphylococcus aureusSurface-Active Agents1,2-DipalmitoylphosphatidylcholineAnti-Infective AgentsOligopeptidesSurface-Active Agents

Identifiers

PMID24156610
PMCPMC3836358
OpenAlexW2166677675

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.