Evidence map›Paper›PMID 18835902›Full record

ArticleBiophysical journal2008

Membrane thickening by the antimicrobial peptide PGLa.

Georg Pabst, Stephan L Grage, Sabine Danner-Pongratz, Weiguo Jing, Anne S Ulrich, Anthony Watts, Karl Lohner, Andrea Hickel

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

24 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
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  11. Effects of artepillin C on model membranes displaying liquid immiscibility.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2019
    Article
  12. Review
  13. Article
  14. Interaction of Artepillin C with model membranes.European biophysics journal : EBJ · 2017
    Article
  15. Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Article
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  20. Review
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 3 institutions in 3 countries.

Georg PabstInstitute of Biophysics and Nanosystems Research, Austrian Academy of Sciences, Graz, Austria.
Stephan L Grage
Sabine Danner-Pongratz
Weiguo Jing
Anne S Ulrich
Anthony Watts
Karl Lohner
Andrea Hickel
Austrian Academy of Sciences · ATKarlsruhe Institute of Technology · DEUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

Using x-ray diffraction, solid-state 2H-NMR, differential scanning calorimetry, and dilatometry, we have observed a perturbation of saturated acyl chain phosphatidylglycerol bilayers by the antimicrobial peptide peptidyl-glycylleucine-carboxyamide (PGLa) that is dependent on the length of the hydrocarbon chain. In the gel phase, PGLa induces a quasi-interdigitated phase, previously reported also for other peptides, which is most pronounced for C18 phosphatidylglycerol. In the fluid phase, we found an increase of the membrane thickness and NMR order parameter for C14 and C16 phosphatidylglycerol bilayers, though not for C18. The data is best understood in terms of a close hydrophobic match between the C18 bilayer core and the peptide length when PGLa is inserted with its helical axis normal to the bilayer surface. The C16 acyl chains appear to stretch to accommodate PGLa, whereas tilting within the bilayer seems to be energetically favorable for the peptide when inserted into bilayers of C14 phosphatidylglycerol. In contrast to the commonly accepted membrane thinning effect of antimicrobial peptides, the data demonstrate that pore formation does not necessarily relate to changes in the overall bilayer structure.

Indexed as

Antimicrobial Cationic PeptidesCalorimetry, Differential ScanningCell MembraneHot TemperatureLipid BilayersMagnetic Resonance SpectroscopyPhosphatidylglycerolsScattering, Small AngleTemperatureThermodynamicsX-Ray Diffraction1,2-dipalmitoylphosphatidylglycerolAntimicrobial Cationic Peptidesdistearoyl phosphatidylglycerolLipid Bilayerspeptide-Gly-Leu-amidePhosphatidylglycerols

Identifiers

PMID18835902
PMCPMC2599817
OpenAlexW2104039224

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.