Evidence map›Paper›PMID 25182242›Full record

ArticleEuropean biophysics journal : EBJ2014

Lipid interactions of LAH4, a peptide with antimicrobial and nucleic acid transfection activities.

Barbara Perrone, Andrew J Miles, Evgeniy S Salnikov, B A Wallace, Burkhard Bechinger

Abstract read
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In one paragraph

Article in European biophysics journal : EBJ, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.0field-weighted citation impact, top 16% 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

13 citing papers in PubMed, 32 citations in OpenAlex.

  1. Polarized ATR-FTIR Spectroscopy Reveals Light-Induced Peptide Insertion of LAH4 Into Photoswitchable Membranes.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Article
  2. Article
  3. Article
  4. Peptide-Assisted Nucleic Acid Delivery Systems on the Rise.International journal of molecular sciences · 2021
    Review
  5. Article
  6. Review
  7. Article
  8. Activity and characterization of a pH-sensitive antimicrobial peptide.Biochimica et biophysica acta. Biomembranes · 2019
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. 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

5 authors at 4 institutions in 2 countries.

Barbara PerroneUMR7177, Institut de Chimie, Université de Strasbourg/CNRS, 1, rue Blaise Pascal, Strasbourg, 67070, France.
Andrew J Miles
Evgeniy S Salnikov
B A Wallace
Burkhard Bechinger
Université de Strasbourg · FRBirkbeck, University of London · GBCentre National de la Recherche Scientifique · FRInstitute of Structural and Molecular Biology · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H023852/1
6 · The paper itself

Abstract

The cationic amphipathic designer peptide LAH4 exhibits potent antimicrobial, nucleic acid transfection and cell penetration activities. Closely related derivatives have been developed to enhance viral transduction for gene therapeutic assays. LAH4 contains four histidines and, consequently, its overall charge and membrane topology in lipid bilayers are strongly pH dependent. In order to better understand the differential interactions of this amphipathic peptide with negatively-charged membranes its interactions, topologies, and penetration depth were investigated in the presence of lipid bilayers as a function of pH, buffer, phospholipid head group, and fatty acyl chain composition using a combination of oriented synchrotron radiation circular dichroism spectroscopy as well as oriented and non-oriented solid-state NMR spectroscopy. This combination of methods indicates that in the presence of lipids with phosphatidylglycerol head groups, the topological equilibria of LAH4 is shifted towards more in-plane configurations even at neutral pH. In contrast, a transmembrane alignment is promoted when LAH4 interacts with membranes made of dimyristoyl phospholipids rather than palmitoyl-oleoyl-phospholipids. Finally, the addition of citrate buffer favours LAH4 transmembrane alignments, even at low pH, probably by complex formation with the cationic charges of the peptide. In summary, this study has revealed that the membrane topology of this peptide is readily modulated by the environmental conditions.

Indexed as

Anti-Infective AgentsAntimicrobial Cationic PeptidesCell MembraneHydrogen-Ion ConcentrationLipid BilayersStatic ElectricityAnti-Infective AgentsAntimicrobial Cationic PeptidesLAH(4) protein, syntheticLipid Bilayers

Identifiers

PMID25182242
OpenAlexW2051046184

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.