Evidence map›Paper›PMID 31505894›Full record

ArticleInternational journal of molecular sciences2019

Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide.

Marie-Lise Jobin, Lydie Vamparys, Romain Deniau, Axelle Grélard, Cameron D Mackereth, Patrick F J Fuchs, Isabel D Alves

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Article
  2. Review
  3. Synthetic Lipid Biology.Chemical reviews · 2025
    Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. 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.

Marie-Lise JobinInstitute of Chemistry & Biology of Membranes & Nanoobjects (CBMN), CNRS UMR5248, University of Bordeaux, Bordeaux INP, allée Geoffroy St-Hilaire, 33600 Pessac, France. marie-lise.jobin@u-bordeaux.fr.
Lydie VamparysUniversity of Paris, Institut Jacques Monod, CNRS, 75013 Paris, France.
Romain DeniauUniversity of Paris, Institut Jacques Monod, CNRS, 75013 Paris, France.
Axelle GrélardInstitute of Chemistry & Biology of Membranes & Nanoobjects (CBMN), CNRS UMR5248, University of Bordeaux, Bordeaux INP, allée Geoffroy St-Hilaire, 33600 Pessac, France.ORCID 0000-0002-6708-2253
Cameron D MackerethINSERM U1212, CNRS UMR5320, ARNA Laboratory, University of Bordeaux, IECB, 2 rue Robert Escarpit, 33600 Pessac, France.ORCID 0000-0002-0776-7947
Patrick F J FuchsSorbonne University, École normale supérieure, PSL University, CNRS, Laboratoire des biomolécules (LBM), 75005 Paris, France.
Isabel D AlvesInstitute of Chemistry & Biology of Membranes & Nanoobjects (CBMN), CNRS UMR5248, University of Bordeaux, Bordeaux INP, allée Geoffroy St-Hilaire, 33600 Pessac, France. i.alves@cbmn.u-bordeaux.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell-penetrating peptides (CPPs) are short peptides that can translocate and transport cargoes into the intracellular milieu by crossing biological membranes. The mode of interaction and internalization of cell-penetrating peptides has long been controversial. While their interaction with anionic membranes is quite well understood, the insertion and behavior of CPPs in zwitterionic membranes, a major lipid component of eukaryotic cell membranes, is poorly studied. Herein, we investigated the membrane insertion of RW16 into zwitterionic membranes, a versatile CPP that also presents antibacterial and antitumor activities. Using complementary approaches, including NMR spectroscopy, fluorescence spectroscopy, circular dichroism, and molecular dynamic simulations, we determined the high-resolution structure of RW16 and measured its membrane insertion and orientation properties into zwitterionic membranes. Altogether, these results contribute to explaining the versatile properties of this peptide toward zwitterionic lipids.

Indexed as

ArginineCell MembraneCell-Penetrating PeptidesCircular DichroismMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularProtein Structure, SecondaryArginineCell-Penetrating Peptidescell-penetrating peptidelipid model systemsmembrane biophysicsmolecular dynamicsNMRpeptide–lipid interaction

Identifiers

PMID31505894
PMCPMC6769507

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.