Evidence map›Paper›PMID 17299584›Full record

ArticlePloS one2007

Non-metabolic membrane tubulation and permeability induced by bioactive peptides.

Antonin Lamazière, Fabienne Burlina, Claude Wolf, Gérard Chassaing, Germain Trugnan, Jesus Ayala-Sanmartin

Open access · goldAbstract readComparative Study
In one paragraph

Article in PloS one, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

33 citing papers in PubMed, 90 citations in OpenAlex.

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  9. In Vitro Assays: Friends or Foes of Cell-Penetrating Peptides.International journal of molecular sciences · 2020
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  15. Arginine-rich cell-penetrating peptides induce membrane multilamellarity and subsequently enter via formation of a fusion pore.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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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 3 institutions in 1 country.

Antonin LamazièreInstitut National de la Santé et de la Recherche Médicale (INSERM), UMR 538, CHU Saint Antoine, Paris, France.
Fabienne Burlina
Claude Wolf
Gérard Chassaing
Germain Trugnan
Jesus Ayala-Sanmartin
Sorbonne Université · FRCentre National de la Recherche Scientifique · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundBasic cell-penetrating peptides are potential vectors for therapeutic molecules and display antimicrobial activity. The peptide-membrane contact is the first step of the sequential processes leading to peptide internalization and cell activity. However, the molecular mechanisms involved in peptide-membrane interaction are not well understood and are frequently controversial. Herein, we compared the membrane activities of six basic peptides with different size, charge density and amphipaticity: Two cell-penetrating peptides (penetratin and R9), three amphipathic peptides and the neuromodulator substance P. METHODOLOGY/PRINCIPAL

findingsExperiments of X ray diffraction, video-microscopy of giant vesicles, fluorescence spectroscopy, turbidimetry and calcein leakage from large vesicles are reported. Permeability and toxicity experiments were performed on cultured cells. The peptides showed differences in bilayer thickness perturbations, vesicles aggregation and local bending properties which form lipidic tubular structures. These structures invade the vesicle lumen in the absence of exogenous energy. CONCLUSIONS/SIGNIFICANCE: We showed that the degree of membrane permeabilization with amphipathic peptides is dependent on both peptide size and hydrophobic nature of the residues. We propose a model for peptide-induced membrane perturbations that explains the differences in peptide membrane activities and suggests the existence of a facilitated "physical endocytosis," which represents a new pathway for peptide cellular internalization.

Indexed as

Amino Acid SequenceAnimalsAnnexin A2Carrier ProteinsCell-Penetrating PeptidesCHO CellsCricetinaeCricetulusDrug CarriersDrug Evaluation, PreclinicalGreen Fluorescent ProteinsHydrophobic and Hydrophilic InteractionsLipid BilayersMembrane FusionMembrane LipidsModels, BiologicalAnnexin A2Carrier ProteinsCell-Penetrating PeptidesDrug CarriersGreen Fluorescent ProteinsLipid BilayersMembrane LipidspenetratinPeptidespolyarginineSubstance P

Identifiers

PMID17299584
PMCPMC1790702
OpenAlexW2009326620

What OpenQuestion holds

Textmetadata
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.