Evidence map›Paper›PMID 17218466›Full record

ArticleBiophysical journal2007

Mechanism of the cell-penetrating peptide transportan 10 permeation of lipid bilayers.

Lindsay E Yandek, Antje Pokorny, Anders Florén, Kristina Knoelke, Ulo Langel, Paulo F F Almeida

Abstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing 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

76 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Computational Insights into Membrane Disruption by Cell-Penetrating Peptides.Journal of chemical information and modeling · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article

16 more citing papers are in PubMed but not listed here.

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.

Lindsay E YandekDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina 28403, USA.
Antje Pokorny
Anders Florén
Kristina Knoelke
Ulo Langel
Paulo F F Almeida

Funding

Mechanisms of amphipathic and cargo delivery peptidesR15GM072507 · NIGMS · UNIVERSITY OF NORTH CAROLINA WILMINGTON · PI ALMEIDA, PAULO F · 2005 to 2012
$758k
NIGMS NIH HHS GM072507NIGMS NIH HHS R15 GM072507
6 · The paper itself

Abstract

The mechanism of the interaction between the cell-penetrating peptide transportan 10 (tp10) and phospholipid membranes was investigated. Tp10 induces graded release of the contents of phospholipid vesicles. The kinetics of peptide association with vesicles and peptide-induced dye efflux from the vesicle lumen were examined experimentally by stopped-flow fluorescence. The experimental kinetics were analyzed by directly fitting to the data the numerical solution of mathematical kinetic models. A very good global fit was obtained using a model in which tp10 binds to the membrane surface and perturbs it because of the mass imbalance thus created across the bilayer. The perturbed bilayer state allows peptide monomers to insert transiently into its hydrophobic core and cross the membrane, until the peptide mass imbalance is dissipated. In that transient state tp10 "catalyzes" dye efflux from the vesicle lumen. These conclusions are consistent with recent reports that used molecular dynamics simulations to study the interactions between peptide antimicrobials and phospholipid bilayers. A thermodynamic analysis of tp10 binding and insertion in the bilayer using water-membrane transfer hydrophobicity scales is entirely consistent with the model proposed. A small bilayer perturbation is both necessary and sufficient to achieve very good agreement with the model, indicating that the role of the lipids must be included to understand the mechanism of cell-penetrating and antimicrobial peptides.

Indexed as

Models, ChemicalModels, MolecularProtein TransportComputer SimulationDiffusionGalaninLipid BilayersLiposomesMembrane FluidityPermeabilityPhospholipidsPorosityRecombinant Fusion ProteinsWasp VenomsGalaninLipid BilayersLiposomesPhospholipidsRecombinant Fusion ProteinstransportanWasp Venoms

Identifiers

PMID17218466
PMCPMC1864827

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.