Evidence map›Paper›PMID 14747329›Full record

ArticleBiophysical journal2004

Aggregation and water-membrane partition as major determinants of the activity of the antibiotic peptide trichogin GA IV.

Lorenzo Stella, Claudia Mazzuca, Mariano Venanzi, Antonio Palleschi, Mara Didonè, Fernando Formaggio, Claudio Toniolo, Basilio Pispisa

Abstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Membrane Topology and Oligomerization of Peptaibols by Solid-State NMR Spectroscopy.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Review
  2. Article
  3. C-Terminal Nucleobase Modification Amplifies Peptide-Mediated Liposome Fusion.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. 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

8 authors.

Lorenzo StellaDipartimento di Scienze e Tecnologie Chimiche, Università di Roma Tor Vergata, 00133 Rome, Italy.
Claudia Mazzuca
Mariano Venanzi
Antonio Palleschi
Mara Didonè
Fernando Formaggio
Claudio Toniolo
Basilio Pispisa

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Water-membrane partition and aggregation behavior are fundamental aspects of the biological activity of antibiotic peptides, natural compounds causing the death of pathogenic organisms by perturbing the permeability of their membranes. A synthetic fluorescent analog of the natural lipopeptaibol trichogin GA IV was used to study its interaction with model membranes. Time-resolved fluorescence data show that in water, an equilibrium between monomers and small aggregates is present, the two species having different affinity for membranes. Therefore, association curves are strongly dependent on peptide concentration. A similar heterogeneity is present in the membrane phase, which strongly suggests the occurrence of a monomer-aggregate equilibrium in this case, too. The relative population of each species was determined and a strong correlation between the concentration of membrane-bound aggregates and membrane leakage was found, thereby suggesting that liposome perturbation is due to peptide aggregates only. Light-scattering measurements demonstrate that leakage is not due to liposome micellization. Moreover, experiments with markers of different sizes show that molecules with a diameter of approximately 4 nm are released only to a minor extent. Overall, these results suggest that, within the concentration range explored, pore formation by peptide aggregates is the most likely mechanism of action for trichogin in membranes.

Indexed as

Anti-Bacterial AgentsMembrane FluidityAntimicrobial Cationic PeptidesDimerizationGlycopeptidesLipopeptidesLiposomesMacromolecular SubstancesMembrane LipidsMembrane ProteinsMembranes, ArtificialMolecular ConformationPeptidesPermeabilityPorosityProtein BindingAnti-Bacterial AgentsAntimicrobial Cationic PeptidesGlycopeptidesLipopeptidesLiposomesMacromolecular SubstancesMembrane LipidsMembrane ProteinsMembranes, ArtificialPeptidestrichogin GA IVWater

Identifiers

PMID14747329
PMCPMC1303941

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.