Evidence map›Paper›PMID 15722429›Full record

ArticleBiophysical journal2005

Mechanism of membrane activity of the antibiotic trichogin GA IV: a two-state transition controlled by peptide concentration.

Claudia Mazzuca, Lorenzo Stella, Mariano Venanzi, Fernando Formaggio, Claudio Toniolo, Basilio Pispisa

Open access · greenAbstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 68 citations in OpenAlex.

  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. Azulene-A Bright Core for Sensing and Imaging.Molecules (Basel, Switzerland) · 2021
    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

6 authors at 3 institutions in 1 country.

Claudia MazzucaDipartimento di Scienze e Tecnologie Chimiche, Università di Roma Tor Vergata, 00133 Rome, Italy.
Lorenzo Stella
Mariano Venanzi
Fernando Formaggio
Claudio Toniolo
Basilio Pispisa
University of Rome Tor Vergata · ITIstituto di Chimica Biomolecolare · ITUniversity of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synthetic fluorescent analogs of the natural lipopeptide trichogin GA IV were used to investigate the peptide position and orientation in model membranes. A translocation assay based on Forster energy transfer indicates that trichogin is associated to both the outer and inner leaflet of the membrane, even at low concentration, when it is not active. Fluorescence quenching measurements, performed by using water soluble quenchers and quenchers positioned in the membrane at different depths, indicate that at low membrane-bound peptide/lipid ratios trichogin lies close to the region of polar headgroups. By increasing peptide concentration until membrane leakage takes place, a cooperative transition occurs and a significant fraction of the peptide becomes deeply buried into the bilayer. Remarkably, this change in peptide position is strictly coupled with peptide aggregation. Therefore, the mechanism of trichogin action can be envisaged as based on a two-state transition controlled by peptide concentration. One state is the monomeric, surface bound and inactive peptide, and the other state is a buried, aggregated form, which is responsible for membrane leakage and bioactivity.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesBiophysicsDose-Response Relationship, DrugGlycopeptidesLipid BilayersLipidsLipopeptidesLiposomesMacromolecular SubstancesMembranesModels, ChemicalPeptidesProtein TransportSpectrometry, FluorescenceSpectroscopy, Fourier Transform InfraredAnti-Bacterial AgentsAntimicrobial Cationic PeptidesGlycopeptidesLipid BilayersLipidsLipopeptidesLiposomesMacromolecular SubstancesPeptidestrichogin GA IVWater

Identifiers

PMID15722429
PMCPMC1305488
OpenAlexW2051643294

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.