Evidence map›Paper›PMID 37909050›Full record

ArticleCell reports methods2023

B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles.

Mirko Sadi, Nicolas Carvalho, Corentin Léger, Bruno Vitorge, Daniel Ladant, J Iñaki Guijarro, Alexandre Chenal

Abstract read
In one paragraph

Article in Cell reports methods, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Covalently Linked Peptides and Membrane Potential Enable CyaA Segment Translocation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Article
  4. CyaA translocation across eukaryotic cell membranes.Frontiers in molecular biosciences · 2024
    Article
  5. 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

7 authors.

Mirko SadiInstitut Pasteur, Université de Paris Cité, CNRS UMR3528, Biochemistry of Macromolecular Interactions Unit, 75015 Paris, France; Université de Paris Cité, 75005 Paris, France.
Nicolas CarvalhoInstitut Pasteur, Université de Paris Cité, CNRS UMR3528, Biochemistry of Macromolecular Interactions Unit, 75015 Paris, France; Université de Paris Cité, 75005 Paris, France.
Corentin LégerInstitut Pasteur, Université de Paris Cité, CNRS UMR3528, Biochemistry of Macromolecular Interactions Unit, 75015 Paris, France.
Bruno VitorgeInstitut Pasteur, Université de Paris Cité, CNRS UMR3528, Biological NMR and HDX-MS Technological Platform, 75015 Paris, France.
Daniel LadantInstitut Pasteur, Université de Paris Cité, CNRS UMR3528, Biochemistry of Macromolecular Interactions Unit, 75015 Paris, France.
J Iñaki GuijarroInstitut Pasteur, Université de Paris Cité, CNRS UMR3528, Biological NMR and HDX-MS Technological Platform, 75015 Paris, France. Electronic address: inaki.guijarro@pasteur.fr.
Alexandre ChenalInstitut Pasteur, Université de Paris Cité, CNRS UMR3528, Biochemistry of Macromolecular Interactions Unit, 75015 Paris, France. Electronic address: alexandre.chenal@pasteur.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amphitropic proteins and peptides reversibly partition from solution to membrane, a key process that regulates their functions. Experimental approaches classically used to measure protein partitioning into lipid bilayers, such as fluorescence and circular dichroism, are hardly usable when the peptides or proteins do not exhibit significant polarity and/or conformational changes upon membrane binding. Here, we describe binding to lipid vesicles (B2LiVe), a simple, robust, and widely applicable nuclear magnetic resonance (NMR) method to determine the solution-to-membrane partitioning of unlabeled proteins or peptides. B2LiVe relies on previously described proton 1D-NMR fast-pulsing techniques. Membrane partitioning induces a large line broadening, leading to a loss of protein signals; therefore, the decrease of the NMR signal directly measures the fraction of membrane-bound protein. The method uses low polypeptide concentrations and has been validated on several membrane-interacting polypeptides, ranging from 3 to 54 kDa, with membrane vesicles of different sizes and various lipid compositions.

Indexed as

Lipid BilayersPeptidesMagnetic Resonance ImagingMagnetic Resonance SpectroscopyMembrane ProteinsLipid BilayersMembrane ProteinsPeptidesaffinityamphitropic proteinsCP: Cell biologyCP: Molecular biologynuclear magnetic resonancepartition coefficientpeptidesprotein membrane bindingproton 1D-NMR fast-pulsing techniquesselective adiabatic pulsessolution to membrane partitioning

Identifiers

PMID37909050
PMCPMC10694493

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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.