Evidence map›Paper›PMID 27835700›Full record

ArticlePloS one2016

Membrane Assembly and Ion Transport Ability of a Fluorinated Nanopore.

Raphaël Godbout, Sébastien Légaré, Maud Auger, Claudia Carpentier, François Otis, Michèle Auger, Patrick Lagüe, Normand Voyer

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Fluorinated peptide biomaterials.Peptide science (Hoboken, N.J.) · 2021
    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.

Raphaël GodboutDépartement de chimie, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Université Laval, Québec, Québec, Canada.
Sébastien LégaréDépartement de biochimie, microbiologie et bio-informatique, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Université Laval, Québec, Québec, Canada.
Maud AugerDépartement de chimie, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA), Centre québécois sur les matériaux fonctionnels (CQMF), Université Laval, Québec, Québec, Canada.
Claudia CarpentierDépartement de chimie, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Université Laval, Québec, Québec, Canada.
François OtisDépartement de chimie, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Université Laval, Québec, Québec, Canada.
Michèle AugerDépartement de chimie, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA), Centre québécois sur les matériaux fonctionnels (CQMF), Université Laval, Québec, Québec, Canada.
Patrick LagüeDépartement de biochimie, microbiologie et bio-informatique, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Université Laval, Québec, Québec, Canada.
Normand VoyerDépartement de chimie, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Université Laval, Québec, Québec, Canada.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A novel 21-residue peptide incorporating six fluorinated amino acids was prepared. It was designed to fold into an amphiphilic alpha helical structure of nanoscale length with one hydrophobic face and one fluorinated face. The formation of a fluorous interface serves as the main vector for the formation of a superstructure in a bilayer membrane. Fluorescence assays showed this ion channel's ability to facilitate the translocation of alkali metal ions through a phospholipid membrane, with selectivity for sodium ions. Computational studies showed that a tetramer structure is the most probable and stable supramolecular assembly for the active ion channel structure. The results illustrate the possibility of exploiting multiple Fδ-:M+ interactions for ion transport and using fluorous interfaces to create functional nanostructures.

Indexed as

Amino AcidsCations, MonovalentHalogenationHydrophobic and Hydrophilic InteractionsIon ChannelsIon TransportLipid BilayersMolecular Dynamics SimulationNanoporesPeptidesPhosphatidylcholinesProtein FoldingProtein MultimerizationProtein Structure, SecondarySodium1-palmitoyl-2-oleoylphosphatidylcholineAmino AcidsCations, MonovalentIon ChannelsLipid BilayersPeptidesPhosphatidylcholinesSodium

Identifiers

PMID27835700
PMCPMC5106009

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.