Evidence map›Paper›PMID 25008079›Full record

ArticleJournal of the Royal Society, Interface2014

Droplet interface bilayer reconstitution and activity measurement of the mechanosensitive channel of large conductance from Escherichia coli.

Hanna M G Barriga, Paula Booth, Stuart Haylock, Richard Bazin, Richard H Templer, Oscar Ces

Abstract read
In one paragraph

Article in Journal of the Royal Society, Interface, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Review
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  4. Article
  5. Article
  6. Probing membrane protein properties using droplet interface bilayers.Experimental biology and medicine (Maywood, N.J.) · 2019
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  15. Microchamber device for detection of transporter activity of adherent cells.Frontiers in bioengineering and biotechnology · 2015
    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

6 authors.

Hanna M G BarrigaMembrane Biophysics Platform, Institute of Chemical Biology and Department of Chemistry, Imperial College London, South Kensington, London SW7 2AX, UK hanna.barriga@imperial.ac.uk.
Paula BoothDepartment of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
Stuart HaylockMembrane Biophysics Platform, Institute of Chemical Biology and Department of Chemistry, Imperial College London, South Kensington, London SW7 2AX, UK.
Richard BazinPfizer Global Research and Development, Sandwich CT13 9NJ, UK.
Richard H TemplerMembrane Biophysics Platform, Institute of Chemical Biology and Department of Chemistry, Imperial College London, South Kensington, London SW7 2AX, UK.
Oscar CesMembrane Biophysics Platform, Institute of Chemical Biology and Department of Chemistry, Imperial College London, South Kensington, London SW7 2AX, UK o.ces@imperial.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/F0131674/1
6 · The paper itself

Abstract

Droplet interface bilayers (DIBs) provide an exciting new platform for the study of membrane proteins in stable bilayers of controlled composition. To date, the successful reconstitution and activity measurement of membrane proteins in DIBs has relied on the use of the synthetic lipid 1,2-diphytanoyl-sn-glycero-3-phosphocholine (DPhPC). We report the functional reconstitution of the mechanosensitive channel of large conductance (MscL) into DIBs composed of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), a lipid of significantly greater biological relevance than DPhPC. MscL functionality has been demonstrated using a fluorescence-based assay, showing that dye flow occurs across the DIB when MscL is gated by the cysteine reactive chemical 2-(trimethylammonium)ethyl methane thiosulfonate bromide (MTSET). MscL has already been the subject of a number of studies investigating its interaction with the membrane. We propose that this method will pave the way for future MscL studies looking in detail at the effects of controlled composition or membrane asymmetry on MscL activity using biologically relevant lipids and will also be applicable to other lipid-protein systems, paving the way for the study of membrane proteins in DIBs with biologically relevant lipids.

Indexed as

Escherichia coliEscherichia coli ProteinsFluorescent DyesGlycerylphosphorylcholineIon ChannelsLipid BilayersLipidsMesylatesPhosphatidylcholines1,2-diphytanoylphosphatidylcholine1,2-oleoylphosphatidylcholine(2-(trimethylammonium)ethyl)methanethiosulfonateEscherichia coli ProteinsFluorescent DyesGlycerylphosphorylcholineIon ChannelsLipid BilayersLipidsMesylatesMscL protein, E coliPhosphatidylcholines1,2-dioleoyl-sn-glycero-3-phosphocholinedroplet interface bilayersfluorescencemechanosensitive channel of large conductance

Identifiers

PMID25008079
PMCPMC4233688

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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.