Evidence map›Paper›PMID 27547605›Full record

ArticleBeilstein journal of nanotechnology2016

Reconstitution of the membrane protein OmpF into biomimetic block copolymer-phospholipid hybrid membranes.

Matthias Bieligmeyer, Franjo Artukovic, Stephan Nussberger, Thomas Hirth, Thomas Schiestel, Michaela Müller

Abstract read
In one paragraph

Article in Beilstein journal of nanotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Flippase-Mediated Hybrid Vesicle Division.Advanced materials (Deerfield Beach, Fla.) · 2025
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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.

Matthias BieligmeyerInstitute of Interfacial Process Engineering and Plasma Technology, Department of Chemical Interfacial Process Engineering, University of Stuttgart, Nobelstraße 12, 70569 Stuttgart, Germany.
Franjo ArtukovicInstitute of Biomaterials and Biomolecular Systems, Department of Biophysics, University of Stuttgart, Pfaffenwaldring 57, 70550 Stuttgart, Germany.
Stephan NussbergerInstitute of Biomaterials and Biomolecular Systems, Department of Biophysics, University of Stuttgart, Pfaffenwaldring 57, 70550 Stuttgart, Germany.
Thomas HirthInstitute of Interfacial Process Engineering and Plasma Technology, Department of Chemical Interfacial Process Engineering, University of Stuttgart, Nobelstraße 12, 70569 Stuttgart, Germany; Fraunhofer Institute for Interfacial Engineering and Biotechnology, Department of Interfacial Engineering and Materials Science, Nobelstraße 12, 70569 Stuttgart, Germany.
Thomas SchiestelFraunhofer Institute for Interfacial Engineering and Biotechnology, Department of Interfacial Engineering and Materials Science, Nobelstraße 12, 70569 Stuttgart, Germany.
Michaela MüllerFraunhofer Institute for Interfacial Engineering and Biotechnology, Department of Interfacial Engineering and Materials Science, Nobelstraße 12, 70569 Stuttgart, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structure and function of many transmembrane proteins are affected by their environment. In this respect, reconstitution of a membrane protein into a biomimetic polymer membrane can alter its function. To overcome this problem we used membranes formed by poly(1,4-isoprene-block-ethylene oxide) block copolymers blended with 1,2-diphytanoyl-sn-glycero-3-phosphocholine. By reconstituting the outer membrane protein OmpF from Escherichia coli into these membranes, we demonstrate functionality of this protein in biomimetic lipopolymer membranes, independent of the molecular weight of the block copolymers. At low voltages, the channel conductance of OmpF in 1 M KCl was around 2.3 nS. In line with these experiments, integration of OmpF was also revealed by impedance spectroscopy. Our results indicate that blending synthetic polymer membranes with phospholipids allows for the reconstitution of transmembrane proteins under preservation of protein function, independent of the membrane thickness.

Indexed as

biomimeticsblock copolymerlipopolymer mixtureOmpF reconstitutionself-assembly

Identifiers

PMID27547605
PMCPMC4979867

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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.