Evidence map›Paper›PMID 40143542›Full record

ArticleBiophysical journal2025

Reversible tuning of membrane sterol levels by cyclodextrin in a dialysis setting.

Cynthia Alsayyah, Emmanuel Rodrigues, Julia Hach, Mike F Renne, Robert Ernst

Abstract read
In one paragraph

Article in Biophysical journal, 2025. 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. 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

5 authors.

Cynthia AlsayyahMedical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, Homburg, Saar, Germany; Preclinical Center for Molecular Signaling (PZMS), Medical Faculty, Saarland University, Homburg, Saar, Germany; Center for Biophysics (ZBP), Saarland University, Saarland, Germany.
Emmanuel RodriguesMedical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, Homburg, Saar, Germany; Preclinical Center for Molecular Signaling (PZMS), Medical Faculty, Saarland University, Homburg, Saar, Germany; Center for Biophysics (ZBP), Saarland University, Saarland, Germany.
Julia HachMedical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, Homburg, Saar, Germany; Preclinical Center for Molecular Signaling (PZMS), Medical Faculty, Saarland University, Homburg, Saar, Germany; Center for Biophysics (ZBP), Saarland University, Saarland, Germany.
Mike F RenneMedical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, Homburg, Saar, Germany; Preclinical Center for Molecular Signaling (PZMS), Medical Faculty, Saarland University, Homburg, Saar, Germany; Center for Biophysics (ZBP), Saarland University, Saarland, Germany.
Robert ErnstMedical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, Homburg, Saar, Germany; Preclinical Center for Molecular Signaling (PZMS), Medical Faculty, Saarland University, Homburg, Saar, Germany; Center for Biophysics (ZBP), Saarland University, Saarland, Germany. Electronic address: robert.ernst@uni-saarland.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Large unilamellar vesicles are popular membrane models for studying the impact of lipids and bilayer properties on the structure and function of transmembrane proteins. However, the functional reconstitution of transmembrane proteins in liposomes can be challenging, especially if the hydrophobic thickness of the protein does not match the thickness of the lipid bilayer. Such hydrophobic mismatch causes protein aggregation and low yields during the reconstitution procedure, which are exacerbated in sterol-rich membranes featuring low membrane compressibility. Here, we explore new approaches to reversibly tune the sterol content of (proteo)liposomes with methyl-β-cyclodextrin (mβCD) in a dialysis setting. Maintaining (proteo)liposomes in a confined compartment minimizes loss of material during cholesterol transfer and facilitates efficient removal of mβCD. We monitor the sterol concentration in the membrane with help of the solvatochromic probe C-Laurdan, which reports on lipid packing. Using Förster resonance energy transfer, we show that cholesterol delivery to proteoliposomes induces the oligomerization of a membrane property sensor, whereas a subsequent removal of cholesterol demonstrates full reversibility. We propose that tuning membrane compressibility by mβCD-meditated cholesterol delivery and removal in a dialysis setup provides a new handle to study the impact of sterols and membrane compressibility on membrane protein structure, function, and dynamics.

Indexed as

beta-CyclodextrinsDialysisSterolsCholesterolLiposomesProteolipidsbeta-CyclodextrinsCholesterolLiposomesmethyl-beta-cyclodextrinProteolipidsSterols

Identifiers

PMID40143542
PMCPMC12256852

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Registered trials

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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.