Evidence map›Paper›PMID 40858559›Full record

ArticleNature communications2025

DeFrND: detergent-free reconstitution into native nanodiscs with designer membrane scaffold peptides.

Qian Ren, Jing Wang, Vinay Idikuda, Shanwen Zhang, Jeehae Shin, W Grant Ludlam, Luis M Real Hernandez, Sara Zdancewicz, Alex J B Kreutzberger, Hucheng Chang and 7 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. IR-AMES uncovers structure and composition of Alzheimer's tau oligomers.bioRxiv : the preprint server for biology · 2026
    Article
  6. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

17 authors.

Qian Ren *Department of Molecular Medicine, UF Scripps Biomedical Research, Jupiter, Florida, USA.ORCID http://orcid.org/0009-0008-8514-4973
Jing Wang *Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY, USA.
Vinay Idikuda *Departments of Anesthesiology, Neuroscience, Biochemistry and Molecular Biophysics, Center for Investigation of Membrane Excitability Diseases, Washington University School of Medicine, St. Louis, MO, USA.ORCID http://orcid.org/0000-0001-6324-5839
Shanwen Zhang *Department of Molecular Medicine, UF Scripps Biomedical Research, Jupiter, Florida, USA.
Jeehae ShinDepartment of Molecular Medicine, UF Scripps Biomedical Research, Jupiter, Florida, USA.ORCID http://orcid.org/0000-0003-3127-3450
W Grant LudlamDepartment of Neuroscience, UF Scripps Biomedical Research, Jupiter, FL, USA.
Luis M Real HernandezDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA.
Sara ZdancewiczDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA.
Alex J B KreutzbergerDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA.
Hucheng ChangDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA.
Volker KiesslingDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA.ORCID http://orcid.org/0000-0002-9388-5703
Lukas K TammDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA.ORCID http://orcid.org/0000-0002-1674-4464
Ahmad JomaaDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA.ORCID http://orcid.org/0000-0002-5543-7942
Ilya LeventalDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA.ORCID http://orcid.org/0000-0002-1206-9545
Kirill MartemyanovDepartment of Neuroscience, UF Scripps Biomedical Research, Jupiter, FL, USA.
Baron ChandaDepartments of Anesthesiology, Neuroscience, Biochemistry and Molecular Biophysics, Center for Investigation of Membrane Excitability Diseases, Washington University School of Medicine, St. Louis, MO, USA. bchanda@wustl.edu.ORCID http://orcid.org/0000-0003-4954-7034
Huan BaoDepartment of Molecular Medicine, UF Scripps Biomedical Research, Jupiter, Florida, USA. baoh@virginia.edu.ORCID http://orcid.org/0000-0002-4301-4627

Funding

Washington University Center for Cellular ImagingP30CA091842 · NCI · WASHINGTON UNIVERSITY · PI TIMOTHY J. EBERLEIN · 2001 to 2026
$128.0M
WU INSTITUTE OF CLINICAL AND TRANSLATIONAL SCIENCESUL1TR002345 · NCATS · WASHINGTON UNIVERSITY · PI William G. Powderly · 2017 to 2026
$97.8M
NCCAT: National Center for CryoEM Access and Training- Supplement for Windows 10 and FFIU24GM129539 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2018 to 2023
$53.9M
WU P&FP30DK020579 · NIDDK · WASHINGTON UNIVERSITY · PI Clay F. Semenkovich · 2013 to 2026
$27.1M
NCCAT: National Center for CryoEM Access and TrainingR24GM154192 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI EDWARD T ENG, Jeffrey S Kieft · 2024 to 2026
$21.0M
Structural Dynamics of the Exocytotic Fusion Machine in Neurons.P01GM072694 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI TAMM, LUKAS K · 2005 to 2021
$17.4M
Biophysical mechanisms of gating and modulation in voltage-gated ion channel superfamilyR35NS116850 · NINDS · WASHINGTON UNIVERSITY · PI Baron Chanda · 2020 to 2026
$6.9M
Developing next-generation nanodiscs for the study and modulation of membrane proteinsDP2GM140920 · NIGMS · UNIVERSITY OF VIRGINIA · PI BAO, HUAN · 2020 to 2020
$2.7M
Architecture of inhibitory G protein signaling in the hippocampusR01NS128039 · NINDS · UNIVERSITY OF MINNESOTA · PI Kirill A. Martemyanov, KEVIN D WICKMAN · 2023 to 2026
$2.6M
Structural landscape of photoreceptor synapsesR01EY034339 · NEI · UNIVERSITY OF FLORIDA · PI MARTEMYANOV, KIRILL A., SINGH, APPU · 2022 to 2024
$1.4M
Unraveling the Mechanisms of Protein Sorting and Localization to OrganellesR35GM160490 · NIGMS · UNIVERSITY OF VIRGINIA · PI Ahmad Jomaa · 2025 to 2026
$888k
Designer nanodiscs to probe and reprogram membrane biologyR35GM156801 · NIGMS · UNIVERSITY OF VIRGINIA · PI Huan Bao · 2025 to 2026
$801k
NCATS NIH HHS UL1 TR002345NCI NIH HHS P30 CA091842NEI NIH HHS R01 EY034339NIA NIH HHS R21 AG078699NIDDK NIH HHS P30 DK020579NIGMS NIH HHS DP2 GM140920NIGMS NIH HHS P01 GM072694NIGMS NIH HHS R24 GM154192NIGMS NIH HHS R35 GM156801NIGMS NIH HHS R35 GM160490NIGMS NIH HHS U24 GM129539NINDS NIH HHS F32 NS124758NINDS NIH HHS R01 NS128039NINDS NIH HHS R35 NS116850U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) DP2GM140920U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R35GM156801U.S. Department of Health & Human Services | NIH | National Institute on Aging (U.S. National Institute on Aging) R21AG078699
6 · The paper itself

Abstract

Membrane scaffold protein-based nanodiscs have facilitated unprecedented structural and biophysical analysis of membrane proteins in a near-native lipid environment. However, successful reconstitution of membrane proteins in nanodiscs requires prior solubilization and purification in detergents, which may impact their physiological structure and function. Furthermore, the detergent-mediated reconstitution of nanodiscs is unlikely to recapitulate the precise composition or asymmetry of native membranes. To circumvent this fundamental limitation of traditional nanodisc technology, we herein describe the development of membrane-solubilizing peptides to directly extract membrane proteins from native cell membranes into nanoscale discoids. By systematically protein engineering and screening, we create a class of chemically modified Apolipoprotein-A1 mimetic peptides to enable the formation of detergent-free nanodiscs with high efficiency. Nanodiscs generated with these engineered membrane scaffold peptides are suitable for obtaining high-resolution structures using single-particle cryo-EM with native lipids. To further highlight the versatility of our approach, we directly extract a sampling of membrane signaling proteins with their surrounding native membranes for biochemical and biophysical interrogations.

Indexed as

Membrane ProteinsNanostructuresPeptidesApolipoprotein A-ICell MembraneCryoelectron MicroscopyDetergentsHumansLipid BilayersProtein EngineeringApolipoprotein A-IDetergentsLipid BilayersMembrane ProteinsPeptides

Identifiers

PMID40858559
PMCPMC12381110

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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.