ArticleProceedings of the National Academy of Sciences of the United States of America2014
Detergent-free isolation, characterization, and functional reconstitution of a tetrameric K+ channel: the power of native nanodiscs.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.
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Who cites it
150 citing papers in PubMed, 320 citations in OpenAlex.
- Understanding charged polymer-lipid interactions in model membranes revealed by EPR and solid-state NMR: Implications for membrane protein studies.Chemistry and physics of lipids · 2026Article
- Molecular Mechanisms Governing Peptide Nanodisc Assembly and Stability.bioRxiv : the preprint server for biology · 2026Article
- Swapped and non-swapped TRAAK states co-exist in membranes at a ratio influenced by temperature.Nature communications · 2026Article
- A comparison of the effect of SMA derivatives on the structural topology and dynamics of two bacteriophage peptides.Chemistry and physics of lipids · 2026Article
- Insights into the structure and modulation of human TWIK-2.Nature communications · 2026Article
- RePol: A high-throughput screen for optimizing membrane protein solubilization and purification using polymers.Protein science : a publication of the Protein Society · 2026Article
- Method for Purification and Electrophysiological Recordings of Ion Channels from Trypanosomatids.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Planar Lipid Bilayers and Liposomes: Essential Models for Advancing Protein Structure and Function Research.Advances in experimental medicine and biology · 2026Review
- MAASTY: a (dis)ordered copolymer for structural determination of human membrane proteins in native nanodiscs.Nature communications · 2025Article
- Article
- Coming Clean and Avoiding Bubble Trouble-Using Detergents Wisely in the Purification of Membrane Proteins for Cryo-EM Studies.Biomolecules · 2025Review
- Maintaining the Integral Membrane Proteome: Revisiting the Functional Repertoire of Integral Membrane Proteases.Chembiochem : a European journal of chemical biology · 2025Review
- Advancements in the conservation of the conformational epitope of membrane protein immunogens.Frontiers in immunology · 2025Review
- On the Properties of Styrene-Maleic Acid Copolymer-Lipid Nanoparticles: A Solution NMR Perspective.Polymers · 2024Article
- Lipid unsaturation promotes BAX and BAK pore activity during apoptosis.Nature communications · 2024Article
- Review
- Characterization of membrane protein interactions by peptidisc-mediated mass photometry.iScience · 2024Article
- Factors influencing the detergent-free membrane protein isolation using synthetic nanodisc-forming polymers.Biochimica et biophysica acta. Biomembranes · 2024Article
- Alternatives to Styrene- and Diisobutylene-Based Copolymers for Membrane Protein Solubilization via Nanodisc Formation.Angewandte Chemie (International ed. in English) · 2023Article
- Label-free measurement of antimicrobial peptide interactions with lipid vesicles and nanodiscs using microscale thermophoresis.Scientific reports · 2023Article
90 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
A major obstacle in the study of membrane proteins is their solubilization in a stable and active conformation when using detergents. Here, we explored a detergent-free approach to isolating the tetrameric potassium channel KcsA directly from the membrane of Escherichia coli, using a styrene-maleic acid copolymer. This polymer self-inserts into membranes and is capable of extracting membrane patches in the form of nanosize discoidal proteolipid particles or "native nanodiscs." Using circular dichroism and tryptophan fluorescence spectroscopy, we show that the conformation of KcsA in native nanodiscs is very similar to that in detergent micelles, but that the thermal stability of the protein is higher in the nanodiscs. Furthermore, as a promising new application, we show that quantitative analysis of the co-isolated lipids in purified KcsA-containing nanodiscs allows determination of preferential lipid-protein interactions. Thin-layer chromatography experiments revealed an enrichment of the anionic lipids cardiolipin and phosphatidylglycerol, indicating their close proximity to the channel in biological membranes and supporting their functional relevance. Finally, we demonstrate that KcsA can be reconstituted into planar lipid bilayers directly from native nanodiscs, which enables functional characterization of the channel by electrophysiology without first depriving the protein of its native environment. Together, these findings highlight the potential of the use of native nanodiscs as a tool in the study of ion channels, and of membrane proteins in general.
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