ArticleBiochimica et biophysica acta2015
The use of SMALPs as a novel membrane protein scaffold for structure study by negative stain electron microscopy.
Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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Who cites it
74 citing papers in PubMed.
- DNA-Lipid Nanodiscs with a Polyethylene Glycol Interface.Journal of the American Chemical Society · 2026Article
- The effect of lipid saturation on the formation of styrene maleic acid lipid nanoparticles.Biophysical chemistry · 2026Article
- Swapped and non-swapped TRAAK states co-exist in membranes at a ratio influenced by temperature.Nature communications · 2026Article
- Planar Lipid Bilayers and Liposomes: Essential Models for Advancing Protein Structure and Function Research.Advances in experimental medicine and biology · 2026Review
- High-Throughput Identification and Characterization of LptDE-Binding Bicycle Peptides Using Phage Display and Cryo-EM.Journal of medicinal chemistry · 2025Article
- Broad-Spectrum Antiviral Styrene Maleic-Acid Copolymer Lipid Particle Nanodiscs for pH-Responsive Irreversible Virus Inactivation.Biomacromolecules · 2025Article
- Characterization of intact FeoB in a lipid bilayer using styrene-maleic acid (SMA) copolymers.Biochimica et biophysica acta. Biomembranes · 2025Article
- Conformations of membrane human immunodeficiency virus (HIV-1) envelope glycoproteins solubilized in Amphipol A18 lipid-nanodiscs.Journal of virology · 2024Article
- Article
- The application and development of electron microscopy for three-dimensional reconstruction in life science: a review.Cell and tissue research · 2024Review
- The application of nanodiscs in membrane protein drug discovery & development and drug delivery.Frontiers in chemistry · 2024Review
- pH-tunable membrane-active polymers, NCMNP2a-Chemical science · 2023Article
- ATG9 vesicles comprise the seed membrane of mammalian autophagosomes.The Journal of cell biology · 2023Article
- Conformations of Human Immunodeficiency Virus Envelope Glycoproteins in Detergents and Styrene-Maleic Acid Lipid Particles.Journal of virology · 2023Article
- Recent advances in membrane mimetics for membrane protein research.Biochemical Society transactions · 2023Review
- Divalent nanobodies to platelet CLEC-2 can serve as agonists or antagonists.Communications biology · 2023Article
- Membranes under the Magnetic Lens: A Dive into the Diverse World of Membrane Protein Structures Using Cryo-EM.Chemical reviews · 2022Review
- Detergents and alternatives in cryo-EM studies of membrane proteins.Acta biochimica et biophysica Sinica · 2022Review
- The function of BK channels extracted and purified within SMALPs.The Biochemical journal · 2022Article
- Detergent-Free Isolation of Membrane Proteins and Strategies to Study Them in a Near-Native Membrane Environment.Biomolecules · 2022Review
14 more citing papers are in PubMed but not listed here.
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8 authors.
Funding
Abstract
Despite the great progress recently made in resolving their structures, investigation of the structural biology of membrane proteins still presents major challenges. Even with new technical advances such as lipidic cubic phase crystallisation, obtaining well-ordered crystals remains a significant hurdle in membrane protein X-ray crystallographic studies. As an alternative, electron microscopy has been shown to be capable of resolving >3.5Å resolution detail in membrane proteins of modest (~300 kDa) size, without the need for crystals. However, the conventional use of detergents for either approach presents several issues, including the possible effects on structure of removing the proteins from their natural membrane environment. As an alternative, it has recently been demonstrated that membrane proteins can be effectively isolated, in the absence of detergents, using a styrene maleic acid co-polymer (SMA). This approach yields SMA lipid particles (SMALPs) in which the membrane proteins are surrounded by a small disk of lipid bilayer encircled by polymer. Here we use the Escherichia coli secondary transporter AcrB as a model membrane protein to demonstrate how a SMALP scaffold can be used to visualise membrane proteins, embedded in a near-native lipid environment, by negative stain electron microscopy, yielding structures at a modest resolution in a short (days) timeframe. Moreover, we show that AcrB within a SMALP scaffold is significantly more active than the equivalent DDM stabilised form. The advantages of SMALP scaffolds within electron microscopy are discussed and we conclude that they may prove to be an important tool in studying membrane protein structure and function.
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