ArticleChemistry and physics of lipids2019
Characterizing the structure of styrene-maleic acid copolymer-lipid nanoparticles (SMALPs) using RAFT polymerization for membrane protein spectroscopic studies.
Article in Chemistry and physics of lipids, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- An ionic liquid-functionalized styrene-maleic anhydride copolymer brush stationary phase coupled with offline two-dimensional LC-MS/MS for comprehensive exosomal phospholipid profiling in breast cancer.Analytical and bioanalytical chemistry · 2026Article
- The effect of lipid saturation on the formation of styrene maleic acid lipid nanoparticles.Biophysical chemistry · 2026Article
- Influence of lipid saturation on the structural properties of styrene maleic acid lipid nanoparticles (SMALPs).Biochimica et biophysica acta. Biomembranes · 2025Article
- Comparison of lipid dynamics and permeability in styrene-maleic acid and diisobutylene-maleic acid copolymer lipid nanodiscs by electron paramagnetic resonance spectroscopy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Article
- Vinyl Ether Maleic Acid Polymers: Tunable Polymers for Self-Assembled Lipid Nanodiscs and Environments for Membrane Proteins.Biomacromolecules · 2024Article
- Characterization of nanodisc-forming peptides for membrane protein studies.Journal of colloid and interface science · 2024Article
- [Modified styrene-maleic anhydride copolymer-based chromatographic stationary phase for phospholipid separation and analysis].Se pu = Chinese journal of chromatography · 2023Article
- Electron paramagnetic resonance spectroscopic characterization of the human KCNE3 protein in lipodisq nanoparticles for structural dynamics of membrane proteins.Biophysical chemistry · 2023Article
- pH-tunable membrane-active polymers, NCMNP2a-Chemical science · 2023Article
- Enhancing the stability and homogeneity of non-ionic polymer nanodiscs by tuning electrostatic interactions.Journal of colloid and interface science · 2023Article
- Purification and membrane interactions of human KCNQ1Biochimica et biophysica acta. Biomembranes · 2022Article
- Detergent-Free Isolation of Membrane Proteins and Strategies to Study Them in a Near-Native Membrane Environment.Biomolecules · 2022Review
- Synthesis and Evaluation of a Library of Alternating Amphipathic Copolymers to Solubilize and Study Membrane Proteins.Biomacromolecules · 2022Article
- Kinetic analysis of antibody binding to integral membrane proteins stabilized in SMALPs.BBA advances · 2021Article
- Development of Methodology to Investigate the Surface SMALPome of Mammalian Cells.Frontiers in molecular biosciences · 2021Article
- Simple Derivatization of RAFT-Synthesized Styrene-Maleic Anhydride Copolymers for Lipid Disk Formulations.Biomacromolecules · 2020Article
- Structural characterization of styrene-maleic acid copolymer-lipid nanoparticles (SMALPs) using EPR spectroscopy.Chemistry and physics of lipids · 2019Article
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8 authors.
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Abstract
Membrane proteins play an important role in maintaining the structure and physiology of an organism. Despite their significance, spectroscopic studies involving membrane proteins remain challenging due to the difficulties in mimicking their native lipid bilayer environment. Membrane mimetic systems such as detergent micelles, liposomes, bicelles, nanodiscs, lipodisqs have improved the solubility and folding properties of the membrane proteins for structural studies, however, each mimetic system suffers from its own limitations. In this study, using three different lipid environments, vesicles were titrated with styrene-maleic acid (StMA) copolymer leading to a homogeneous SMALP system (∼10 nm) at a weight ratio of 1:1.5 (vesicle: StMA solution). A combination of Dynamic Light Scattering (DLS) and Transmission Electron Microscopy (TEM) was used to characterize these SMALPs. We used a controlled synthesis mechanism to synthesize StMA based block copolymers called reversible addition-fragmentation chain transfer polymerization (RAFT) SMALPs. Incorporation of the Voltage Sensor Domain of KCNQ1 (Q1-VSD) into RAFT SMALPs indicates that this is a promising application of this system to study membrane proteins using different biophysical techniques. V165C in Q1-VSD corresponding to the hydrophobic region was incorporated into the SMALP system. Continuous Wave-Electron Paramagnetic Resonance (CW-EPR) line shape analysis showed line shape broadening, exposing a lower rigid component and a faster component of the spin label.
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