ArticleBiophysical chemistry2026
The effect of lipid saturation on the formation of styrene maleic acid lipid nanoparticles.
Article in Biophysical chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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.
The trial behind it
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Who cites it
1 citing paper in PubMed.
- 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
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The ability to use styrene maleic acid (SMA) to solubilize membrane proteins has been of significant interest. The formation of the lipid nanodiscs and extraction of the proteins without the use of detergent allows for the study of these membrane proteins in a more native environment. Traditional mimetic systems, such as micelles, bicelles, and liposomes all have compatibility limitations in their ability to provide a native environment for the protein. Lipid composition plays a significant role in the compatibility of these mimetic systems with membrane proteins. In this study, lipids with varying degrees of saturation are used to assess the efficacy of the SMA polymer in forming styrene maleic acid lipid nanoparticles (SMALPs). Lipids ranging from fully saturated to fully unsaturated are used along with two SMA polymers with various hydrophobic tail lengths. Dynamic light scattering (DLS) and transmission electron microscopy (TEM) are used to characterize the liposomes and SMALPs. Continuous Wave-Electron Paramagnetic Resonance Spectroscopy (CW-EPR) is used to understand the effect of SMA on a spin-labeled membrane protein incorporated in the SMALP system. Results show the dynamic properties of membrane proteins incorporated in SMALPs are dependent on SMA polymer tail length as well as the lipid saturation. Lineshape analysis shows evidence of the hydrophobic tail of the SMA playing a role in how the protein is positioned within the SMALPs.
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Registered trials
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 Socratic graph.