ArticleChemistry and physics of lipids2026
A comparison of the effect of SMA derivatives on the structural topology and dynamics of two bacteriophage peptides.
Article in Chemistry and physics of lipids, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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.
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Who cites it
3 citing papers 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
- Article
- The effect of lipid saturation on the formation of styrene maleic acid lipid nanoparticles.Biophysical chemistry · 2026Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Researchers have explored and cultivated suitable membrane mimetics to preserve a physiological solvent condition for membrane protein functions. This involves emulating the properties of lipid bilayers, particularly within the hydrophobic core. Membrane mimetics exist in diverse forms, such as micelles, bicelles, liposomes, and nanodiscs. Polymers, such as styrene-maleic acid (SMA), have been found to offer a potentially suitable means to solubilize membrane proteins without resorting to detergents. It is widely recognized that various membrane mimetics yield distinct structural and dynamic configurations in membrane proteins. Styrene-maleic acid derivatives (SMADs) are of particular significance in this study; they are known for their ability to generate lipid nanoparticles. It has been hypothesized that using SMA derivatives with the same charge as the target membrane protein preserves the protein's structural and dynamic attributes compared to other bilayer membrane mimetics. This study explores the impact of different charges of SMA derivatives on two bacteriophage-encoded peptides explicitly focusing on their influence as charged peptides. Positively charged, neutral, and negatively charged SMA derivatives interactions with pinholin S
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Registered trials
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