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Abstract <p><b>Objective:</b> Reconstituting a membrane protein in a membrane-like environment is an essential factor, determining the relevance of structural data obtained for a membrane protein. Mixtures of lauryl maltose neopentyl glycol (LMNG) with cholesteryl hemisuccinate (CHS) are a recently introduced membrane-like medium with a proven stabilizing effect on membrane proteins of several classes. However, the structure of LMNG/CHS micelles remains underinvestigated. <b>Methods:</b> In the present work, we apply diffusion and nuclear Overhauser effect NMR spectroscopy and the transmembrane domain pf EphA2 as a sensor transmembrane protein to characterize the properties of LMNG/CHS micelles in comparison to other membrane mimetics, including phospholipid bicelles. <b>Results and Discussion:</b> According to the diffusion measurements, CHS addition to LMNG micelles reduces the temperature- and concentration-induced growth of the particles, preventing LMNG from forming non-regular rod-like structures. CHS is evenly distributed within the micelles, with no preference for the protein-adjacent regions. For a model protein, LMNG/CHS provides an environment similar to dodecyl maltoside but distinct from lipid bicelles in terms of lipid-protein contacts. <b>Conclusions:</b> LMNG/CHS is a membrane mimetic that stabilizes membrane proteins, has a defined micellar structure with even CHS distribution, suppresses undesirable rod-like LMNG aggregation, and offers a lipid-protein contact environment different from that of bicelles but similar to dodecyl maltoside.</p>

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Properties of LMNG/CHS Micelles

  • 期刊论文

  • 发表日期：

    2026年4月30日

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  • Konstantin Mineev,
  • Harald Schwalbe

摘要

Abstract

Objective: Reconstituting a membrane protein in a membrane-like environment is an essential factor, determining the relevance of structural data obtained for a membrane protein. Mixtures of lauryl maltose neopentyl glycol (LMNG) with cholesteryl hemisuccinate (CHS) are a recently introduced membrane-like medium with a proven stabilizing effect on membrane proteins of several classes. However, the structure of LMNG/CHS micelles remains underinvestigated. Methods: In the present work, we apply diffusion and nuclear Overhauser effect NMR spectroscopy and the transmembrane domain pf EphA2 as a sensor transmembrane protein to characterize the properties of LMNG/CHS micelles in comparison to other membrane mimetics, including phospholipid bicelles. Results and Discussion: According to the diffusion measurements, CHS addition to LMNG micelles reduces the temperature- and concentration-induced growth of the particles, preventing LMNG from forming non-regular rod-like structures. CHS is evenly distributed within the micelles, with no preference for the protein-adjacent regions. For a model protein, LMNG/CHS provides an environment similar to dodecyl maltoside but distinct from lipid bicelles in terms of lipid-protein contacts. Conclusions: LMNG/CHS is a membrane mimetic that stabilizes membrane proteins, has a defined micellar structure with even CHS distribution, suppresses undesirable rod-like LMNG aggregation, and offers a lipid-protein contact environment different from that of bicelles but similar to dodecyl maltoside.