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10MAG/LDAO 反胶束的特性：理解其用于蛋白质包封的多功能性。

Characterization of 10MAG/LDAO reverse micelles: Understanding versatility for protein encapsulation.

机构信息

Department of Physics and Astronomy, Rowan University, 201 Mullica Hill Rd, Glassboro, NJ 08028, United States; Department of Biomedical and Biological Sciences, Rowan University, 201 Mullica Hill Rd, Glassboro, NJ 08028, United States.

Department of Chemistry, Virginia Commonwealth University, Richmond, Virginia 23284, United States.

出版信息

Biophys Chem. 2024 Aug;311:107269. doi: 10.1016/j.bpc.2024.107269. Epub 2024 May 21.

DOI:10.1016/j.bpc.2024.107269
PMID:38815545
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11225088/
Abstract

Reverse micelles (RMs) are spontaneously organizing nanobubbles composed of an organic solvent, surfactants, and an aqueous phase that can encapsulate biological macromolecules for various biophysical studies. Unlike other RM systems, the 1-decanoyl-rac-glycerol (10MAG) and lauryldimethylamine-N-oxide (LDAO) surfactant system has proven to house proteins with higher stability than other RM mixtures with little sensitivity to the water loading (W, defined by the ratio of water to surfactant). We investigated this unique property by encapsulating three model proteins - cytochrome c, myoglobin, and flavodoxin - in 10MAG/LDAO RMs and applying a variety of experimental methods to characterize this system's behavior. We found that this surfactant system differs greatly from the traditional, spherical, monodisperse RM population model. 10MAG/LDAO RMs were discovered to be oblate ellipsoids at all conditions, and as W was increased, surfactants redistributed to form a greater number of increasingly spherical ellipsoidal particles with pools of more bulk-like water. Proteins distinctively influence the thermodynamics of the mixture, encapsulating at their optimal RM size and driving protein-free RM sizes to scale accordingly. These findings inform the future development of similarly malleable encapsulation systems and build a foundation for application of 10MAG/LDAO RMs to analyze biological and chemical processes under nanoscale confinement.

摘要

反胶束（RMs）是由有机溶剂、表面活性剂和水相自发组成的纳米气泡，可以包裹生物大分子进行各种生物物理研究。与其他 RM 系统不同，1-癸酰基-rac-甘油（10MAG）和十二烷基二甲基氧化胺（LDAO）表面活性剂系统已被证明可容纳比其他 RM 混合物更稳定的蛋白质，对水含量（W，定义为水与表面活性剂的比例）的敏感性较小。我们通过将三种模型蛋白 - 细胞色素 c、肌红蛋白和黄素蛋白 - 包裹在 10MAG/LDAO RM 中，并应用各种实验方法来研究这种独特的性质，从而研究了这种特性。我们发现，这种表面活性剂系统与传统的、球形的、单分散 RM 群体模型有很大的不同。在所有条件下，10MAG/LDAO RM 均被发现为扁长椭球体，随着 W 的增加，表面活性剂重新分布，形成越来越多的球形椭球体，其中包含更多的类似块状的水。蛋白质显著影响混合物的热力学，在其最佳 RM 大小下进行包裹，并相应地驱动无蛋白质 RM 大小按比例缩小。这些发现为类似可塑的封装系统的未来发展提供了信息，并为 10MAG/LDAO RM 在纳米尺度限制下分析生物和化学过程的应用奠定了基础。

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