Formation of a Mimetic Biomembrane from the Hydrophobic Protein Zein and Phospholipids: Structure and Application,The Journal of Physical Chemistry C

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Formation of a Mimetic Biomembrane from the Hydrophobic Protein Zein and Phospholipids: Structure and Application
The Journal of Physical Chemistry C ( IF 3.3 ) Pub Date : 2017-09-05 00:00:00 , DOI: 10.1021/acs.jpcc.7b04573
Liping Wang ₁ , Toshiaaki Gotoh ₂ , Yuzhu Wang ₃ , Tsutomu Kouyama ₂ , Jin-Ye Wang ₁

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α-Zein, a storage protein in corn endosperm, could be purified easily and in large amounts. In this study, α-zein was incorporated into phospholipid–cholesterol (PC–Chol) liposomes. The maximal amount of α-zein incorporated in the liposome was 0.05% (mol/mol) and the PC:Zein molar ratio was near 2400. At this level of zein insertion, the phase transition temperature of the lipid bilayer was little affected, but the leakage of doxorubicin (DOX) from the PC–Chol liposome became obviously slower when α-zein was added at a higher temperature than the phase transition temperature. Cryogenic transmission electron micrographs of the PC–Chol–Zein liposome showed that adjacent membranes in multilamellar vesicles were often aligned at a regular interval of about 7 nm. Data from synchrotron small-angle X-ray scattering of the PC–Chol–Zein liposome indicated the formation of the multilamellar structure with an intermembrane interval of 7.2 nm, whereas no homogeneous membrane alignment was observed in the absence of zein. The present observation can be well explained by supposing that α-zein takes on such an elongated conformation that it penetrates through two adjacent membrane layers. This feature seems to be compatible with a recently proposed superhelical structural model of α-zein. Meanwhile, experiments with the fluorescent-labeled α-zein showed that the PC–Chol–Zein liposome could be uptaken by an intact cell and localized in some specialized area (possibly endosomes) within the cell instead of being diffusely distributed in the cell. Thus, the PC–Chol–Zein liposome seems to act as an interesting biomembrane model and may be applicable as a drug delivery system.

中文翻译：

由疏水蛋白玉米醇溶蛋白和磷脂的模拟生物膜的形成：结构和应用。

玉米胚乳中的一种贮藏蛋白α-玉米醇溶蛋白可以很容易地被大量纯化。在这项研究中，α-玉米醇溶蛋白被掺入磷脂-胆固醇（PC-Chol）脂质体中。脂质体中掺入的α-玉米醇溶蛋白的最大量为0.05％（mol / mol），PC：玉米醇溶蛋白的摩尔比接近2400。在此玉米醇溶蛋白插入水平下，脂质双层的相变温度几乎不受影响，但当在比相变温度更高的温度下添加α-玉米醇溶蛋白时，阿霉素（PC-Chol）脂质体从阿霉素（DOX）的泄漏变得明显变慢。PC-Chol-Zein脂质体的低温透射电子显微照片显示，多层囊泡中的相邻膜通常以约7 nm的规则间隔排列。PC-Chol-Zein脂质体的同步加速器小角度X射线散射数据表明，膜间间隔为7.2 nm的多层结构形成，而在没有玉米醇溶蛋白的情况下未观察到均匀的膜排列。通过假设α-玉米醇溶蛋白具有如此细长的构型，使其穿透两个相邻的膜层，可以很好地解释本观察结果。该特征似乎与最近提出的α-玉米醇溶蛋白的超螺旋结构模型相容。同时，用荧光标记的α-玉米醇溶蛋白进行的实验表明，PC-Chol-玉米醇溶蛋白脂质体可以被完整的细胞摄取并定位在细胞内的某些特定区域（可能是内体）中，而不是分散地分布在细胞中。因此，

更新日期：2017-09-06

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