Engineering Globular Protein Vesicles through Tunable Self-Assembly of Recombinant Fusion Proteins
Engineering Globular Protein Vesicles through Tunable Self-Assembly of Recombinant Fusion Proteins
复制标题
DOI：
10.1002/smll.201700399
复制
发表时间：
2017-09-27
期刊：
影响因子：
13.3
通讯作者：
Champion, Julie A.
中科院分区：
文献类型：
--
作者：
Jang, Yeongseon;Choi, Won Tae;Champion, Julie A.
由折叠的球状蛋白组装而成的囊泡具有不同于传统脂质或聚合囊泡的功能。然而，它们在理解组装过程和控制囊泡属性方面也提出了挑战。通过对重组融合蛋白组装行为的详细研究，这项工作报告了一种简单的策略来设计包含功能球状结构域的蛋白囊泡。这是通过含有亮氨酸拉链和弹性蛋白样多肽的重组球状融合蛋白的可调自组装实现的。融合蛋白通过拉链的高亲和力结合在溶液中形成复合体，并在升温时通过动态凝聚物转变为稳定的中空囊泡。热驱动力可以通过蛋白质浓度或温度来调节，它控制着囊泡的大小以及囊泡是单层还是双层的。这些结果为通过自组装来设计具有所需尺寸和膜结构的球状蛋白囊泡提供了关键信息。
Vesicles assembled from folded, globular proteins have potential for functions different from traditional lipid or polymeric vesicles. However, they also present challenges in understanding the assembly process and controlling vesicle properties. From detailed investigation of the assembly behavior of recombinant fusion proteins, this work reports a simple strategy to engineer protein vesicles containing functional, globular domains. This is achieved through tunable self-assembly of recombinant globular fusion proteins containing leucine zippers and elastin-like polypeptides. The fusion proteins form complexes in solution via high affinity binding of the zippers, and transition through dynamic coacervates to stable hollow vesicles upon warming. The thermal driving force, which can be tuned by protein concentration or temperature, controls both vesicle size and whether vesicles are single or bi-layered. These results provide critical information to engineer globular protein vesicles via self-assembly with desired size and membrane structure.