Nanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion.
Nanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion.
复制标题
DOI：
10.1038/ncomms10619
复制
发表时间：
2016-02-10
影响因子：
16.6
通讯作者：
Yan H
中科院分区：
文献类型：
--
作者：
Zhao Z;Fu J;Dhakal S;Johnson-Buck A;Liu M;Zhang T;Woodbury NW;Liu Y;Walter NG;Yan H
细胞通常会对酶进行区室化，以提高其代谢途径的效率。在这里，我们报告了一种通用的方法来构建DNA纳米笼酶，以提高催化活性和稳定性。纳米笼的酶实现了自组装成DNA纳米笼与良好控制的化学计量和架构，使一组常见的代谢酶的封装和近端聚阴离子表面的影响进行了系统的研究。在散装和单分子水平上的活性测定表明，DNA纳米笼封装的酶的底物周转数增加。出乎意料的是，我们观察到蛋白质的大小与其活性增强之间存在显著的负相关性。这种效果是一致的模型，其中远端聚阴离子表面的纳米笼增强活性酶构象的稳定性，通过一个强有力的结合水化层的行动。我们进一步表明，DNA纳米笼保护封装的酶对蛋白酶，证明其在功能性生物材料和生物技术的实用性。 细胞区室化酶以提高其代谢途径的效率。在这里，作者描述了一种自组装方法来构建DNA纳米笼酶，以提高催化活性和稳定性，并观察到蛋白质大小和活性增强之间的反向相关性。
Cells routinely compartmentalize enzymes for enhanced efficiency of their metabolic pathways. Here we report a general approach to construct DNA nanocaged enzymes for enhancing catalytic activity and stability. Nanocaged enzymes are realized by self-assembly into DNA nanocages with well-controlled stoichiometry and architecture that enabled a systematic study of the impact of both encapsulation and proximal polyanionic surfaces on a set of common metabolic enzymes. Activity assays at both bulk and single-molecule levels demonstrate increased substrate turnover numbers for DNA nanocage-encapsulated enzymes. Unexpectedly, we observe a significant inverse correlation between the size of a protein and its activity enhancement. This effect is consistent with a model wherein distal polyanionic surfaces of the nanocage enhance the stability of active enzyme conformations through the action of a strongly bound hydration layer. We further show that DNA nanocages protect encapsulated enzymes against proteases, demonstrating their practical utility in functional biomaterials and biotechnology. Cells compartmentalize enzymes for enhanced efficiency of their metabolic pathways. Here, the authors describe a self-assembly approach to construct DNA nanocaged enzymes for enhancing catalytic activity and stability, and observe an inversed correlation between the protein size and the activity enhancement.