Protein Catenation Enhances Both the Stability and Activity of Folded Structural Domains
Protein Catenation Enhances Both the Stability and Activity of Folded Structural Domains
复制标题
蛋白质链连接增强折叠结构域的稳定性和活性
DOI：
10.1002/anie.201705194
复制
发表时间：
2017
期刊：
影响因子：
--
通讯作者：
Zhang Wen-Bin
中科院分区：
文献类型：
--
作者：
Wang Xiao-Wei;Zhang Wen-Bin
链烯是具有独特性质的有趣分子结构。在这里，我们报告的细胞合成的蛋白链烷含有折叠的结构域，辅助p53二聚化和SpyTag/SpyCatcher化学之间的协同作用。显示绿色荧光蛋白（GFP）的串联增加化学稳定性而不破坏荧光性质，并且串联的二氢叶酸还原酶（DHFR）表现出比野生型DHFR和环状/线性对照高约4 °C的解链温度和高约27%的催化活性。链化还赋予DHFR相当大的蛋白水解抗性。结果表明，连接可以提高折叠蛋白质的稳定性和活性，从而使拓扑工程的一个有吸引力的方法来定制蛋白质的性质，而不改变其天然序列。
Catenanes are intriguing molecular architectures with unique properties. Herein, we report the cellular synthesis of protein catenanes containing folded structural domains, aided by synergy between p53 dimerization and SpyTag/SpyCatcher chemistry. Concatenation of green fluorescent protein (GFP) was shown to increase chemical stability without disrupting the fluorescence properties, and concatenated dihydrofolate reductase (DHFR) exhibited a melting temperature around 4 °C higher and catalytic activity around 27 % higher than the wild‐type DHFR and the cyclic/linear controls. Catenation also confers considerable proteolytic resistance on DHFR. The results suggest that catenation could enhance both the stability and activity of folded proteins, thus making topology engineering an attractive approach for tailoring protein properties without varying their native sequences.