A Straight Path to Circular Proteins
A Straight Path to Circular Proteins
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DOI：
10.1074/jbc.m901752200
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发表时间：
2009-06-05
影响因子：
4.8
通讯作者：
Ploegh, Hidde L.
中科院分区：
文献类型：
--
作者：
Antos, John M.;Popp, Maximilian Wei-Lin;Ploegh, Hidde L.
折叠和稳定性是控制蛋白质行为的参数。赋予蛋白质额外稳定性的可能性对它们在体内的使用和实验室中的结构分析具有重要意义。环状多肽的大小从14到78个氨基酸不等，是天然存在的，与线性多肽相比，它们往往具有更强的抗变性和蛋白水解性。天然的化学连接和基于内含素的方法可以生产更大蛋白质的环状衍生物，从而改善稳定性和复性。在这里，我们表明，环状蛋白可以通过索尔特酶催化的环化反应以极高的效率可逆地制备，只需要对被环化的蛋白质进行最小的修饰。
Folding and stability are parameters that control protein behavior. The possibility of conferring additional stability on proteins has implications for their use in vivo and for their structural analysis in the laboratory. Cyclic polypeptides ranging in size from 14 to 78 amino acids occur naturally and often show enhanced resistance toward denaturation and proteolysis when compared with their linear counterparts. Native chemical ligation and intein-based methods allow production of circular derivatives of larger proteins, resulting in improved stability and refolding properties. Here we show that circular proteins can be made reversibly with excellent efficiency by means of a sortase-catalyzed cyclization reaction, requiring only minimal modification of the protein to be circularized.