Protein-Templated Peptide Ligation**

Protein-Templated Peptide Ligation**
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DOI:
10.1002/anie.201400681
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发表时间:
2014-04-22
影响因子:
16.6
通讯作者:
Grossmann, Tom N.
Grossmann, Tom N.
中科院分区:
化学1区
文献类型:
--
作者:
Brauckhoff, Nicolas;Hahne, Gernot;Grossmann, Tom N.

文献摘要

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分子模板结合了特定的反应物,从而增加了它们的有效浓度并加速了相应的反应。这一概念已经成功地应用于一些化学问题,特别是核酸模板反应。我们提出了第一个蛋白质模板化反应,允许两个肽的N-末端连接。在蛋白质模板的存在下,连接反应加速了三个数量级以上。模板化反应具有很高的选择性,并在粗细胞裂解液中进行的蛋白质标记反应中证明了其稳健性。
Molecular templates bind particular reactants, thereby increasing their effective concentrations and accelerating the corresponding reaction. This concept has been successfully applied to a number of chemical problems with a strong focus on nucleic acid templated reactions. We present the first protein-templated reaction that allows N-terminal linkage of two peptides. In the presence of a protein template, ligation reactions were accelerated by more than three orders of magnitude. The templated reaction is highly selective and proved its robustness in a protein-labeling reaction that was performed in crude cell lysate.