Massachusetts Institute of Technology, Department of Chemistry, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Chem Commun (Camb). 2021 Apr 4;57(26):3227-3230. doi: 10.1039/d1cc00095k. Epub 2021 Mar 1.
We report aqueous, site-selective modification of proteins using a reactive peptide interface comprising a nine-residue sequence. This interface is the fastest (second-order rate constant of 152 M s) catalyst-free, cysteine-based method for modifying proteins available to date, and enables near-quantitative labeling of antibodies in cell lysate.
我们报告了使用包含九残基序列的反应性肽界面，对蛋白质进行水相、位点选择性修饰。这种界面是目前为止最快的（二阶速率常数为 152 M s）、无催化剂、基于半胱氨酸的蛋白质修饰方法，可实现细胞裂解物中抗体的近乎定量标记。
