通过噻唑烷形成将1,2-氨基硫醇官能团进行基因整合用于位点特异性蛋白质修饰。
Genetic incorporation of 1,2-aminothiol functionality for site-specific protein modification via thiazolidine formation.
作者信息
Bi Xiaobao, Pasunooti Kalyan Kumar, Tareq Ahmad Hussen, Takyi-Williams John, Liu Chuan-Fa
机构信息
Division of Structural Biology and Biochemistry, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.
出版信息
Org Biomol Chem. 2016 Jun 21;14(23):5282-5. doi: 10.1039/c6ob00854b. Epub 2016 May 20.
Here we report a new site-specific conjugation strategy to modify proteins via thiazolidine ligation. Proteins harbouring a 1,2-aminothiol moiety introduced by amber codon suppression technology could be modified chemoselectively with aldehyde-functionalized reagents, such as a biotin-labeled peptide or ubiquitin, under mild conditions to yield homogeneous biotinylated or ubiquitinated products.
在此，我们报道了一种通过噻唑烷连接修饰蛋白质的新的位点特异性共轭策略。利用琥珀密码子抑制技术引入1,2-氨基硫醇部分的蛋白质，可在温和条件下与醛功能化试剂（如生物素标记的肽或泛素）进行化学选择性修饰，以产生均一的生物素化或泛素化产物。
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