Chemical protein synthesis elucidates key modulation mechanism of the tyrosine-O-sulfation in inducing strengthened inhibitory activity of hirudin  

作　　者：Ye Yang Mingchan Liang Rui Wang Chunmao He 

机构地区：[1]School of Chemistry and Chemical Engineering,South China University of Technology,Guangzhou 510640,China [2]Pingshan translational medicine center,Shenzhen Bay Laboratory,Shenzhen 518118,China

出　　处：《Chinese Chemical Letters》2023年第5期213-216,共4页中国化学快报（英文版）

基　　金：The financial support from the National Natural Science Foundation of China(Nos.91853117 and 22077036);the Natural Science Foundation of Guangdong Province(No.2020A1515010766)are greatly acknowledged。

摘　　要：Tyrosine sulfation is an important post-translational modification that enhances the inhibitory activity of hirudin.Herein,we developed a facile synthetic strategy to afford the sulfated hirudins with up to three modifications and in multi-milligram scales,after a single HPLC purification step.Through these synthetic proteins,a novel type of modulation mechanism exhibited by tyrosine sulfation was proposed,which would help to delineate the structure-function relationships in other sulfated proteins and more importantly,to serve as a basis for the development of related antithrombotic agents.

关 键 词：Tyrosine sulfation HIRUDIN Chemical protein synthesis Post-translational modification Native chemical ligation 

分 类 号：TQ460.1[化学工程—制药化工]