Adding an unnatural covalent bond to proteins through proximity-enhanced bioreactivity.

Journal: 
Nat Methods
Publication Year: 
2013
Authors: 
Zheng Xiang
Haiyan Ren
Ying S Hu
Irene Coin
Jing Wei
Hu Cang
Lei Wang
PubMed link: 
23913257
Public Summary: 
Natural proteins often rely on the disulfide bond to covalently link side chains. Here we genetically introduce a new type of covalent bond into proteins by enabling an unnatural amino acid to react with a proximal cysteine. We demonstrate the utility of this bond for enabling irreversible binding between an affibody and its protein substrate, capturing peptide-protein interactions in mammalian cells, and improving the photon output of fluorescent proteins.
Scientific Abstract: 
Natural proteins often rely on the disulfide bond to covalently link side chains. Here we genetically introduce a new type of covalent bond into proteins by enabling an unnatural amino acid to react with a proximal cysteine. We demonstrate the utility of this bond for enabling irreversible binding between an affibody and its protein substrate, capturing peptide-protein interactions in mammalian cells, and improving the photon output of fluorescent proteins.