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

被引：0

作者：

Xiang, Zheng ^{[1
]}

Ren, Haiyan ^{[1
]}

Hu, Ying S. ^{[2
]}

Coin, Irene ^{[1
]}

Wei, Jing ^{[3
]}

Cang, Hu ^{[2
]}

Wang, Lei ^{[1
]}

机构：

[1] Salk Inst Biol Studies, Jack H Skirball Ctr Chem Biol & Prote, La Jolla, CA 92037 USA

[2] Salk Inst Biol Studies, Waitt Adv Biophoton Ctr, La Jolla, CA 92037 USA

[3] Jadebio Inc, La Jolla, CA USA

来源：

NATURE METHODS | 2013年 / 10卷 / 09期

基金：

美国国家卫生研究院;

关键词：

ESCHERICHIA-COLI; GENETIC-CODE; AMINO-ACIDS; INHIBITORS; RECEPTORS; MOLECULES; CELLS;

D O I：

10.1038/NMETH.2595

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：885 / +

页数：5

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