Premium
A Biocompatible Condensation Reaction for the Labeling of Terminal Cysteine Residues on Proteins
Author(s) -
Ren Hongjun,
Xiao Fei,
Zhan Ke,
Kim YoungPil,
Xie Hexin,
Xia Zuyong,
Rao Jianghong
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200903627
Subject(s) - cysteine , rhodamine , chemistry , residue (chemistry) , in vitro , biochemistry , fluorescence , amino acid residue , condensation reaction , combinatorial chemistry , molecule , biophysics , peptide sequence , organic chemistry , biology , catalysis , enzyme , physics , quantum mechanics , gene
Going live : A protein‐labeling method based on the use of a single amino acid tag—an N‐terminal cysteine residue—and small‐molecule probes containing a cyanobenzothiazole (CBT) unit has been used for the specific fluorescence labeling of proteins in vitro and at the surface of live cells (see scheme). This simple ligation reaction proceeds with a high degree of specificity under physiological conditions. Rd: a rhodamine dye; TEV: tobacco etch virus.