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

An unnatural amino acid that forms a covalent bond with a proximal cysteine can be introduced into proteins, facilitating a variety of applications. Natural proteins often rely on the disulfide bond to covalently link side chains. Here we genetically introduce a new type of covalent bond into protei...

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Bibliographic Details
Published in:Nature methods Vol. 10; no. 9; pp. 885 - 888
Main Authors: Xiang, Zheng, Ren, Haiyan, Hu, Ying S, Coin, Irene, Wei, Jing, Cang, Hu, Wang, Lei
Format: Journal Article
Language:English
Published: New York Nature Publishing Group US 01.09.2013
Nature Publishing Group
Subjects:
631/1647/338/469
631/1647/666
631/45/612
631/92/96
Amino Acid Sequence
Amino acids
Amino Acyl-tRNA Synthetases - genetics
Animals
Bioinformatics
Biological Microscopy
Biological Techniques
Biomedical Engineering/Biotechnology
Biomedical research
brief-communication
Cells
Cellular proteins
Chemical bonds
Cysteine - chemistry
Cysteine Endopeptidases - chemistry
Cysteine Endopeptidases - genetics
Cysteine Endopeptidases - metabolism
Escherichia coli - genetics
Fluorescence
Life Sciences
Mammals
Molecular Sequence Data
Mutation
Phenylalanine - analogs & derivatives
Phenylalanine - chemistry
Photons
Physiological aspects
Protein binding
Protein Conformation
Protein Engineering - methods
Proteins
Proteins - chemistry
Proteins - genetics
Proteins - immunology
Proteins - metabolism
Proteomics
Rats
Receptors, Corticotropin-Releasing Hormone - genetics
Receptors, Corticotropin-Releasing Hormone - metabolism
Recombinant Proteins - genetics
Recombinant Proteins - immunology
United States
ISSN:1548-7091, 1548-7105, 1548-7105
Online Access:Get full text
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Description
Summary:An unnatural amino acid that forms a covalent bond with a proximal cysteine can be introduced into proteins, facilitating a variety of applications. 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.
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These authors contributed equally to this work.
ISSN:1548-7091
1548-7105
1548-7105
DOI:10.1038/nmeth.2595