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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Veröffentlicht in:	Nature methods Jg. 10; H. 9; S. 885 - 888
Hauptverfasser:	Xiang, Zheng, Ren, Haiyan, Hu, Ying S, Coin, Irene, Wei, Jing, Cang, Hu, Wang, Lei
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	New York Nature Publishing Group US 01.09.2013 Nature Publishing Group
Schlagworte:	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-Zugang:	Volltext
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Zusammenfassung:	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.
Bibliographie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 These authors contributed equally to this work.
ISSN:	1548-7091 1548-7105 1548-7105
DOI:	10.1038/nmeth.2595