NDLI: Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation

Content Provider	PubMed Central
Author	Kiick, Kristi L. Saxon, Eliana Tirrell, David A. Bertozzi, Carolyn R.
Copyright Year	2002
Abstract	The introduction of chemically unique groups into proteins by means of non-natural amino acids has numerous applications in protein engineering and functional studies. One method to achieve this involves the utilization of a non-natural amino acid by the cell's native translational apparatus. Here we demonstrate that a methionine surrogate, azidohomoalanine, is activated by the methionyl-tRNA synthetase of Escherichia coli and replaces methionine in proteins expressed in methionine-depleted bacterial cultures. We further show that proteins containing azidohomoalanine can be selectively modified in the presence of other cellular proteins by means of Staudinger ligation with triarylphosphine reagents. Incorporation of azide-functionalized amino acids into proteins in vivo provides opportunities for protein modification under native conditions and selective labeling of proteins in the intracellular environment.
Related Links	http://dx.doi.org/10.1073/pnas.012583299
Ending Page	24
Page Count	6
Starting Page	19
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	1
Volume Number	99
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2002-01-08
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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