Presentation and Detection of Azide Functionality in Bacterial Cell Surface Proteins
- 3 August 2004
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 126 (34), 10598-10602
- https://doi.org/10.1021/ja047629c
Abstract
An improved protocol for copper-catalyzed triazole formation on the bacterial cell surface is described. Addition of highly pure CuBr to cells treated with azidohomoalanine (2) leads to ca. 10-fold more extensive cell surface labeling than previously observed. This highly active catalyst allows detection of the methionine analogues azidoalanine (1), azidonorvaline (3), and azidonorleucine (4) in cell surface proteins. Azidoalanine was previously believed to be silent with regard to the cellular protein synthesis machinery.Keywords
This publication has 10 references indexed in Scilit:
- Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli -expressed librariesProceedings of the National Academy of Sciences, 2004
- Activity-Based Protein Profiling in Vivo Using a Copper(I)-Catalyzed Azide-Alkyne [3 + 2] CycloadditionJournal of the American Chemical Society, 2003
- Wildlife and Pastoral Society—Shifting Paradigms in Disease ControlAnnals of the New York Academy of Sciences, 2002
- A Stepwise Huisgen Cycloaddition Process: Copper(I)-Catalyzed Regioselective “Ligation” of Azides and Terminal AlkynesAngewandte Chemie-International Edition, 2002
- A Designed Phenylalanyl-tRNA Synthetase Variant Allows Efficient in Vivo Incorporation of Aryl Ketone Functionality into ProteinsJournal of the American Chemical Society, 2002
- Biosynthesis of Proteins Incorporating a Versatile Set of Phenylalanine AnaloguesChemBioChem, 2002
- Identification of an expanded set of translationally active methionine analogues in Escherichia coliFEBS Letters, 2001
- Improved Solid-Phase Peptide Synthesis Method Utilizing α-Azide-Protected Amino AcidsOrganic Letters, 2001
- Expanding the Scope of Protein Biosynthesis by Altering the Methionyl-tRNA Synthetase Activity of a Bacterial Expression HostAngewandte Chemie-International Edition, 2000
- Expansion of the genetic code: Site‐directed p‐fluoro‐phenylalanine incorporation in Escherichia coliProtein Science, 1998