Published September 1, 2004
| public
Journal Article
Presentation and Detection of Azide Functionality in Bacterial Cell Surface Proteins
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.
Additional Information
Copyright © 2004 American Chemical Society. Published In Issue September 01, 2004. Publication Date (Web): August 3, 2004. Received April 23, 2004. Acknowledgment. We thank Timothy Chan and Profs. Valery Fokin and K. Barry Sharpless for their gift of compound 5. We are grateful to Han Peeters and Mona Shahgoli for assistance with mass spectrometry. We also thank Prof. Richard Roberts for use of his cell sorter. This work was supported by the ARO Institute for Collaborative Biotechnologies (Grant No. DAAD19- 03-D-0004), the NSF Center for the Science and Engineering of Materials (Grant No. DMR 008 0065), NIH Grant GM62523, and the Beckman Institute at the California Institute of Technology. A.J.L. is an NSF Graduate Research Fellow. M.K.S.V. was supported by a grant from The Netherlands Organization for Scientific Research.Additional details
- Eprint ID
- 53817
- Resolver ID
- CaltechAUTHORS:20150116-102630933
- U.S. Army Research Office. Institute for Collaborative Biotechnologies
- DAAD19- 03-D-0004
- NSF Center for the Science and Engineering of Materials
- DMR 008 0065
- NIH
- GM62523
- Beckman Institute at Caltech
- NSF Graduate Research Fellowship
- Netherlands Organization for Scientific Research (NWO)
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2015-01-16Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field