Presentation and detection of azide functionality in bacterial cell surface proteins

A. James Link; Mandy K.S. Vink; David A. Tirrell

doi:10.1021/ja047629c

Presentation and detection of azide functionality in bacterial cell surface proteins

A. James Link, Mandy K.S. Vink, David A. Tirrell

Research output: Contribution to journal › Article › peer-review

294 Scopus citations

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.

Original language	English (US)
Pages (from-to)	10598-10602
Number of pages	5
Journal	Journal of the American Chemical Society
Volume	126
Issue number	34
DOIs	https://doi.org/10.1021/ja047629c
State	Published - Sep 1 2004
Externally published	Yes

All Science Journal Classification (ASJC) codes

General Chemistry
Biochemistry
Catalysis
Colloid and Surface Chemistry

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10.1021/ja047629c

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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.",

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AU - Vink, Mandy K.S.

AU - Tirrell, David A.

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N2 - 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.

AB - 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.

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

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Presentation and detection of azide functionality in bacterial cell surface proteins

Abstract

All Science Journal Classification (ASJC) codes

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