Volume 87 Issue 9 | p. 39 | Concentrates
Issue Date: March 2, 2009

Streamlined Way To Label Glycoproteins

A novel technique for labeling sialylated glycoproteins on animal cell surfaces could have advantages for using proteins to diagnose diseases
Department: Science & Technology
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TAGGED
Periodate oxidation and aniline-catalyzed oxime ligation add biotin tags to sialylated glycoproteins in living cells; green ovals are glycoproteins located in the cell membrane.
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TAGGED
Periodate oxidation and aniline-catalyzed oxime ligation add biotin tags to sialylated glycoproteins in living cells; green ovals are glycoproteins located in the cell membrane.

A novel method for labeling sialylated glycoproteins on animal cell surfaces could have important advantages for glycoproteomics—population studies of glycosylated proteins for cancer diagnostics and other applications (Nat. Methods, DOI: 10.1038/nmeth.1305). In current labeling techniques, reactive groups such as alkynes are introduced into cells as reagent-derivatized substrates that are taken up and incorporated into cell glycoproteins during biosynthesis. The new approach, developed by Philip E. Dawson, James C. Paulson, and coworkers at Scripps Research Institute, is the first to efficiently label cellular glycoproteins by direct synthesis. The researchers use periodate oxidation of diols in conjunction with aniline-catalyzed oxime ligation to add biotin tags to sialic acids on cell glycoproteins. The method is inexpensive and nontoxic, doesn't require growing cells in the presence of reagent- derivatized sugar precursors, and achieves 10- to 100-fold higher levels of labeling than with biosynthetic techniques.

 
Chemical & Engineering News
ISSN 0009-2347
Copyright © American Chemical Society

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