Journal of the American Chemical Society
Communication
Author Contributions
‡These authors contributed equally to this work.
Notes
The authors declare no competing financial interest.
ACKNOWLEDGMENTS
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We thank Rochelle Diamond at the Caltech Flow Cytometry
Cell Sorting Facility, Dr. Mona Shahgholi in the CCE Division
Mass Spectrometry Facility, and The Consortium for Func-
tional Glycomics, Core D and H (NIGMS GM62116), and also
Dr. Peng George Wang for providing the BgtA vector. This
work was supported by grants from the NIH (R01 GM084724
to L.C.H.−W. and NIH/NRSA 5T32 GM07616 to C.K. and
J.C.).
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demonstrate that our chemoenzymatic labeling approach can
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histological detection, our chemoenzymatic approach could
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of Fucα(1-2)Gal glycosylation.12
In conclusion, we have developed a new chemoenzymatic
strategy that detects Fucα(1-2)Gal glycans with improved
efficiency and selectivity over existing methods. Our strategy
detects a variety of complex Fucα(1-2)Gal glycans and
glycoproteins and permits living cells or complex tissue extracts
to be rapidly interrogated. We anticipate that the strategy will
accelerate both the discovery of new Fucα(1-2)Gal glyco-
proteins and advance an understanding of the biological roles of
this important sugar in neurobiology and cancer. Moreover, this
study represents a proof-of-concept that chemoenzymatic
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ASSOCIATED CONTENT
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S
* Supporting Information
Figures and detailed experimental procedures, including the
synthesis of 1, chemoenzymatic labeling reactions, LC−MS
analyses, detection of glycoproteins, immunostaining, flow
cytometry analysis, and complete refs 9 and 11. This material is
(11) Schroder, F. H.; et al. N. Engl. J. Med. 2009, 360, 1320.
̈
AUTHOR INFORMATION
́
(12) Peracaula, R.; Tabares, G.; Royle, L.; Harvey, D. J.; Dwek, R. A.;
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Rudd, P. M.; de Llorens, R. Glycobiology 2003, 13, 457.
Corresponding Author
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dx.doi.org/10.1021/ja211312u | J. Am. Chem. Soc. 2012, 134, 4489−4492