Chemical methods for O-GlcNAc detection and preparation of O-GlcNAc modified proteins
- 1Department of Chemistry, University of Southern California, Los Angeles, California, 90089, United States
Abstract
Chemistry, through the synthesis of a radioactive sugar-donor, played a critical role in the discovery of O-GlcNAc and has been contributing indispensable tools ever since. Here, we cover where chemical methods have contributed to both the discovery and characterization of O-GlcNAc modifications. We will first discuss metabolic labeling and chemoenzymatic modification as two techniques that leverage the power of bioorthogonal chemistry to visualize, enrich, and even quantify O-GlcNAc modifications from living systems. We will then describe how solid-phase peptide synthesis can be combined with protein ligation methods as the only current pathway to homogeneously O-GlcNAc-modified proteins for downstream biological experiments. In each section, we point out the positives and considerations for each approach and provide protocols for normalization of best practices across the field.
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BibTeX
@article{hayniecion2026chemical,
title = {{Chemical methods for O-GlcNAc detection and preparation of O-GlcNAc modified proteins}},
author = {Rhianna L. Haynie-Cion and Michelle Marie B. Helmeke and Dongning Liu and Jack T. Swanson and Matthew R. Pratt},
journal = {Glycobiology},
year = {2026},
month = oct,
doi = {10.1093/glycob/cwag095},
url = {https://doi.org/10.1093/glycob/cwag095},
note = {CC BY},
}
RIS
TY - JOUR
TI - Chemical methods for O-GlcNAc detection and preparation of O-GlcNAc modified proteins
AU - Rhianna L. Haynie-Cion
AU - Michelle Marie B. Helmeke
AU - Dongning Liu
AU - Jack T. Swanson
AU - Matthew R. Pratt
PY - 2026
DA - 2026/10/09
JO - Glycobiology
DO - 10.1093/glycob/cwag095
UR - https://doi.org/10.1093/glycob/cwag095
AB - Chemistry, through the synthesis of a radioactive sugar-donor, played a critical role in the discovery of O-GlcNAc and has been contributing indispensable tools ever since. Here, we cover where chemical methods have contributed to both the discovery and characterization of O-GlcNAc modifications. We will first discuss metabolic labeling and chemoenzymatic modification as two techniques that leverage the power of bioorthogonal chemistry to visualize, enrich, and even quantify O-GlcNAc modifications from living systems. We will then describe how solid-phase peptide synthesis can be combined with protein ligation methods as the only current pathway to homogeneously O-GlcNAc-modified proteins for downstream biological experiments. In each section, we point out the positives and considerations for each approach and provide protocols for normalization of best practices across the field.
SN - 0959-6658
SN - 1460-2423
ER -