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Updated: May 12, 2026

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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
Published on: December 26, 2011
A Photoactivatable Glycoenzyme Platform for Spatiotemporally Controlled, Protein-Selective, and In Vivo Glycan
Xiaocui Zheng1, Wanqing Wei1,2,3, Changjiang Wang1
1State Key Laboratory of Coordination Chemistry, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210023, China.
Journal of the American Chemical Society
|March 2, 2026
Summary
Researchers developed GLOBE, a platform for optical control of cell-surface sugar modifications. This method uses light to precisely regulate glycoenzyme activity, enabling targeted glycan oxidation and editing in cells and tissues.
Area of Science:
- Biochemistry
- Chemical Biology
- Glycoscience
Background:
- Cell-surface glycosylation is complex and difficult to control precisely.
- Dynamic and spatially intricate nature of glycans presents challenges for targeted manipulation.
Purpose of the Study:
- To present GLOBE, a novel platform for optical regulation of glycoenzyme activity.
- To enable precise, spatiotemporal control over cell-surface glycosylation.
- To demonstrate applications in glycan oxidation, selective targeting, and in vivo editing.
Main Methods:
- Site-specific incorporation of photocaged unnatural amino acids (ONBY) into glycoenzymes (e.g., galactose oxidase).
- Optical activation using light to control enzyme activity.
- Integration with targeting aptamers for protein selectivity.
- Development of photoresponsive cascades for sequential glycan modification.
- Utilizing upconversion nanoparticles for in vivo photoactivation.
Main Results:
- Achieved micrometer-scale spatial and temporal resolution of cell-surface glycan oxidation.
- Demonstrated binding-gated and protein-selective glycan oxidation using MUC1-targeting aptamers.
- Successfully implemented orthogonal photoresponsive cascades for enhanced labeling.
- Enabled in vivo glycan editing in a murine tumor model via nanoparticle-assisted photoactivation.
Conclusions:
- GLOBE offers a modular and programmable framework for probing and manipulating glycosylation.
- Provides precise spatiotemporal control at single-cell and tissue levels.
- Represents a versatile strategy for investigating and engineering the biological sugar code.
Related Concept Videos
Protein Glycosylation
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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Oligosaccharide Assembly
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...

