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Protein Glycosylation

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...

Oligosaccharide Assembly

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...

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Related Experiment Video

Updated: Jun 4, 2026

Hierarchical and Programmable One-Pot Oligosaccharide Synthesis

Hierarchical and Programmable One-Pot Oligosaccharide Synthesis

Published on: September 6, 2019

Programmable one-pot glycosylation.

Chung-Yi Wu¹, Chi-Huey Wong

¹Genomics Research Center, Academia Sinica, Nankang, Taipei 115, Taiwan. cyiwu@gate.sinica.edu.tw

Topics in Current Chemistry

|February 4, 2011

Summary

This summary is machine-generated.

Programmable one-pot synthesis enables efficient oligosaccharide construction by sequentially activating thioglycoside building blocks. This strategy allows for rapid synthesis of diverse oligosaccharides and glycoconjugates for disease research.

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Area of Science:

Carbohydrate Chemistry
Organic Synthesis
Glycobiology

Background:

Oligosaccharide synthesis requires precise control over regio- and stereochemistry.
Traditional methods involve complex multi-step procedures with intermediate purifications.

Purpose of the Study:

To present a programmable one-pot synthesis strategy for oligosaccharides.
To highlight the application of this method for synthesizing diverse oligosaccharides and glycoconjugates.

Main Methods:

Sequential activation of thioglycoside building blocks based on reactivity differences.
Utilizing modified protecting group strategies and neighboring group participation to control anomeric activation.
Performing sequential glycosylation reactions in a single vessel without intermediate purification.

Main Results:

Demonstrated rapid access to oligosaccharides with high molecular diversity.
Successfully applied the reactivity-based strategy to one-pot glycosylation reactions.
Enabled synthesis of oligosaccharides and glycoconjugates relevant to infectious diseases and cancer antigens.

Conclusions:

Programmable one-pot synthesis offers an efficient and versatile approach to complex carbohydrate synthesis.
This strategy simplifies the production of oligosaccharides and glycoconjugates for biomedical applications.
The method facilitates the generation of molecular diversity crucial for studying carbohydrate-related diseases.