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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.
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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.
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Related Experiment Video

Updated: Jun 15, 2025

Hierarchical and Programmable One-Pot Oligosaccharide Synthesis
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Precise AIE-Based Ternary Co-Assembly for Saccharide Recognition and Classification.

Yongxin Chang1,2, Juan Shao1, Xinjia Zhao1

  • 1State Key Laboratory of Medical Proteomics, National Chromatographic R. & A. Center, CAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, P. R. China.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|August 28, 2024
PubMed
Summary

This study introduces a novel strategy for saccharide recognition using a halogen ion-driven aggregation-induced emission module. The method precisely identifies diverse saccharides, including isomers, via self-assembly and fluorescence enhancement.

Keywords:
aggregation‐induced emissionarray sensorco‐assemblysaccharide recognition

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Area of Science:

  • Carbohydrate Chemistry
  • Supramolecular Chemistry
  • Analytical Chemistry

Background:

  • Saccharides play crucial roles in biological processes.
  • Selective recognition of diverse saccharide structures remains a significant challenge.
  • Conventional receptor designs are often complex and delicate.

Purpose of the Study:

  • To develop a novel and precise ternary co-assembled strategy for saccharide recognition.
  • To overcome the limitations of conventional complex receptor designs.
  • To create an adaptable sensor for saccharide classification and analysis.

Main Methods:

  • Utilized a halogen ion-driven aggregation-induced emission module (p-Toluidine, N, N'-1-propen-1-yl-3-ylidene hydrochloride - PN-Tol).
  • Employed a ternary co-assembly strategy involving PN-Tol and 4-mercaptophenylboronic acid (MPBA).
  • Investigated the formation of microstructures and fluorescence enhancement upon saccharide binding.

Main Results:

  • Achieved specific binding of PN-Tol to MPBA, forming highly ordered co-assemblies.
  • Observed heterogeneous ternary assembly behaviors with various saccharides, forming distinct microstructures (cluster-like, spherical, rod-like).
  • Demonstrated significant fluorescence enhancement and successful classification of diverse saccharides, including epimers and optical isomers, using an array sensor.

Conclusions:

  • The novel ternary co-assembly strategy offers a precise and adaptable approach to saccharide recognition.
  • The developed sensor enables effective classification and analysis of various saccharides.
  • This strategy opens new avenues for saccharide analysis and sequencing.