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Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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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.
Multiple sugar molecules that may or may...
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Updated: Jun 27, 2025

Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+
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Precise Structural Analysis of Neutral Glycans Using Aerolysin Mutant T240R Nanopore.

Wenqi Lu1,2, Xinjia Zhao1, Minmin Li1

  • 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.

ACS Nano
|May 2, 2024
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel method using nanopore technology and an R-binaphthyl tag to detect and distinguish neutral glycans, including isomers, with single-monosaccharide resolution. This breakthrough advances glycan analysis and structural determination.

Keywords:
biosensingglycanmolecular dynamicsmutantnanoporestructure analysis

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Area of Science:

  • Biochemistry and Molecular Biology
  • Analytical Chemistry
  • Nanotechnology

Background:

  • Glycans are crucial for multicellular organism functions, but their structural complexity and heterogeneity have hindered research compared to DNA and proteins.
  • Existing glycan analysis methods face challenges due to structural isomerism and the lack of high-efficiency techniques.
  • Nanopore technology offers sensitive single-molecule detection but struggles with small, uncharged glycans.

Purpose of the Study:

  • To develop a method for detecting and distinguishing neutral glycans using nanopore technology.
  • To overcome the limitations of analyzing small, uncharged glycan molecules.
  • To enable high-resolution analysis of glycan structural isomers.

Main Methods:

  • Derivatization of glycans with an R-binaphthyl tag to enhance interaction with the nanopore.
  • Utilizing an aerolysin nanopore (specifically the T240R mutant) for single-molecule detection.
  • Employing molecular docking simulations to understand interaction mechanisms and translocation dynamics.

Main Results:

  • Successful detection of neutral glycans, including di-, tri-, and tetrasaccharides, with single-monosaccharide resolution.
  • Unambiguous identification of six disaccharide isomers and linkage isomers of trisaccharides and tetrasaccharides.
  • Demonstration of the kinetic translocation process, revealing interactions that slow glycan passage through the nanopore.

Conclusions:

  • The R-binaphthyl tagging strategy effectively enables nanopore detection of neutral glycans and their isomers.
  • This method provides a robust theoretical and experimental foundation for nanopore-based glycan structural analysis.
  • The technology holds significant potential for advancing glycan structural determination and sequencing.