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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.
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Protein Glycosylation01:25

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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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Glyco-macroligand microarray with controlled orientation and glycan density.

Satya Nandana Narla1, Xue-Long Sun

  • 1Department of Chemistry, Cleveland State University, Cleveland, OH 44115, USA.

Lab on a Chip
|March 17, 2012
PubMed
Summary

We developed a new glycan microarray using temporary spacers to control glycan density and orientation. This method enhances lectin binding, offering a versatile tool for glycan recognition studies.

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Area of Science:

  • Carbohydrate Chemistry
  • Surface Chemistry
  • Biomaterials Science

Background:

  • Glycan microarrays are crucial for understanding carbohydrate-protein interactions.
  • Controlling glycan density and orientation is essential for accurate binding studies.
  • Existing methods often lack precise control over these parameters.

Purpose of the Study:

  • To develop a novel glycan microarray platform enabling controlled glycan density and orientation.
  • To investigate the impact of glycan spacing on lectin binding affinity.
  • To establish a versatile tool for glycan recognition profiling.

Main Methods:

  • End-point immobilization of glycopolymer with detachable macromolecular spacers (polyacrylamide-BA, lysozyme-BA, BSA-BA).
  • Formation of isourea bonds on amine-functionalized glass slides at pH 10.3.
  • Detachment of spacers at pH 7.4 to create oriented and density-controlled glycopolymer microarrays.
  • Analysis of lectin (Arachis hypogaea) binding using surface plasmon resonance (SPR).

Main Results:

  • The spaced glycopolymer microarray demonstrated enhanced lectin binding compared to non-spaced arrays.
  • Polyacrylamide-BA spaced arrays exhibited the highest lectin binding.
  • SPR confirmed density-dependent lectin binding trends.
  • The platform allows tunable glycan density, glycopolymer density, and orientation.

Conclusions:

  • The developed glyco-macroligand microarray platform provides precise control over glycan presentation.
  • This method significantly enhances lectin binding detection.
  • The platform is a versatile tool for glycan recognition profiling in biological research and applications.