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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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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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Molecularly imprinted materials for glycan recognition and processing.

Yan Zhao1

  • 1Department of Chemistry, Iowa State University, Ames, Iowa 50011-3111, USA. zhaoy@iastate.edu.

Journal of Materials Chemistry. B
|April 28, 2022
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Summary
This summary is machine-generated.

Researchers developed novel synthetic materials for binding and processing carbohydrates (glycans). These molecularly imprinted materials show potential to rival natural proteins in biological applications and advance glycobiology research.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Synthetic Chemistry

Background:

  • Carbohydrates (glycans) are abundant and crucial in biological processes like cell adhesion, infections, inflammation, and cancer.
  • Glycosylation is the most common protein posttranslational modification.
  • Molecular imprinting technology has been historically applied to glycosides.

Purpose of the Study:

  • To highlight recent advancements in molecularly imprinted materials designed for glycan binding and processing.
  • To showcase synthetic alternatives to natural carbohydrate-binding proteins (lectins) and enzymes (glycosidases).

Main Methods:

  • Development of novel imprinting techniques for creating glycan-binding materials.
  • Application of postmodification strategies to enhance material properties.
  • Evaluation of synthetic materials' affinity and hydrolytic capabilities for complex glycans.

Main Results:

  • Creation of synthetic glycan-binding materials with high affinity, comparable to natural lectins.
  • Development of artificial glycosidases capable of selective complex glycan hydrolysis.
  • Demonstration of molecularly imprinted materials as effective tools for glycan manipulation.

Conclusions:

  • Advanced molecular imprinting techniques yield synthetic materials for glycan binding and processing.
  • These novel materials offer promising alternatives to natural biomolecules in glycochemistry and glycobiology.
  • The developed materials are expected to drive progress in glycochemistry, glycobiology, and biomass conversion.