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Protein Glycosylation01:25

Protein Glycosylation

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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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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
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Regenerative Glycosylation.

Yashapal Singh1, Tinghua Wang1, Scott A Geringer1

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This study introduces 3,3-difluoroxindole (HOFox) for efficient glycosylation reactions, enhancing yields and reducing times. The method proves particularly effective for challenging glycosyl donors and acceptors, enabling complex oligosaccharide synthesis.

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Area of Science:

  • Carbohydrate Chemistry
  • Organic Synthesis
  • Medicinal Chemistry

Background:

  • 3,3-difluoroxindole (HOFox) has emerged as a valuable reagent in glycosylation chemistry.
  • 3,3-difluoro-3H-indol-2-yl (OFox) imidates are key intermediates in HOFox-mediated glycosylations.
  • Regenerative synthesis strategies for OFox imidates have been previously established.

Purpose of the Study:

  • To extend the application of HOFox-mediated glycosylation to diverse sugar series.
  • To evaluate the impact of HOFox on reaction efficiency, including yield and reaction time.
  • To demonstrate the utility of this method in the synthesis of complex oligosaccharides.

Main Methods:

  • Utilizing 3,3-difluoroxindole (HOFox) as a promoter for glycosidic bond formation.
  • Employing in situ synthesis and activation of 3,3-difluoro-3H-indol-2-yl (OFox) imidates.
  • Applying the methodology across various glycosyl donors and acceptors, including challenging substrates.

Main Results:

  • Achieved enhanced yields and/or reduced reaction times for a variety of glycosylations.
  • Demonstrated the pronounced efficacy of HOFox in reactions involving unreactive glycosyl donors and/or acceptors.
  • Successfully executed a multistep regenerative synthesis of oligosaccharides.

Conclusions:

  • HOFox-mediated glycosylation offers a versatile and efficient approach for constructing diverse glycosidic linkages.
  • The method significantly improves glycosylation outcomes, especially for sterically hindered or electronically deactivated substrates.
  • This work provides a robust platform for the synthesis of complex carbohydrates and oligosaccharides.