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Related Concept Videos

Oligosaccharide Assembly01:24

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.
Multiple sugar molecules that may or may...
Protein Glycosylation01:25

Protein Glycosylation

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.
Glycosylation occurs in...
Proteoglycans01:05

Proteoglycans

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,...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

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Related Experiment Video

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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

Glycosylation mediated-BAIL in aqueous solution.

Sébastien Delacroix1, Jean-Pierre Bonnet, Matthieu Courty

  • 1Laboratoire des Glucides CNRS FRE3517, 33 rue Saint-Leu, 80039 Amiens, France; Laboratoire de Réactivité et de Chimie des Solides UMR7314, 33 rue Saint-Leu, 80039 Amiens, France; Institut de Chimie de Picardie FR3085, 33 rue Saint-Leu, 80000 Amiens, France.

Carbohydrate Research
|September 24, 2013
PubMed
Summary

Brønsted acid ionic liquid (BAIL) catalysts efficiently activate unreactive glycosyl donors in water. This groundbreaking study demonstrates BAILs for glycosylation in aqueous solutions, offering a greener approach.

Keywords:
Aqueous mediaBrønsted acid ionic liquidGlycosylationTetrazole

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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

Area of Science:

  • Organic Chemistry
  • Green Chemistry
  • Carbohydrate Chemistry

Background:

  • Glycosylation reactions are crucial in synthesizing complex carbohydrates.
  • Activating unreactive glycosyl donors often requires harsh conditions or protecting groups.
  • Developing efficient catalytic systems for glycosylation in aqueous media remains a challenge.

Purpose of the Study:

  • To demonstrate the efficacy of Brønsted acid ionic liquids (BAILs) as catalysts for glycosyl donor activation.
  • To achieve glycosylation reactions in aqueous solution for the first time using BAILs.
  • To explore a greener and more sustainable approach to glycosylation.

Main Methods:

  • Utilized various Brønsted acid ionic liquids as catalysts.
  • Employed unreactive and unprotected glycosyl donors.
  • Conducted reactions in aqueous solution.

Main Results:

  • Successfully activated unreactive and unprotected glycosyl donors using BAILs.
  • Achieved glycosylation in aqueous solution, a novel approach.
  • Demonstrated the catalytic activity of BAILs in promoting glycosidic bond formation.

Conclusions:

  • Brønsted acid ionic liquids are effective catalysts for activating challenging glycosyl donors.
  • Aqueous glycosylation is feasible using BAILs, offering environmental benefits.
  • This work opens new avenues for sustainable carbohydrate synthesis.