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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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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.
Glycosylation occurs in...
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Proteoglycans01:05

Proteoglycans

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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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Intramolecular Aldol Reaction01:18

Intramolecular Aldol Reaction

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Intramolecular aldol reaction occurs in dicarbonyl compounds such as dialdehydes, diketones, and keto-aldehydes. The dicarbonyl compounds possess more than one nucleophilic ⍺ carbon for the base to deprotonate and form the enolates. For example, in symmetrical diketones, there are four ⍺ carbons. Hence, four types of enolates are possible when treated with a base. However, since the molecule is symmetrical, the enolates formed on either side of one carbonyl group are equivalent to those...
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Membrane Carbohydrates01:30

Membrane Carbohydrates

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The plasma membrane is a dynamic barrier composed of lipids, proteins, and carbohydrates. It is the epicenter of many cellular processes required for cell growth and survival. Carbohydrates have unique structural and chemical properties that help the plasma membrane to carry out its functions effectively.
Membrane carbohydrates do not have any hydrophobic region and are exclusively located on the cell's outer surface. The addition of sugar molecules or glycosylation of proteins happens in...
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Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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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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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

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Intramolecular glycosylation.

Xiao G Jia1, Alexei V Demchenko1

  • 1Department of Chemistry and Biochemistry, University of Missouri - St. Louis, One University Blvd., 434 Benton Hall (MC27), St. Louis, MO 63121, USA.

Beilstein Journal of Organic Chemistry
|October 25, 2017
PubMed
Summary

Synthesizing complex carbohydrate oligomers is difficult. This review explores intramolecular glycosylation methods that improve stereocontrol by linking sugar units, simplifying synthesis.

Keywords:
carbohydratesglycosylationintramolecular reactionsoligosaccharides

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Regioselective O-Glycosylation of Nucleosides via the Temporary 2',3'-Diol Protection by a Boronic Ester for the Synthesis of Disaccharide Nucleosides
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Glycan Node Analysis: A Bottom-up Approach to Glycomics
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Regioselective O-Glycosylation of Nucleosides via the Temporary 2',3'-Diol Protection by a Boronic Ester for the Synthesis of Disaccharide Nucleosides
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Glycan Node Analysis: A Bottom-up Approach to Glycomics
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Area of Science:

  • Carbohydrate Chemistry
  • Organic Synthesis
  • Stereoselective Reactions

Background:

  • Carbohydrate oligomer synthesis presents significant challenges, including complex protecting group strategies, functionalization, purification, and characterization.
  • Achieving high stereocontrol in glycosylation reactions is a primary obstacle in carbohydrate chemistry.

Purpose of the Study:

  • To review methods for intramolecular glycosylation reactions.
  • To highlight strategies for achieving facial stereoselectivity in these reactions.

Main Methods:

  • Overview of intramolecular glycosylation techniques.
  • Discussion of tethering strategies for glycosyl donors and acceptors.

Main Results:

  • Intramolecular glycosylation offers a pathway to enhanced stereocontrol.
  • Tethering donor and acceptor moieties facilitates facial selectivity.

Conclusions:

  • Intramolecular glycosylation represents a promising approach to overcome stereochemical challenges in carbohydrate synthesis.
  • Tethering strategies are key to achieving predictable stereoselectivity in the formation of complex carbohydrates.