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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

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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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Biosynthesis of Polysaccharides01:26

Biosynthesis of Polysaccharides

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Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...
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Peptidoglycan Synthesis01:28

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Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan...
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Proteoglycans01:05

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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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Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
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Recent advances in glycan synthesis.

Bo-Han Li1, Xin-Shan Ye2

  • 1Institute of Systems Biomedicine, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China.

Current Opinion in Chemical Biology
|June 2, 2020
PubMed
Summary

Scientists are advancing complex carbohydrate (glycan) synthesis through chemical, chemoenzymatic, and automated methods. Recent progress focuses on efficient glycosylation, stereoselectivity, and assembling intricate glycan chains for life science applications.

Keywords:
CarbohydrateChemical synthesisChemoenzymatic synthesisOligosaccharidePolysaccharideReview

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Area of Science:

  • Carbohydrate Chemistry
  • Glycoscience
  • Organic Synthesis

Background:

  • Carbohydrates (glycans) are crucial in life sciences but challenging to synthesize due to complex structures.
  • Overcoming synthetic hurdles in glycan assembly is a persistent goal for researchers.

Purpose of the Study:

  • To provide an overview of recent advancements in glycan synthesis.
  • To highlight progress in chemical, chemoenzymatic, and automated synthesis strategies.
  • To focus on efficiency, stereoselectivity, and complex glycan assembly.

Main Methods:

  • Review of chemical synthesis approaches.
  • Exploration of chemoenzymatic strategies.
  • Discussion of automated glycan synthesis platforms.

Main Results:

  • Recent developments show improved efficiency in glycosylation methods.
  • Enhanced stereoselectivity in forming glycosidic linkages has been achieved.
  • New methods facilitate the assembly of complex glycan structures.

Conclusions:

  • Significant progress has been made in overcoming challenges in glycan synthesis.
  • The discussed methods offer improved control over efficiency and stereoselectivity.
  • These advancements are key to assembling complex glycans for diverse life science applications.