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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.
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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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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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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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Glycocalyx and its Functions01:14

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The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
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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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Related Experiment Video

Updated: Dec 11, 2025

Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes
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Self-Assembling Glycopeptide Conjugate as a Versatile Platform for Mimicking Complex Polysaccharides.

Hanxuan Wang1, Zhichao Liu1, Chuanjing An1

  • 1State Key Laboratory of Natural and Biomimetic Drugs and Department of Chemical Biology School of Pharmaceutical Sciences Peking University Beijing 100191 China.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|August 25, 2020
PubMed
Summary

Researchers developed self-assembling glycopeptide conjugates as safe, accessible mimics of complex polysaccharides. A mannosylated version showed immunostimulatory effects in cellular assays and mouse vaccination, highlighting a new carbohydrate-based platform.

Keywords:
glycopeptide conjugatesimmune activationpolysaccharidesself‐assembly

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Area of Science:

  • Carbohydrate chemistry
  • Glycobiology
  • Materials science

Background:

  • Polysaccharides are vital biomolecules but challenging to produce, characterize, and apply due to their complexity.
  • Existing synthetic mimics often involve unnatural components or modification difficulties.
  • A need exists for safer, more accessible carbohydrate-based systems.

Purpose of the Study:

  • To develop self-assembling glycopeptide conjugates as versatile polysaccharide mimics.
  • To investigate the role of natural linkages and modifications in self-assembly and safety.
  • To evaluate the biological activity of these novel carbohydrate structures.

Main Methods:

  • Synthesis of self-assembling glycopeptide conjugates with natural O-glycosidic linkages and phosphoryl modifications.
  • Characterization of nanoparticle formation in aqueous solutions.
  • Assessment of immunostimulatory effects using cellular assays and mouse vaccination models.

Main Results:

  • Conveniently accessible glycopeptide conjugates were successfully synthesized and self-assembled into nanoparticles.
  • These nanoparticles displayed structurally controllable carbohydrates, mimicking polysaccharides.
  • A mannosylated glycopeptide conjugate demonstrated significant immunostimulatory effects in vitro and in vivo.

Conclusions:

  • Glycopeptide conjugates offer a promising platform for creating tunable carbohydrate mimics.
  • The developed system provides a safer and more manageable approach to harnessing polysaccharide functions.
  • This platform has potential applications in areas requiring precise control over carbohydrate presentation and biological activity.