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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...
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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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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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Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives
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Synthesis of poly(aspartimide)-based bio-glycoconjugates.

Irina Carlescu1, Helen M I Osborn, Jacques Desbrieres

  • 1Department of Natural and Synthetic Polymers, Faculty of Chemical Engineering and Environmental Protection, Gh. Asachi of Iasi, Technical University, Bd. D. Mangeron 71A, 700050 Iasi, Romania.

Carbohydrate Research
|November 14, 2009
PubMed
Summary

Researchers synthesized novel bioconjugates using poly(aspartimide) to inhibit influenza virus. Aliphatic linkers effectively incorporated sialic acid, unlike aromatic linkers, showing potential for antiviral drug development.

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Area of Science:

  • Polymer chemistry and medicinal chemistry
  • Bioconjugation strategies
  • Antiviral research

Background:

  • Influenza virus poses a significant global health threat.
  • Developing novel antiviral agents is crucial for pandemic preparedness.
  • Poly(aspartimide) offers a versatile scaffold for drug delivery and bioconjugation.

Purpose of the Study:

  • To synthesize and analyze novel bioconjugates for potential influenza virus inhibition.
  • To investigate the use of poly(aspartimide) as a polymer support for antiviral compounds.
  • To explore the influence of linker structure on the incorporation of sialic acid derivatives.

Main Methods:

  • Synthesis of poly(aspartimide)-based bioconjugates.
  • Attachment of sialic acid-linker-amine compounds to the polymer backbone.
  • Characterization using Nuclear Magnetic Resonance (NMR) spectroscopy ((1)H and (13)C).

Main Results:

  • Successful synthesis of poly(aspartimide)-sialic acid bioconjugates.
  • NMR analysis confirmed varying degrees of compound incorporation.
  • Aliphatic linkers facilitated higher incorporation of sialic acid compared to aromatic linkers.

Conclusions:

  • The study demonstrates the feasibility of using poly(aspartimide) for creating potential influenza inhibitors.
  • Linker chemistry significantly impacts the successful conjugation of sialic acid derivatives.
  • These findings provide a basis for designing more effective antiviral bioconjugates.