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Related Concept Videos

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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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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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
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CO2-Switchable Supramolecular Block Glycopolypeptide Assemblies.

Qiang Yan1, Hongji Zhang1, Yue Zhao1

  • 1Département de Chimie, Université de Sherbrooke, Sherbrooke, Québec J1K 2R1, Canada.

ACS Macro Letters
|May 20, 2022
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Summary
This summary is machine-generated.

Researchers created a novel CO2-sensitive glycopolypeptide that self-assembles into viral-like structures. This supramolecular block copolymer can reversibly disassemble and reassemble in response to carbon dioxide, mimicking viral capsid dynamics.

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Area of Science:

  • Supramolecular Chemistry
  • Polymer Science
  • Biomaterials

Background:

  • Viral capsid assembly and disassembly are complex processes crucial for viral function.
  • Developing synthetic materials that mimic these dynamic biological processes is a significant challenge.
  • Carbon dioxide (CO2) is a readily available and tunable physiological stimulus.

Purpose of the Study:

  • To design and synthesize a novel supramolecular block glycopolypeptide sensitive to CO2.
  • To investigate the self-assembly behavior of the glycopolypeptide in aqueous solution.
  • To explore the reversible disassembly and assembly triggered by CO2, mimicking viral capsid nanostructures.

Main Methods:

  • Orthogonal coupling of end-functionalized biopolymers: dextran with β-cyclodextrin terminal (Dex-CD) and poly(l-valine) with a benzimidazole tail (BzI-PVal).
  • Host-guest interactions driving end-to-end coupling.
  • Utilizing a CO2-cleavable connection (CD/BzI) for stimulus-responsive behavior.

Main Results:

  • Successful synthesis of a supramolecular block glycopolypeptide.
  • Demonstration of self-assembly into vesicular and fibrous aggregates in aqueous solution.
  • Reversible disassembly and assembly of aggregates in response to CO2 exposure and removal (breathing in/out).

Conclusions:

  • The developed CO2-sensitive supramolecular block glycopolypeptide exhibits reversible self-assembly.
  • This system effectively mimics the dynamic disintegration and construction of viral capsid nanostructures.
  • The findings offer potential for novel biomimetic materials and drug delivery systems.