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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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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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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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Glycocalyx and its Functions01:14

Glycocalyx and its Functions

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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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Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

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Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
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Glycosaminoglycans01:23

Glycosaminoglycans

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Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
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Facile and Efficient Preparation of Tri-component Fluorescent Glycopolymers via RAFT-controlled Polymerization
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ROMP-based Glycopolymers with High Affinity for Mannose-Binding Lectins.

Clément Gonnot1, Mathieu Scalabrini2, Benoit Roubinet3

  • 1Institut des Molécules et Matériaux du Mans (IMMM), UMR 6283 CNRS - Le Mans Université, Avenue Olivier Messiaen, 72085 Le Mans Cedex 9 France.

Biomacromolecules
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Summary
This summary is machine-generated.

Novel glycopolymers were synthesized using ring-opening metathesis polymerization and postpolymerization modification. These advanced materials exhibit potent multivalent inhibition of carbohydrate-lectin interactions, showing promise for therapeutic applications.

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Area of Science:

  • Polymer Chemistry
  • Carbohydrate Chemistry
  • Biomaterials Science

Background:

  • Lectins are proteins that bind carbohydrates, playing roles in biological processes.
  • Modulating lectin activity is crucial for understanding and treating lectin-mediated diseases.
  • Multivalent interactions can significantly enhance binding affinity and biological activity.

Purpose of the Study:

  • To synthesize well-defined glycopolymers with controlled architecture.
  • To investigate the potential of these glycopolymers in inhibiting carbohydrate-lectin interactions.
  • To explore the impact of multivalent effects on binding inhibition.

Main Methods:

  • Ring-opening metathesis polymerization (ROMP) of norbornenyl azlactone to create polymer backbones.
  • Postpolymerization modification (PPM) via click aminolysis to attach various glycosides.
  • Evaluation of binding inhibition against a panel of lectins using synthesized glycopolymers.

Main Results:

  • Successfully synthesized poly(norbornenyl azlactone)s with controlled molecular weights.
  • Glycopolymers functionalized with pegylated mannoside demonstrated potent binding inhibition (subnanomolar IC50s).
  • Polymers exhibited significantly enhanced inhibitory activity compared to monovalent analogues due to multivalent effects.

Conclusions:

  • Sugar-functionalized poly(norbornenyl azlactone)s are effective tools for studying multivalent carbohydrate-lectin interactions.
  • These glycopolymers show promise for applications targeting lectin-mediated bacterial and viral binding to host cells.
  • The study highlights the power of polymer design and multivalent presentation in modulating biological interactions.