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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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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

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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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Glycosaminoglycans01:23

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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.
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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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Oligosaccharide Assembly01:24

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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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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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Multivalent glycans for biological and biomedical applications.

Yujun Kim1, Ji Young Hyun2, Injae Shin1

  • 1Department of Chemistry, Yonsei University, Seoul 03722, Republic of Korea. njae@yonsei.ac.kr.

Chemical Society Reviews
|August 4, 2021
PubMed
Summary

Synthetic multivalent glycans offer enhanced binding to proteins, aiding in understanding biological processes and developing new biomedical agents. This review covers advances in their design and applications from 2014-2020.

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Area of Science:

  • Carbohydrate Chemistry
  • Glycobiology
  • Biomedical Engineering

Background:

  • Protein-glycan interactions are vital for cellular functions and implicated in diseases like infections and cancer.
  • Multivalent glycans exhibit significantly stronger binding affinities compared to their monomeric forms.
  • This enhanced binding property makes multivalent glycans valuable tools for biological research and therapeutic development.

Purpose of the Study:

  • To review recent advancements (2014-2020) in the synthesis of multivalent glycans.
  • To discuss the biological and biomedical applications of these synthetic glycan structures.
  • To provide insights for researchers designing novel multivalent glycans with targeted activities.

Main Methods:

  • Review of literature published between 2014 and 2020.
  • Focus on synthetic multivalent glycan constructs including neoglycopeptides, neoglycoproteins, glycodendrimers, glycopolymers, glyconanoparticles, and glycoliposomes.
  • Analysis of reported biological and biomedical applications.

Main Results:

  • Significant progress in the development of diverse synthetic multivalent glycan architectures.
  • Demonstrated utility of these glycans in elucidating glycan-mediated biological processes.
  • Successful application in the discovery and development of novel glycan-based biomedical agents.
  • Examples include neoglycopeptides, neoglycoproteins, glycodendrimers, glycopolymers, glyconanoparticles, and glycoliposomes.

Conclusions:

  • Synthetic multivalent glycans represent a powerful platform for biological and biomedical applications.
  • Continued innovation in their design and synthesis is yielding promising results.
  • This field holds significant potential for future therapeutic and diagnostic strategies.