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Related Concept Videos

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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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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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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Amyloid Fibrils03:03

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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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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Updated: Oct 2, 2025

Microwave-assisted Functionalization of Polyethylene glycol and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation
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Microwave-assisted Functionalization of Polyethylene glycol and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation

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Protein Aggregation Nucleated by Functionalized Dendritic Polyglycerols.

Samuel P Bernhard1, Mackenzie S Fricke1, Rainer Haag2

  • 1Department of Chemistry and Biochemistry, Bozeman, MT, 59717, USA.

Polymer Chemistry
|February 28, 2022
PubMed
Summary
This summary is machine-generated.

Dendritic polyglycerols (dPGs) functionalized with lactose were synthesized to study galectin-3 aggregation. The size of dPGs influenced galectin-3 multimer formation, highlighting the role of specific protein-carbohydrate interactions.

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Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining
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Area of Science:

  • Biomaterials Science
  • Glycobiology
  • Polymer Chemistry

Background:

  • Dendritic polyglycerols (dPGs) offer low toxicity and biocompatibility, making them suitable for biological studies.
  • Their branched structure and numerous endgroups are ideal for investigating multivalent interactions, including protein-carbohydrate binding.
  • Galectin-3, a protein overexpressed in cancer, plays a role in multivalent interactions.

Purpose of the Study:

  • To synthesize lactose-functionalized dPGs with varying hydrodynamic radii and functional group densities.
  • To investigate the templated aggregation of galectin-3 using these novel dPGs.
  • To elucidate the role of galectin-3's N-terminal domain in multimer formation and compare polymer-templated aggregation mechanisms.

Main Methods:

  • Synthesis of a series of lactose-functionalized dendritic polyglycerols (dPGs).
  • Characterization of dPGs by varying hydrodynamic radii and lactose densities.
  • Dynamic light scattering (DLS) to measure aggregate sizes formed by dPGs and galectin-3.

Main Results:

  • A direct correlation was observed between the hydrodynamic radii of lactose-functionalized dPGs and the size of galectin-3 aggregates.
  • The density of lactose functional groups on dPGs also influenced aggregate formation.
  • The study identified the critical role of galectin-3's N-terminal domain in multimerization.

Conclusions:

  • Lactose-functionalized dPGs effectively template the aggregation of galectin-3.
  • The size and functionalization density of dPGs are key factors in controlling galectin-3 aggregation.
  • These findings provide insights into galectin-3's role in cancer progression and offer a model for studying specific protein-carbohydrate interactions.