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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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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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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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Protein Folding Quality Check in the RER01:29

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Tail-anchoring of Proteins in the ER Membrane01:45

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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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.
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Sulfonium-Containing Glycopolypeptides Tethering Trehalose for Protein Stabilization.

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New cationic trehalose-glycopolypeptides effectively stabilize proteins like glucose oxidase (GOx). These polymers protect GOx from lyophilization and heat, maintaining its enzymatic activity and preventing aggregation.

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Area of Science:

  • Biomaterials Science
  • Polymer Chemistry
  • Protein Stabilization

Background:

  • Protein denaturation due to aggregation is a significant challenge.
  • External stimuli can compromise protein structure and function.
  • Developing effective protein stabilization methods is crucial for various applications.

Purpose of the Study:

  • To synthesize novel cationic trehalose-glycopolypeptides.
  • To evaluate the stabilization efficacy of these polymers on a model protein, glucose oxidase (GOx).
  • To investigate the protection against lyophilization and thermal stress.

Main Methods:

  • Synthesis of poly(ethylene glycol)-b-(l-methionine-g-trehalose) (PEG-b-(Met-g-Tre)) polymers.
  • Formation of polyionic complexes (PICs) between glycopolypeptides and GOx.
  • Isothermal titration calorimetry (ITC) to study interactions.
  • Lyophilization and heating experiments to assess protein stability.
  • Transmission electron microscopy (TEM) to visualize protein aggregation.

Main Results:

  • PICs formed between trehalose-glycopolypeptides and GOx via electrostatic interactions.
  • GOx retained approximately 80% enzymatic activity after six lyophilization cycles.
  • PEG-b-(Met-g-Tre) demonstrated protective effects against heating at 60 °C.
  • TEM results indicated prevention of protein aggregation, preserving GOx bioactivity.

Conclusions:

  • A synthesis strategy for precise preparation of trehalose-glycopolypeptides was established.
  • The synthesized glycopolypeptides offer a robust method for stabilizing proteins.
  • These findings contribute to the development of advanced protein stabilization techniques.