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Related Concept Videos

Biosynthesis of Polysaccharides01:26

Biosynthesis of Polysaccharides

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Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...
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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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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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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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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.
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ATP and Macromolecule Synthesis01:28

ATP and Macromolecule Synthesis

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Biological macromolecules are organic compounds, predominantly composed of carbon atoms. The carbon atoms are covalently bonded with hydrogen, oxygen, nitrogen, and other minor elements. There are four major biological macromolecule classes: carbohydrates, lipids, proteins, and nucleic acids.
Most macromolecules are composed of single subunits, or building blocks, called monomers. The monomers combine with each other using covalent bonds to form larger molecules known as polymers.
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Related Experiment Video

Updated: Aug 22, 2025

Activation and Conjugation of Soluble Polysaccharides using 1-Cyano-4-Dimethylaminopyridine Tetrafluoroborate CDAP
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Activation and Conjugation of Soluble Polysaccharides using 1-Cyano-4-Dimethylaminopyridine Tetrafluoroborate CDAP

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A Poly-ADP-Ribose Polymer-GCSF Conjugate.

Qinqin Cheng1, Xiao-Nan Zhang1, Lei Zhang1

  • 1Department of Pharmacology and Pharmaceutical Sciences, School of Pharmacy, University of Southern California, Los Angeles, California 90089, United States.

Biomacromolecules
|November 9, 2022
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Summary
This summary is machine-generated.

Polymer-drug conjugates using poly-ADP-ribose (PAR) polymers and granulocyte colony-stimulating factor (GCSF) protein show potent cell proliferation and sustained high neutrophil levels in mice, demonstrating therapeutic potential.

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Area of Science:

  • Biotechnology
  • Polymer Chemistry
  • Cellular Biology

Background:

  • Poly-ADP-ribose (PAR) is a biocompatible polymer involved in cellular signaling.
  • PARPs synthesize PAR, regulating cellular processes.
  • PAR's properties suggest potential for therapeutic delivery.

Purpose of the Study:

  • To create PAR polymer-GCSF conjugates for therapeutic applications.
  • To evaluate the efficacy of PAR polymer-GCSF conjugates in vitro and in vivo.

Main Methods:

  • Human PARP1-catalyzed auto-poly-ADP-ribosylation was used to synthesize PAR polymers.
  • A clickable NAD+ analogue was employed for conjugation.
  • PAR polymers were conjugated with human granulocyte colony-stimulating factor (GCSF) protein.
  • Cell proliferative activity and in vivo neutrophil levels were assessed.

Main Results:

  • The PAR polymer-GCSF conjugate demonstrated potent cell proliferative activity.
  • A single dose in mice led to sustained high neutrophil levels for 11 days.
  • The conjugate showed excellent in vivo efficacy.

Conclusions:

  • Functionalized PAR polymers serve as effective scaffolds for therapeutic protein/peptide conjugation.
  • PAR polymer-based conjugates offer improved pharmacological activities.
  • This approach holds promise for developing novel therapeutics.