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Phosphodiester Linkages01:01

Phosphodiester Linkages

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Phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.
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Phosphorylation01:02

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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In cellular metabolism (the complete breakdown of glucose to extract energy),  glycolysis is the first step. Glycolysis takes place in the cytoplasm of both prokaryotic and eukaryotic cells. Glucose enters heterotrophic cells in two ways. One method is through secondary active transport, where the transport takes place against the glucose concentration gradient. The other mechanism uses a group of integral proteins called GLUT proteins, also known as glucose transporter proteins. These...
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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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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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Phosphates as Assisting Groups in Glycan Synthesis.

Eric T Sletten1, Giulio Fittolani1, Nives Hribernik1

  • 1Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, 14476 Potsdam, Germany.

ACS Central Science
|January 31, 2024
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Scientists used phosphates to control the synthesis of complex sugars called glycans. Removing phosphates revealed the final structure and triggered the formation of nanostructures.

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Area of Science:

  • Carbohydrate Chemistry
  • Glycobiology
  • Biotechnology

Background:

  • Biological pathways utilize reversible phosphorylation for regulation.
  • Chemical synthesis of complex oligosaccharides faces challenges like aggregation and site-specificity.
  • Glycans play crucial roles in various biological processes.

Purpose of the Study:

  • To adapt the biological concept of phosphorylation for chemical synthesis of glycans.
  • To achieve site-specific enzymatic modification of synthetic glycans.
  • To develop a method for solubilizing and isolating aggregating glycans.
  • To trigger the self-assembly of glycan nanostructures.

Main Methods:

  • Chemical phosphorylation of synthetic glycans at specific sites.
  • Enzymatic elongation using sialylation guided by phosphate groups.
  • Utilizing phosphates for glycan solubilization and isolation.
  • Enzymatic dephosphorylation using alkaline phosphatase.

Main Results:

  • Site-specific enzymatic sialylation of glycans was achieved.
  • Phosphorylation improved the solubility and isolation of aggregating glycans.
  • Traceless removal of phosphates regenerated the native glycan structures.
  • The dephosphorylation step triggered the self-assembly of glycan nanostructures.

Conclusions:

  • Phosphorylation serves as a versatile tool in synthetic glycobiology.
  • This method overcomes limitations in complex glycan synthesis and enables nanostructure formation.
  • Enzymatic dephosphorylation is a key step for revealing native structures and initiating assembly.