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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.
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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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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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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

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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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Formation of Lipopolysaccharides01:19

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Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin,...
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Site-Selective Modification of (Oligo)Saccharides.

Martin D Witte1, Adriaan J Minnaard1

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Site-selective modification of oligosaccharides is crucial for developing new drugs and vaccines. Advances in catalysis are enabling precise chemical and enzymatic modifications for improved efficacy and overcoming resistance.

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Area of Science:

  • Carbohydrate Chemistry
  • Medicinal Chemistry
  • Catalysis

Background:

  • Oligosaccharides are vital biomolecules involved in cellular functions, medicine, and materials science.
  • Understanding oligosaccharide function necessitates targeted modifications, including the incorporation of reactive and reporter groups.
  • The development of oligosaccharide-based therapeutics, such as drugs and vaccines, requires precise structural alterations.

Purpose of the Study:

  • To explore site-selective modification strategies for oligosaccharides.
  • To review advancements in chemical and enzymatic methods for modifying oligosaccharides.
  • To highlight the importance of these modifications for therapeutic applications and overcoming antibiotic resistance.

Main Methods:

  • Review of site-selective modification techniques for mono- and oligosaccharides.
  • Discussion of various catalytic approaches: transition-metal catalysis, enzyme catalysis, organocatalysis, and photoredox catalysis.
  • Emphasis on late-stage modification strategies for naturally available oligosaccharides.

Main Results:

  • Significant progress has been made in developing site-selective and late-stage modification methods for oligosaccharides.
  • Catalysis research has provided powerful tools for precise chemical alterations of carbohydrate structures.
  • Site-selective modification offers an attractive alternative to laborious total synthesis when natural oligosaccharides are accessible.

Conclusions:

  • Site-selective modification of oligosaccharides is key for optimizing drug efficacy and developing new vaccines.
  • The fields of enzymatic and chemical glycan modification are converging, promising future advancements.
  • Further research is needed to fully integrate these approaches for broader applications in glycobiology and medicine.