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Related Concept Videos

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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RNA editing is a post-transcriptional modification where a precursor mRNA (pre-mRNA) nucleotide sequence is changed by base insertion, deletion, or modification. The extent of RNA editing varies from a few hundred bases, in mitochondrial DNA of trypanosomes, to a just single base, in nuclear genes of mammals. Even a single base change in the pre-mRNA can convert a codon for one amino acid into the codon for another amino acid or a stop codon. This type of re-coding can significantly affect the...
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Protein Modifications in the RER01:26

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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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Protein Glycosylation01:25

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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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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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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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Author Spotlight: Understanding Rhamnolipid Regulation in Pseudomonas aeruginosa
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Recent advances in β-l-rhamnosylation.

Diksha Rai1, Suvarn S Kulkarni1

  • 1Department of Chemistry, Indian Institute of Technology Bombay, Powai, Mumbai, 400076, India. suvarn@chem.iitb.ac.in.

Organic & Biomolecular Chemistry
|April 10, 2020
PubMed
Summary

Synthesizing beta-l-rhamnose, a key component of pathogen carbohydrates, is challenging. This review covers recent advances in beta-l-rhamnosylation methods and their use in creating complex oligosaccharides.

Area of Science:

  • Carbohydrate Chemistry
  • Organic Synthesis
  • Glycoscience

Background:

  • L-Rhamnose is a crucial monosaccharide in pathogen-associated antigenic oligosaccharides and polysaccharides.
  • Achieving 1,2-cis stereoselectivity in l-rhamnoside glycosylation is difficult due to steric and electronic factors, and lack of neighboring group participation.
  • Despite challenges, various synthetic strategies have been developed to achieve beta-stereoselectivity in l-rhamnosylation.

Purpose of the Study:

  • To review recent advancements in beta-l-rhamnosylation methodologies.
  • To highlight the application of these methods in the total synthesis of biologically significant beta-l-rhamnose-containing oligosaccharides.

Main Methods:

  • Exploration of diverse synthetic pathways for glycosylation of l-rhamnose derivatives.

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  • Application of developed methodologies in complex oligosaccharide synthesis.
  • Analysis of stereochemical outcomes, focusing on achieving beta-selectivity.

    • Main Results:

    • Successful development of various strategies to overcome stereochemical challenges in beta-l-rhamnosylation.
    • Demonstration of the utility of these methods in constructing complex carbohydrate structures.
    • Expansion of synthetic accessibility to important beta-l-rhamnose containing natural products.

    Conclusions:

    • Significant progress has been made in achieving beta-stereoselectivity in l-rhamnosylation.
    • These advancements facilitate the synthesis of biologically relevant oligosaccharides containing beta-l-rhamnose.
    • The reviewed methodologies offer valuable tools for carbohydrate chemists and drug discovery efforts.