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Related Concept Videos

Proteoglycans01:05

Proteoglycans

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,...
Protein Glycosylation01:25

Protein Glycosylation

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...
Targets for Drug Action: Overview01:26

Targets for Drug Action: Overview

Drugs target macromolecules to modify ongoing cellular processes. Primary drug targets include receptors, ion channels, transporters, and enzymes.
Receptors are either membrane-spanning or intracellular proteins, which upon binding a ligand, get activated and transmit the signal downstream to elicit a response. Drugs bind receptors, either mimicking the action of endogenous ligands or blocking the receptor activity to bring about a modified response. Nearly 35% of approved drugs target the G...
Targeted Cancer Therapies02:57

Targeted Cancer Therapies

The targeted cancer therapies, also known as “molecular targeted therapies,” take advantage of the molecular and genetic differences between the cancer cells and the normal cells. It needs a thorough understanding of the cancer cells to develop drugs that can target specific molecular aspects that drive the growth, progression, and spread of cancer cells without affecting the growth and survival of other normal cells in the body.
There are several types of targeted therapies against specific...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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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Related Experiment Video

Updated: Jun 23, 2026

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

Therapeutically targeting protein-glycan interactions.

A Rek1, E Krenn, A J Kungl

  • 1ProtAffin Biotechnologie AG, Graz, Austria.

British Journal of Pharmacology
|April 18, 2009
PubMed
Summary

Glycosylation, the attachment of sugar chains to proteins, impacts many diseases. New research highlights targeting these protein-glycan interactions for novel therapeutics.

Area of Science:

  • Biochemistry
  • Glycobiology
  • Pharmacology

Background:

  • Glycosylation is a common protein modification, crucial for biological processes.
  • O-linked glycans, such as glycosaminoglycans, significantly influence inflammation, coagulation, cancer, and viral infections.
  • Protein-glycan interactions modulate protein structure and function, impacting numerous (patho-)biological processes.

Purpose of the Study:

  • To provide an overview of current therapeutic approaches targeting protein-glycan interactions.
  • To discuss the advantages and disadvantages of these novel therapeutic strategies.
  • To highlight the potential of pharmacologically interfering with protein-glycan interactions.

Main Methods:

  • Review of existing literature on glycosylation and protein-glycan interactions.

More Related Videos

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
10:07

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

Related Experiment Videos

Last Updated: Jun 23, 2026

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
10:07

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

  • Analysis of therapeutic strategies targeting these interactions.
  • Discussion of recent advancements in '-ome' sciences (proteomics, glycomics).

    • Main Results:

    • Protein-glycan interactions are complex but increasingly targetable.
    • Novel inhibitors are progressing through preclinical and clinical studies.
    • The antithrombin III-glycan interaction serves as a long-standing example of successful targeting.

    Conclusions:

    • Targeting protein-glycan interactions offers significant therapeutic potential.
    • Advancements in glycomics and proteomics facilitate the development of new drugs.
    • Pharmacological interference with these interactions is a promising area for future medicine.