Related Experiment Video
Updated: Aug 5, 2026
08:49
Printed Glycan Array: A Sensitive Technique for the Analysis of the Repertoire of Circulating Anti-carbohydrate Antibodies in Small Animals
Published on: February 14, 2019
Using Synthetic Glycans to Investigate Anti-Glycan Antibodies and Explore Their Medical Potential
Fabienne Weber1,2, Aina Valenti1,2, Jiří Ledvinka1,2
1Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Potsdam, Germany.
Angewandte Chemie (International Ed. in English)
|July 27, 2026
Summary
Synthetic glycans are revolutionizing antibody development for immune surveillance. These advanced carbohydrate structures enable new diagnostics, therapeutics, and personalized medicine approaches for various diseases.
Area of Science:
- Immunology
- Carbohydrate Chemistry
- Biomedical Research
Background:
- The cell-surface glycan layer is crucial for immune functions like pathogen defense and cancer surveillance.
- Endogenous anti-glycan antibodies are key to identifying abnormal cellular structures.
- Glycans are promising targets for immunotherapies but their complexity hinders development.
Purpose of the Study:
- To summarize strategies for using synthetic glycans in antibody development.
- To explore applications of synthetic glycans in research and medicine.
- To highlight the potential of synthetic glycans in personalized medicine.
Main Methods:
- Advances in automated solid-phase assembly, chemoenzymatic strategies, and one-pot synthesis provide access to well-defined glycans.
- Utilizing synthetic glycans for antibody development and profiling antibody repertoires.
- Applying synthetic glycans in diagnostic and therapeutic antibody development.
Main Results:
- Synthetic glycans offer unprecedented access to homogenous and complex structures.
- These synthetic glycans facilitate biomarker discovery through antibody repertoire profiling.
- Applications range from vaccine design to therapeutic antibody development.
Conclusions:
- Synthetic glycans are powerful tools for advancing antibody development.
- They enable new diagnostic and therapeutic strategies in translational medicine.
- Synthetic glycans hold significant promise for personalized medicine applications.
Related Concept Videos
01:05Proteoglycans
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,...
01:25Protein 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...
Glycosylation occurs in...