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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
Therapeutically targeting protein-glycan interactions.
British Journal of Pharmacology
|April 18, 2009
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.
- 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.
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