Abstract
Biological functions of a variety of proteins are mediated via their interaction with glycosaminoglycans (GAGs). The structural diversity within the wide GAG landscape provides individual interaction sites for a multitude of proteins involved in several pathophysiological processes. This ‘GAG angle’ of such proteins as well as their specific GAG ligands give rise to novel therapeutic concepts for drug development. Current glycomic technologies to elucidate the glycan structure–function relationships, methods to investigate the selectivity and specificity of glycan–protein interactions and existing therapeutic approaches to interfere with GAG–protein interactions are discussed.
Financial & competing interests disclosure
All authors are employees of ProtAffin Biotechnologie AG, Austria. The company has interest in the development of protein-based GAG antagonists. The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.
No writing assistance was utilized in the production of this manuscript.