Technology > Science of Glycans
Glycans are linear or branched polysaccharides which drive a variety of biological processes mainly by binding proteins and modulating their function. Specifically, glycosaminoglycans (GAGs) consist of typical disaccharide building blocks which arrange into extended stretches of linear, O-linked polysaccharides. These long carbohydrate chains are covalently attached to core proteins, the so-called proteoglycans, and they exhibit well-defined domain structures resulting from specific sulfation patterns which selectively bind to proteins.
The best known GAG in therapeutic terms is heparin, which has been marketed for over 40 years for its anti-thrombolytic properties. Other members of the GAG family include heparan sulfate and chondroitin sulfate, both of which constitute the extracellular glycan network. By binding to many varied proteins such as chemokines, growth factors, metalloproteases,and integrins, the extracellular matrix (ECM) is a key therapeutic hot spot in the body, since all cell-cell interactions are governed by constituents of the ECM.
The majority of marketed pharmaceuticals are based on modifying interactions between proteins and other proteins or small molecules. Development of monoclonal antibodies (mAbs) has greatly improved the ability to modulate protein-protein interactions; however, regulation of protein function by modulating protein-glycan interactions has largely remained unexplored.
ProtAffin has developed a novel approach to modulate protein-glycan interactions and modify protein function.
