Dr. Albert Korir's Undergraduate Research
Analytical Studies on Protein-Binding Activities of Glycosaminoglycans
Heparin and HS are linear and highly sulfated complex polysaccharides ubiquitously found on all mammalian cell surfaces and within the extracellular matrix. They are members of GAGs which bind selectively to a variety of proteins and pathogens and therefore play important roles in many physiological and pathological processes including angiogenesis, anticoagulation and metastasis. Many of the biological functions of GAGs have been discovered using heparin. Heparin and related HS consist of repeating disaccharide sequences of hexuronic acid (D-glucuronic or L-iduronic) and D-glucosamine joined via α(1->4) or β(1->4) glycosidic linkages. The residues have varying levels of N- or O-sulfation resulting in chemical heterogeneity of the heparin and HS chain. The chemical heterogeneity facilitates binding to a variety of biomolecules such as chemokines. Soluble GAGs can potentially inhibit binding of a chemokine to its receptor thus blocking its biological activity. Our lab is involved in developing and improving analytical methods to separate and characterize GAG sequences important for protein-binding.