Human serum albumin (HSA) is the most abundant transport protein in blood. It has astonishing capacities to bind metabolites and a wide range of drugs (i.e. warfarin, ibuprofen, and indomethacin). Physiological and pathological changes can induce an alteration of protein conformation and efficiency of ligand binding resulting in the function impairment in HSA. Covalently binding to glucose (glycation) is one of basic impairments found in HSA. Glycated HSA (GHSA) has been used as a biomarker for glycemic control. Especially, earlier studies observed high concentration of GHSA in diabetic patients. Thus, many studies were devoted to explore the feasibility of GHSA as a diabetes biomarker.

        In addition to glucose, galactose and fructose were also able to bind to HSA. Glucose and galactose are hexose monosaccharide where galactose is a C4 epimer of glucose. Both sugars were found to share several glycation sites and similar glycation mechanism. Apart from diabetes with glucated HSA, monitoring galactated proteins may provide a useful tool for galactosemia control. Some other monosaccharides and carbohydrates can also bind to HSA.

        Our group employs Molecular Dynamics (MD) simulations to understand the binding mechanism and affinity of sugars. Our first aim is to understand the nature of sugar binding activities and reveal how such binding impacts on protein conformation and function. When such processes are well understood, we then explore the possibility of glycated HSA as a diabetic biomarker. The designed aptamer has been used to detect the level of GHSA in a sample. Also, our collaborator uses this aptamer to design an aptasensor. Our second task is to explain how this aptamer binds and detect only GHSA in order to improve the aptamer selectivity. There are still a lot of interesting work to do.