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Date of Award


Document Type

Campus Access Dissertation

Degree Name

Doctor of Philosophy in Chemistry (PhD)

Administrative Home Department

Department of Chemistry

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Committee Member 1


Committee Member 2


Committee Member 3



Biomarkers are disease specific proteins that are overexpressed under pathological conditions. These proteins save lives because they play key roles in early diagnosis of diseases. Many of these biomarkers are glycosylated proteins (glycoproteins) and their receptors (lectins). Current biomarker detection techniques depend on antibodies and/or tagged reagents. Thus, there is a constant need to develop fast and simple detection techniques that do not require antibodies and labeled reagents. We recently developed such a simple method for (glyco)protein purification/identification and found that this method could also be used for biomarker detection. Our method was able to detect biomarker proteins in blood plasma and in other complex mixtures. One of those detected proteins was human Galectin-3 (Gal-3), a protein that serves as a biomarker for multiple diseases such as cancer, cardiovascular diseases, and diabetes. Gal-3 is a multifunctional protein (lectin), which is overexpressed in a wide variety of cellular and pathological events. However, the molecular basis of its multifunctional property and the reasons behind its occurrence in multiple diseases are poorly understood. Our research has revealed that the binding site of Gal-3 shows considerable plasticity to accommodate a completely unexpected group of ligands, namely proteoglycans and their constituents glycosaminoglycans (GAGs). Our findings explain, at least in part, the multifunctional ability of Gal-3 and provide a reason why this protein is involved in so many pathological events. To understand the plasticity of the binding site of Gal-3, several mutants were generated and characterized. I will present the biomarker detection technique and will discuss the binding site plasticity of Gal-3 as revealed by mutational analysis.