Glycoscience is important in many areas such as human health, energy and material science. Glycans have been shown to be involved in the pathophysiology of almost every major disease. Additional glycan structure knowledge is required to help advance personal medicine, and pharmaceutical developments, among others. For glycoscience to advance there is a need for large quantities of well-defined glycans and have quick access to glycosyltransferases for manipulating glycan synthesis.
Herein, we will cover our efforts on studying the substrate specificities of human glycosyltransferases such as FUT8 and Gn-T V, and their application on N-glycan synthesis. Complex asymmetric N-glycan isomer structures have been related to many diseases such as breast cancer, among others. Synthesis of complex asymmetric N-glycan isomer structures including: alpha-1,6 core-fucosylated, and tri-antennary structures can be achieved by taking advantage of the high specificity of glycosyltransferases that can work as unique catalyst to generate well-defined glycan structures.
| Identifer | oai:union.ndltd.org:GEORGIA/oai:scholarworks.gsu.edu:chemistry_diss-1133 |
| Date | 15 December 2016 |
| Creators | Calderon Molina, Angie Dayan |
| Publisher | ScholarWorks @ Georgia State University |
| Source Sets | Georgia State University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Chemistry Dissertations |
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