A lecture entitled “Multivalent homo-and hetero-glycoconjugates (i) To uncover intricate carbohydrate-protein interactions and (ii) In autoimmune therapeutics development” was delivered by Dr. Gour Chand Daskhan, Alberta Glycomics Centre, Department of Chemistry, 4-082 Centennial Centre for Interdisciplinary Science (CCIS), University of Alberta, Edmonton, AB, T6G 2G2, Canada |
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Title of Seminar: |
“Multivalent homo-and hetero-glycoconjugates (i) To uncover intricate carbohydrate-protein interactions and (ii) In autoimmune therapeutics development” was delivered by Dr. Gour Chand Daskhan. |
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Abstract |
Multivalent carbohydrate-protein interactions play crucial role in a diverse range of biological processes. Homoglycoclusters constituted by multiple copies of identical sugar units on the synthetic scaffolds contribute extensively to discovery of many facets of recognition processes. The presence of non-identical sugar units on a scaffold, which we termed a heteroglycocluster, has emerged as an alternative potential ligand to deepen understanding of the complex heterogeneity of the glycocalyx. In this context, using cyclopetides as an artificial templates, construction of diverse range of multivalent homo-and hetero-glycoclusters was accomplished and their lectin binding potency was investigated through a range of biochemical and biophysical methods.[1] |
B-cells play a crucial role in adaptive immunity. Multivalent presentations of well-defined antigens to modulate and suppress B-cell activation, and therefore could be useful as autoimmune therapeutics. Towards these goals, a conjugation strategy consisting of sequential ligation protocols for the self antigen with co-presentation of two different carbohydrate antigens on a poly(ethylene glycol)-based molecular scaffold was developed. Various homo- and hetero-glycoconjugates displaying both ABO-blood group antigens to target B-cell receptors (BCR) ligands with sialoglycan as co-receptor ligands were synthesized. The ability of these hetero-glycoconjugates to recognize and suppress B-cell activation in vitro and in vivo models is currently under investigation. In addition, an analytical protocol based on use of liquid chromatography coupled with fluorescence and mass spectrometric methods was also implemented to profile N-linked glycans.[2] |