Tama Ghosh

Insights into FUT8 substrate binding: a computational modeling approach

Tama Ghosh
MSc Student 
Department of Biochemistry

Date: December 2, 2024
Time: 1:00 p.m. to 2:00 p.m. 
Room: CSF 1302

 

Abstract:

Glycosylation is the addition of a sugar (carbohydrate) to another molecule, and this process plays a vital role in human health and immune response. In many cancers and infectious diseases there are changes to glycans (i.e., carbohydrate chains) and therefore targeting these changes is a way to create new treatments and diagnostics tools. The changes to the glycans occur due to the action of enzymes. FUT8 is one such enzyme that plays a key role in glycosylation process in our cells. Unfortunately, when FUT8 adds too many additional sugars to the glycan this contributes to cancer and infectious diseases. FUT8 drive the addition of a sugar (α-1,6-fucose) to the innermost sugar (N-acetyl-D-glucosamine, GlcNAc), which is known as core fucosylation. Core fucosylation is important for the modulation of cellular behavior, in both healthy and disease states. Therefore, by controlling the abnormal activity of FUT8 a new way of drug discovery can be unfold. Specifically, previous experimental work has indicated that with the changes of glycan structures, the enzymes catalytic activity also changes. This study aims to identify the structure and function of FUT8 by using computational modeling that analyzes the substrate binding to FUT8. This work will establish a foundation for future research in developing potential therapeutic targeting FUT8 for the treatment of cancer and infectious diseases.