The ultimate goal of this research is to provide a facile method for tracking O-linked glycosylation in a variety of settings. This will be accomplished via the direct labelling of metabolically labelled O-glycans utilizing a highly adaptable Staudinger-ligation acitivatable fluorogenic dye. The modular nature of synthesis will allow independent tuning of photophysical, chemical and physical characteristics of the probe. A double quench mechanism should provide exceedingly low background, facilitating use with a variety of detection systems. The ability to specifically track O-linked glycosylation has, of yet, been unavailable. Initially this probe will be used in conjunction with 2D gel electrophoresis to provide a """"""""fingerprint"""""""" of O-glycosylation and in conjunction with mass spectrometry techniques will provide the identity of O-linked glycoproteins. Such a method should greatly facilitate efforts to understand the impact of O-linked glycosylation and the mechnasims which regulate this post-translational modification.
| Boyce, Michael; Carrico, Isaac S; Ganguli, Anjali S et al. (2011) Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway. Proc Natl Acad Sci U S A 108:3141-6 |
