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.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
3F32GM069157-02S1
Application #
7147091
Study Section
Special Emphasis Panel (ZRG1)
Program Officer
Marino, Pamela
Project Start
2003-09-15
Project End
2006-07-14
Budget Start
2004-09-15
Budget End
2006-07-14
Support Year
2
Fiscal Year
2006
Total Cost
$41,330
Indirect Cost
Name
University of California Berkeley
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
124726725
City
Berkeley
State
CA
Country
United States
Zip Code
94704
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