Evaluating MOG-I-DOMAIN in the Suppression of Experimental Autoimmune Encephalomyelitis

Friday, October 28, 2011
Hall 1-2 (San Jose Convention Center)
Crisandra Wilkie , University of Kansas, Lawrence, KS
Barlas Buyuktimkin , Pharmaceutical Chemistry, University of Kansas, Lawrence, KS
John Stewart , Pharmaceutical Chemistry, University of Kansas, Lawrence, KS
Teruna Siahaan, PhD , Pharmaceutical Chemistry, University of Kansas, Lawrence, KS
The overall purpose of this study is to evaluate the effectiveness of MOG-I-domain in suppressing EAE, a mouse model for multiple sclerosis (MS). My short term goal is to produce a pure MOG-I-domain conjugate for the in vivo studies. MS is a disease within the central nervous system. It is caused when nerve cells become damaged while the myelin sheath is being attacked by T cells. We believe that the conjugated protein will be able to block the signal that causes the T cells to attack. To make the MOG-I-domain conjugate I first had to synthesize the MOG peptide and purify it. After that task was take the peptide and attach it to the I-domain GMB in which it will react at a pH of 8.5. The MOG-I-domain will then go through a final purification through the size exclusion chromatography (SEC). We have been able to successfully synthesize and purify the MOG peptide. We submitted a sample of our peptide to mass spec to be sure that the peak was our pure peptide. Since we have successfully synthesized the PLP peptide to I-domain GMB using the same method we believe we will be able to also synthesize MOG-I-domain with little difficulty.