Student Scholar Symposium Abstracts and Posters

Document Type

Chapman access only poster or presentation

Publication Date

Fall 12-1-2021

Faculty Advisor(s)

Dr. Cecilia Lopez


Myelin basic protein (MBP) is necessary for the proper function of the central nervous system. Since it maintains the integrity of the myelin sheath, its degradation is implicated in multiple sclerosis (MS). MS is a chronic autoimmune neuromuscular disease that currently has no cure. Patients with MS are typically diagnosed when their immune system reacts to modified forms of MBP. Once translated, MBP is heavily modified by the chemical addition of molecules including phosphoryl (PO3-) and methyl (CH3) groups at serine and arginine residues. Although phosphorylation by various kinases is generally absent in patients with MS, methylated arginine residues as well as the enzyme that causes methylation, PRMT5, have both been implicated in MS and are established markers of autoimmunity. Since arginine groups can be mono- or di-methylated (asymmetric vs. symmetric), we have set out to optimize methods using high performance liquid chromatography (HPLC) for the detection of these three arginine derivatives. Preliminary data shows that monomethylated arginine can be distinguished from dimethylated arginine, however further work to resolve the two dimethylated species is underway. Resolving the two species will allow for a more efficient way to distinguish between healthy modifications of MBP vs. MBP found in MS. Once we can distinguish between these arginine derivatives, we will perform in vitro methylation reactions using modified MBP and resolve these acid hydrolyzed derivatives via HPLC.


Presented at the virtual Fall 2021 Student Scholar Symposium at Chapman University.

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