Investigation of acetylation of β-2 microglobulin to trigger misfolding

• In Event: Poster Presentation and Judging for: Biomedical; Cell & Molecular Biology; Chemistry & Biochemistry; Marine Science; Systematics & Evolutionary Biology.
  In Poster Session: Chemistry & Biochemistry Poster Session

Abstract

β-2 Microglobulin (B2M) is a component of the class 1 major histocompatibility complex molecule which is an integral component of the immune system. When B2M misfolds it forms an amyloid fibril, which leads to the chronic disease dialysis related amyloidosis. It is still a mystery what initially triggers misfolding of this protein in the human body. However, in a separate study it was shown that changing the net charge of a protein will affect its ability to self-assemble into aggregates by optimizing the repulsive intermolecular interactions electrostatically. Conversely, the change in the net charge of a protein could also induce the self-assembly of aggregates by reducing electrostatic repulsion. Acetylation was used to introduce a change in the net charge to test the hypothesis that reducing the net charge will increase the rate of amyloid formation. A common acetylating agent that is used in everyday life is aspirin. Acetic anhydride, a slightly stronger acetylating agent, was chosen to be used. Purified B2M was taken and reacted it with the acetic anhydride and analyzed it using SDS- Page gel. From the gel we could see that the acetic anhydride caused splitting in the bands of the gel. This does not confirm acetylation of the protein, however it does tells us that acetic there is a chemical change occurring in the B2M which warrants further investigation.

Author

• Robbie Moore, Austin College