Recombinant expression and purification of α-synuclein
Gabriel Gardner1, Morgan Malone2, Vijay Rangachari2
1Mississippi INBRE Research Scholar, Alcorn State University, Lorman, MS
2Chemistry and Biochemistry, School of Mathematics and Natural Sciences, The University of Southern Mississippi, Hattiesburg, MS
Parkinson disease (PD) is a progressive neurodegenerative disease that movements balance and posture among elderly patients. The cause of the disease is mainly attributed to the aberrant deposits of the protein, α-synuclein (αS). This protein is found throughout nerve cells in presynaptic terminals, which release neurotransmitters from synaptic vesicles. In PD, the αS protein aggerates to form intracellular deposits celled, ‘Lewy bodies’. In order to understand the properties of aS and how they affect the neurons, the summer work in the lab involved recombinant expression and purification of αS protein in E. coli. The protein was purified using chitin affinity column followed by HFIP treatment and fractionation via size exclusion chromatography. The protein was purified and characterized for purity and used in biophysical experiments. The results and findings are presented in the poster.