Title

Biochemical Characterization Of Alpha-Synuclein Containing Protein Aggregates In A Yeast Model For Parkinson’S Disease

Author(s)

Sydney Hart

School Name

South Carolina Governor's School for Science and Mathematics

Grade Level

12th Grade

Presentation Topic

Cell and Molecular Biology

Presentation Type

Mentored

Mentor

Mentor: Renee Chosed, Biology Department, Furman University

Oral Presentation Award

2nd Place

Abstract

Parkinson's disease (PD) is a disorder where the brain’s motor neurons are affected, resulting in tremors, impaired balance, and muscle spasms. Aggregates and oligomers of the α-synuclein protein were discovered in the dopaminergic neurons of post-mortem PD patients. It is unknown as to why these aggregates and oligomers form or how they cause the symptoms of PD. This study used the budding yeast, Saccharomyces cerevisiae, as a model for the examination of these α-synuclein proteins by overexpressing the protein, leading to its aggregation. The results of this study showed that the human alpha-synuclein gene, tagged with His6 and GFP, can be successfully integrated into the yeast genome. These α-synuclein-containing aggregates and oligomers were purified using affinity chromatography and detergents. The next step will be analysis using mass spectrometry to identify any other proteins or particles aggregated along with α-synuclein. Once the components of these aggregates and oligomers are identified, greater insight will be gained on their formation in the neurons, thus leading to pharmaceuticals that could inhibit the formation of these multi-protein complexes.

Start Date

4-11-2015 8:45 AM

End Date

4-11-2015 9:00 AM

COinS
 
Apr 11th, 8:45 AM Apr 11th, 9:00 AM

Biochemical Characterization Of Alpha-Synuclein Containing Protein Aggregates In A Yeast Model For Parkinson’S Disease

Parkinson's disease (PD) is a disorder where the brain’s motor neurons are affected, resulting in tremors, impaired balance, and muscle spasms. Aggregates and oligomers of the α-synuclein protein were discovered in the dopaminergic neurons of post-mortem PD patients. It is unknown as to why these aggregates and oligomers form or how they cause the symptoms of PD. This study used the budding yeast, Saccharomyces cerevisiae, as a model for the examination of these α-synuclein proteins by overexpressing the protein, leading to its aggregation. The results of this study showed that the human alpha-synuclein gene, tagged with His6 and GFP, can be successfully integrated into the yeast genome. These α-synuclein-containing aggregates and oligomers were purified using affinity chromatography and detergents. The next step will be analysis using mass spectrometry to identify any other proteins or particles aggregated along with α-synuclein. Once the components of these aggregates and oligomers are identified, greater insight will be gained on their formation in the neurons, thus leading to pharmaceuticals that could inhibit the formation of these multi-protein complexes.