Conformational Changes in Alpha-Synuclein Upon Binding to Fatty Acids
Parkinson's disease (PD) is a detrimental neurodegenerative disease that effects one's motor movements in addition to a host of other equally serious ailments. Parkinson's occurs when neurons in the substantia nigra die or become impaired. Parkinson's disease is distinguished by aggregations that have been formed by the neural protein alpha-synuclein (AS). The normal function of alpha-synuclein is unknown. Given that the typical function of this PD causing protein is unknown any information adding to the current knowledge of AS is of great value to the scientific community. The study was focused on the effects of fatty acids on AS. Arachidonic acid is an unsaturated fatty acid that is believed to bind alpha-synuclein and cause multimerization. We propose that alpha-synuclein will bind arachidonic acid and not oleic acid. The study was performed using gel exclusion chromatography to analyze the fatty acid and AS samples. In addition, the gel exclusion fractions were run on a 15% protein gel in order to measure the protein size of each of the collected fractions. We found that when alpha-synuclein is incubated with arachidonic acid they bind and the alpha-synuclein changes conformation. This conformational change caused a decrease in the AS and arachidonic acid samples mobility. This effect was not seen when alpha-synuclein was incubated with oleic acid.
School:
California State University, Fullerton
Department:
Biological Sciences
Research Advisor:
Julia George
Department of Research Advisor:
Molecular and Integrative Physiology
Year of Publication:
2007