Date

2013

Department or Program

Chemistry

Additional Department or Program (if any)

Mathematics

Primary Wellesley Thesis Advisor

Julia H. Miwa

Abstract

Parkinson’s disease is a common neurodegenerative disorder characterized by tremors and motors deficits, caused by the death of dopaminergic neurons and the resulting dopamine depletion in the brain. Examination of the substantia nigra of the brains of Parkinson’s patients reveals abnormal intraneruonal deposition of fibrillar aggregates of the protein alpha-synuclein. While Parkinson’s disease is generally idiopathic in origin, several mutations in alpha-synuclein have been shown to increase the likelihood of the disease. This further implicates alpha-synuclein in the pathogenesis of Parkinson’s disease. This report focuses on wild type alpha-synuclein. A 31-residue peptide corresponding to residues 6-36 of the N-terminus of alpha-synuclein was synthesized, purified, and its conformation examined using circular dichroism spectroscopy. The peptide showed conformational behavior that is similar to what has been found for this region in the full-length protein. Thus, the peptide can be used as a model system for the N-terminal region of alpha-synuclein. In future work, this peptide model and its A30P mutant counterpart can be compared to characterize the role of this mutation in Parkinson’s disease.

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