earticle

영어

Human α-synuclein, a small unfolded protein, has been implicated to play a significant role in Parkinson's disease (PD) and other related diseases. The N-terminal regions of α-synuclein contains seven imperfect repeat sequences (KTKE(Q)GV), which are involved in the aggregation and fibrillation process with their aptitudes to form α- helices. The missense mutants (A30P, E46K, A53T) in the α-synuclein have been discovered in PD patients. In this study, we made three Nterminal deletion mutants (1-35, 1-50, 1-60), and they were expressed in Eschrichia coli BL21, and purified by ion exchange chromatography. Their structural properties were investigated by using circular dichroism, spectrofluorometer, dynamic light scattering, chemical cross-linking, and size exclusion. In addition, ionic liquids (ILs), which are organic salts with high polarity and negligible vapor pressure are used to form amyloid fibrils of α-synuclein.