Aggregation and Fibrillation Study of α-synuclein Under Applied Voltage

Abstract

The application of voltage has been used to control the movement of charged molecule such as DNA, some proteins and phospholipid in recent year. In this study, we first applied voltage to amyloidogenic protein, α-synuclein, which is related to Parkinson’s disease. To offer the new approach using electric field and new insight into aggregation and fibrillation mechanism of α-synuclein, we tried to control the aggregation of α-synuclein, which has a negative charge, by applying voltage to it. The aggregation of α-synuclein without conformational change occurred rapidly when a voltage of 1 V was applied. The protein did not form amyloid-like fibrils, but it did form small aggregates. These results demonstrate that this technique might be useful not only to efficiently control aggregation of α-syn but also to understand the mechanism of aggregation and fibrillation of α-syn.