| 초록 |
The flexible region of the amyloidogenic protein contributes to the conformational rearrangements which are essential for oligomerization and fibrillation. Here, we have employed on intrinsically unstructured amyloidogenic α-synuclein to study the influence of this flexible region on their fibrillation process. Two amino acid residues, one from the N- and the other from the C- terminal, V3 and A140, were selected and mutated into cysteine. After treating with oxidizing agent, the mutant protein formed intramolecular disulfide bond and it developed into circular form of α-synuclein (CFαS). This CFaS showed dramatically reduced tendency to form fibrils due to the limited terminal activity and decrease in flexibility. However, the CFαS still involved in the fibrillation process when coincubated with the wild type α-synuclein (WTαS). Also, we successfully recovered the fibrillation propensity of the mutant protein by introducing reducing agent to break the disulfide bond of the CFaS. |
