| Budget Amount *help |
¥16,250,000 (Direct Cost: ¥12,500,000、Indirect Cost: ¥3,750,000)
Fiscal Year 2017: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
Fiscal Year 2016: ¥6,240,000 (Direct Cost: ¥4,800,000、Indirect Cost: ¥1,440,000)
Fiscal Year 2015: ¥6,890,000 (Direct Cost: ¥5,300,000、Indirect Cost: ¥1,590,000)
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| Outline of Final Research Achievements |
Understanding the mechanisms of protein aggregation is important for advancing our knowledge of proteins. Amyloid fibrils are fibrillar aggregates associated with various amyloidoses. On the other hand, the term amorphous aggregate has been used for other types of aggregates. However, the relationship between amyloid fibrils and amorphous aggregates has not yet been elucidated. We studied the aggregation of various proteins with a focus on distinguishing amyloid fibrils and amorphous aggregates. The results indicated that amyloid fibrils and amorphous aggregates correspond to crystals and glasses of solutes, respectively, and that solubility and supersaturation are two of the most important factors determining protein aggregation. Further understanding the role of supersaturation in determining aggregation-based phase transitions of denatured proteins will provide an important complementary point of view to structural studies of protein aggregates.
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