Mechanism and regulation of protein aggregation in complicated cellular systems

2017 Fiscal Year Final Research Report

• Project/Area Number: 15H04362
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Single-year Grants
• Section: 一般
• Research Field: Biophysics
• Research Institution: Osaka University
• Principal Investigator: Goto Yuji 大阪大学, たんぱく質研究所, 教授 (40153770)
• Co-Investigator(Kenkyū-buntansha): 櫻井 一正 近畿大学, 先端技術総合研究所, 准教授 (10403015)
• Co-Investigator(Renkei-kenkyūsha): OGI HIROTSUGU 大阪大学, 大学院工学研究科, 教授 (90252626)
• Project Period (FY): 2015-04-01 – 2018-03-31
• Keywords: 蛋白質 / 脳神経変性疾患 / 生体分子 / 凝集 / 変性 / アミロイド線維 / 溶解度 / 過飽和

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.

Free Research Field

蛋白質科学