| Project/Area Number |
15K07908
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Physical pharmacy
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| Research Institution | Setsunan University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
小西 元美 摂南大学, 薬学部, 講師 (20229446)
谷口 将済 摂南大学, 薬学部, 助教 (50710696)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2017: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2016: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2015: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
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| Keywords | プリオンタンパク / 凝集 / 立体構造 / CD / フラグメントペプチド / プリオンタンパク質 / 銅イオン / 分子間相互作用 / CDスペクトル / チオフラビンT / 凝集性 / 構造変化 / アポトーシス / 銅 / Catalytide / Caspase-3 |
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| Outline of Final Research Achievements |
In this study, we analyzed the correlation between secondary structure and aggregation, and effect of Cu2+ and pH by using prion fragment peptides. As a result, hPrP180-192 bound each other in the absence of Cu2+. The secondary structure immediately changed to b-sheet in pH7.5 and binding affinity and aggregation ration were increased. In addition, point mutated peptide, hPrP180-192 V/I show the higher aggregation ratio than hPrP180-192 and irreversible conformational change. These results strongly suggest that C-terminal fragment takes part in aggregation of Prion Protein.
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