Physical and chemical analyses of aggregation mechanism by using Prion fragment peptides

2017 Fiscal Year Final Research Report

• Project/Area Number: 15K07908
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Physical pharmacy
• Research Institution: Setsunan University
• Principal Investigator: Akizawa Toshifumi 摂南大学, 薬学部, 教授 (30202526)
• 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)
• Project Period (FY): 2015-04-01 – 2018-03-31
• 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

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.

Free Research Field

分析化学