Amyloid formation characteristics of GNNQQNY from yeast prion protein Sup35 and its seeding with heterogeneous polypeptides

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• 作者：Mamoru Haratake^a ; ^{haratake@ph.sojo-u.ac.jp} ; Tohru Takiguchi^b ; Naho Masuda^b ; Sakura Yoshida^b ; Takeshi Fuchigami^b ; Morio Nakayama^b ; ^{morio@nagasaki-u.ac.jp}
• 关键词：Prion ; Yeast ; Amyloid ; Aggregation ; β-Sheet ; Thioflavin T ; Seeding
• 刊名：Colloids and Surfaces B: Biointerfaces
• 出版年：2017
• 出版时间：1 January 2017
• 年：2017
• 卷：149
• 期：Complete
• 页码：72-79
• 全文大小：1179 K
• 卷排序：149

文摘

Aggregation transition behavior of GNNQQNY to the amyloid state was investigated. Intensive stirring resulted in accelerated self-aggregation of GNNQQNY. The GNNQQNY aggregates served as seeds for the elongation of the monomeric GNNQQNY. The GNNQQNY aggregate could possibly promote the amyloid fibril formation of insulin. Monomeric GNNQQNY can bind to amyloid-β fibrils on mice brain section.