Synergistic Inhibitory Effect of Peptide–Organic Coassemblies on Amyloid Aggregation

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• 作者：Lin Niu ; Lei Liu ; Wenhui Xi ; Qiusen Han ; Qiang Li ; Yue Yu ; Qunxing Huang ; Fuyang Qu ; Meng Xu ; Yibao Li ; Huiwen Du ; Rong Yang ; Jacob Cramer ; Kurt V. Gothelf ; Mingdong Dong ; Flemming Besenbacher ; Qingdao Zeng ; Chen Wang ; Guanghong Wei ; Yanlian Yang
• 刊名：ACS Nano
• 出版年：2016
• 出版时间：April 26, 2016
• 年：2016
• 卷：10
• 期：4
• 页码：4143-4153
• 全文大小：899K
• 年卷期：0
• ISSN：1936-086X

文摘

Inhibition of amyloid aggregation is important for developing potential therapeutic strategies of amyloid-related diseases. Herein, we report that the inhibition effect of a pristine peptide motif (KLVFF) can be significantly improved by introducing a terminal regulatory moiety (terpyridine). The molecular-level observations by using scanning tunneling microscopy reveal stoichiometry-dependent polymorphism of the coassembly structures, which originates from the terminal interactions of peptide with organic modulator moieties and can be attributed to the secondary structures of peptides and conformations of the organic molecules. Furthermore, the polymorphism of the peptide−organic coassemblies is shown to be correlated to distinctively different inhibition effects on amyloid-β 42 (Aβ42) aggregations and cytotoxicity.