超分子化学
淀粉样蛋白(真菌学)
二肽
测试表
淀粉样纤维
化学
生物物理学
材料科学
肽
纳米技术
分子
淀粉样β
生物
生物化学
有机化学
无机化学
疾病
病理
医学
作者
Wei Ji,Chengqian Yuan,Priyadarshi Chakraborty,Pandeeswar Makam,Santu Bera,Sigal Rencus‐Lazar,Junbai Li,Xuehai Yan,Ehud Gazit
出处
期刊:ACS Nano
[American Chemical Society]
日期:2020-05-19
卷期号:14 (6): 7181-7190
被引量:73
标识
DOI:10.1021/acsnano.0c02138
摘要
Conformational transition of proteins and peptides into highly stable, β-sheet-rich structures is observed in many amyloid-associated neurodegenerative disorders, yet the precise mechanism of amyloid formation at the molecular level remains poorly understood due to the complex molecular structures. Short peptides provide simplified models for studying the molecular basis of the assembly mechanism that governs β-sheet fibrillation processes underlying the formation and inhibition of amyloid-like structures. Herein, we report a supramolecular coassembly strategy for the inhibition and transformation of stable β-sheet-rich amyloid-derived dipeptide self-assemblies into adaptable secondary structural fibrillar assemblies by mixing with bipyridine derivatives. The interplay between the type and mixing ratio of bipyridine derivatives allowed the variable coassembly process with stimuli-responsive functional properties, studied by various experimental characterizations and computational methods. Furthermore, the resulting coassemblies showed functional redox- and photoresponsive properties, making them promising candidates for controllable drug release and fluorescent imprint. This work presents a coassembly strategy not only to explore the mechanism of amyloid-like structure formation and inhibition at the molecular level but also to manipulate amyloid-like structures into responsive supramolecular coassemblies for material science and biotechnology applications.
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