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- W2129397712 abstract "Significance Many proteins enter the amyloid state, which is associated with human diseases and is also involved in many biological events. Amyloid formed by various proteins has a uniform “cross-β” structure with protein units stacking repetitively into fibrils. This unique structure brings amyloid favorable mechanical and chemical properties, and inspires the exploration of amyloid as a novel class of bionanomaterials. On the other hand, the uniform fibrillar structure limits the application of amyloid materials for a diverse function. This paper illustrates our discovery, structure characterization, design, and application of an amyloid-based structure, termed “amyloid-like nanosheet.” This nanosheet enriches the architectures of amyloid materials and will aid researchers in designing and investigating amyloid with new functions." @default.
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- W2129397712 date "2015-02-23" @default.
- W2129397712 modified "2023-10-14" @default.
- W2129397712 title "Tunable assembly of amyloid-forming peptides into nanosheets as a retrovirus carrier" @default.
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- W2129397712 doi "https://doi.org/10.1073/pnas.1416690112" @default.
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