Artigo Acesso aberto Revisado por pares

Tunable assembly of amyloid-forming peptides into nanosheets as a retrovirus carrier

2015; National Academy of Sciences; Volume: 112; Issue: 10 Linguagem: Inglês

10.1073/pnas.1416690112

ISSN

1091-6490

Autores

Bin Dai, Dan Li, Wenhui Xi, Fang Luo, Xiang Zhang, Man Zou, Mi Cao, Jun Hu, Wenyuan Wang, Guanghong Wei, Yi Zhang, Cong Liu,

Tópico(s)

HIV Research and Treatment

Resumo

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.

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