胶粘剂
纳米技术
材料科学
粘附
仿生学
水下
淀粉样蛋白(真菌学)
分子动力学
纳米结构
复合材料
生物物理学
化学
生物
图层(电子)
地质学
计算化学
无机化学
海洋学
作者
Chao Zhong,Thomas Gurry,Allen A. Cheng,Jordan Downey,Zhengtao Deng,Collin M. Stultz,Timothy K. Lu
标识
DOI:10.1038/nnano.2014.199
摘要
Many natural underwater adhesives harness hierarchically assembled amyloid nanostructures to achieve strong and robust interfacial adhesion under dynamic and turbulent environments. Despite recent advances, our understanding of the molecular design, self-assembly and structure-function relationships of these natural amyloid fibres remains limited. Thus, designing biomimetic amyloid-based adhesives remains challenging. Here, we report strong and multi-functional underwater adhesives obtained from fusing mussel foot proteins (Mfps) of Mytilus galloprovincialis with CsgA proteins, the major subunit of Escherichia coli amyloid curli fibres. These hybrid molecular materials hierarchically self-assemble into higher-order structures, in which, according to molecular dynamics simulations, disordered adhesive Mfp domains are exposed on the exterior of amyloid cores formed by CsgA. Our fibres have an underwater adhesion energy approaching 20.9 mJ m(-2), which is 1.5 times greater than the maximum of bio-inspired and bio-derived protein-based underwater adhesives reported thus far. Moreover, they outperform Mfps or curli fibres taken on their own and exhibit better tolerance to auto-oxidation than Mfps at pH ≥ 7.0.
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