期刊
NATURE COMMUNICATIONS
卷 11, 期 1, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-019-14257-0
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资金
- Office of Naval Research [N000141812258]
- National Science Foundation [CMMI-1752172]
- Paul N. Cook Career Development Professorship
- MIT Presidential Graduate Fellowship
- U.S. Department of Defense (DOD) [N000141812258] Funding Source: U.S. Department of Defense (DOD)
Despite advances in directing the assembly of biomacromolecules into well-defined nanostructures, leveraging pathway complexity of molecular disorder to order transition while bridging materials fabrication from nano- to macroscale remains a challenge. Here, we present templated crystallization of structural proteins to nanofabricate hierarchically structured materials up to centimeter scale, using silk fibroin as an example. The process involves the use of ordered peptide supramolecular assemblies as templates to direct the folding and assembly of silk fibroin into nanofibrillar structures. Silk polymorphs can be engineered by varying the peptide seeds used. Modulation of the relative concentration between silk fibroin and peptide seeds, silk fibroin molecular weight and pH allows control over nanofibrils morphologies and mechanical properties. Finally, facile integration of the bottom-up templated crystallization with emerging top-down techniques enables the generation of macroscopic nanostructured materials with potential applications in information storage/encryption, surface functionalization, and printable three-dimensional constructs of customized architecture and controlled anisotropy. Despite recent progress in directed assembly of protein molecules into well-defined nanostructures, bridging materials fabrication from nano- to macroscale remains a challenge. Here, using silk fibroin as an example, the authors demonstrate templated crystallization to drive hierarchical materials growth from disordered molecules all the way up to centimeter scale.
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