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Amyloids as Building Blocks for Macroscopic Functional Materials: Designs, Applications and Challenges

Journal

Publisher

MDPI
DOI: 10.3390/ijms221910698

Keywords

amyloid fibril; self-assembly; hydrogel; fiber; responsive material; extracellular matrix

Funding

  1. United States Department of Agriculture [20196702129943]
  2. Office of Naval Research [N000141912126]
  3. U.S. Department of Defense (DOD) [N000141912126] Funding Source: U.S. Department of Defense (DOD)

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Amyloids are self-assembled protein aggregates with cross-beta fibrillar morphology. They are not only associated with diseases like Alzheimer's and Parkinson's, but also play important functional roles in diverse organisms. Amyloid fibrils' rigidity, chemical stability, high aspect ratio, and sequence programmability make them attractive for functional materials in environmental sciences, material engineering, and translational medicines.
Amyloids are self-assembled protein aggregates that take cross-beta fibrillar morphology. Although some amyloid proteins are best known for their association with Alzheimer's and Parkinson's disease, many other amyloids are found across diverse organisms, from bacteria to humans, and they play vital functional roles. The rigidity, chemical stability, high aspect ratio, and sequence programmability of amyloid fibrils have made them attractive candidates for functional materials with applications in environmental sciences, material engineering, and translational medicines. This review focuses on recent advances in fabricating various types of macroscopic functional amyloid materials. We discuss different design strategies for the fabrication of amyloid hydrogels, high-strength materials, composite materials, responsive materials, extracellular matrix mimics, conductive materials, and catalytic materials.

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