Abstract
Amyloids are self-assembled protein aggregates that take cross-β 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.
Highlights
It has been proposed that the incompletely self-assembled oligomeric intermediates may be responsible for the cellular toxicity [73]. This will suggest that when beneficial amyloid fibrils are formed, the reaction will go to completion to prevent the accumulation of oligomeric byproducts
Providing additional control over hydrogel assembly and its physical and mechanical The chirality of amino acids can potentially affect the structure of amyloid fibril, properties [91]
Amyloid fibrils can be engineered to form unique chemical environments to catalyze. Benefitting from their fibrillar morphology, amyloid fibrils can be engineered or reactions, where catalytic sites can be introduced to the amyloid sequences and the fibril modified into conductive materials
Summary
Advances in material science have revealed the sequence-structure-function relationship for multiple types of protein-based biomaterials [7]. Amyloids are proteins that can fold into β-sheet and self-assemble to form elongated and unbranched fibrils that are a few nanometers in diameter and up to a few micrometers in length [8] They were first identified when studying brain tissues of patients with neurodegenerative diseases [9]. That is capable of aggregation and forming amyloid fibrils, though not all of them will take such conformation [27] These findings suggest that amyloid structures alone do not necessarily lead to pathogenicity and can potentially be engineered into biocompatible functional materials. This review focuses on recent advances in engineering amyloids peptides or proteins as functional materials in macroscopic scales. We highlight the numerous applications such as hydrogels, fibers, composites, sensors, and catalysts
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