
AbstractAmyloidosis is a biophysical phenomenon of protein aggregation with biological and pathogenic implications. Among the various strategies developed to date, nanomaterials and multifunctional nanocomposites possessing certain structural and physicochemical traits are promising candidates for mitigating amyloidosis in vitro and in vivo. The mechanisms underpinning protein aggregation and toxicity are introduced, and opportunities in materials science to drive this interdisciplinary field forward are highlighted. Advancement of this emerging frontier hinges on exploitation of protein self‐assembly and interactions of amyloid proteins with nanoparticles, intracellular and extracellular proteins, chaperones, membranes, organelles, and biometals.
amyloidosis, 570, 2500 Materials Science, 2210 Mechanical Engineering, Amyloidosis, Nanostructures, 2211 Mechanics of Materials, Nanomedicine, nanocomposites, Animals, Humans, Computer Simulation, oligomers, nanomaterials
amyloidosis, 570, 2500 Materials Science, 2210 Mechanical Engineering, Amyloidosis, Nanostructures, 2211 Mechanics of Materials, Nanomedicine, nanocomposites, Animals, Humans, Computer Simulation, oligomers, nanomaterials
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 103 | |
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| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 1% |
