| Literature DB >> 31183916 |
Pu Chun Ke1, Emily H Pilkington1, Yunxiang Sun2,3, Ibrahim Javed1, Aleksandr Kakinen1, Guotao Peng4, Feng Ding2, Thomas P Davis1,5.
Abstract
Amyloidosis 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.Entities:
Keywords: amyloidosis; nanocomposites; nanomaterials; oligomers
Mesh:
Year: 2019 PMID: 31183916 PMCID: PMC6904546 DOI: 10.1002/adma.201901690
Source DB: PubMed Journal: Adv Mater ISSN: 0935-9648 Impact factor: 30.849