| Literature DB >> 30369028 |
Ava Faridi1,2, Yunxiang Sun3, Yutaka Okazaki4, Guotao Peng2, Jie Gao4, Aleksandr Kakinen1, Pouya Faridi5, Mei Zhao2, Ibrahim Javed1, Anthony W Purcell5, Thomas P Davis1, Sijie Lin2, Reiko Oda4, Feng Ding3, Pu Chun Ke1.
Abstract
Amyloid fibrils generally display chirality, a feature which has rarely been exploited in the development of therapeutics against amyloid diseases. This study reports, for the first time, the use of mesoscopic chiral silica nanoribbons against the in vivo amyloidogenesis of human islet amyloid polypeptide (IAPP), the peptide whose aggregation is implicated in type 2 diabetes. The thioflavin T assay and transmission electron microscopy show accelerated IAPP fibrillization through elimination of the nucleation phase and shortening of the elongation phase by the nanostructures. Coarse-grained simulations offer complementary molecular insights into the acceleration of amyloid aggregation through their nonspecific binding and directional seeding with the nanostructures. This accelerated IAPP fibrillization translates to reduced toxicity, especially for the right-handed silica nanoribbons, as revealed by cell viability, helium ion microscopy, as well as zebrafish embryo survival, developmental, and behavioral assays. This study has implicated the potential of employing chiral nanotechnologies against the mesoscopic enantioselectivity of amyloid proteins and their associated diseases.Entities:
Keywords: amyloidogenesis; chirality; human IAPP; silica nanoribbons; toxicity
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Year: 2018 PMID: 30369028 PMCID: PMC6263833 DOI: 10.1002/smll.201802825
Source DB: PubMed Journal: Small ISSN: 1613-6810 Impact factor: 13.281