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Inhibition and disaggregation of amyloid β protein fibrils through conjugated polymer–core thermoresponsive micelles

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Abstract

Excess aggregation of amyloid β peptide (Aβ) is a fatal cause of Alzheimer's disease (AD), which leads to physiological toxicity. Inhibiting and disaggregating the Aβ aggregates is an effective strategy to reduce physiological toxicity in neuronal cells. Herein, conjugated polymer-based thermoresponsive micelles (CPMs) were designed with an efficient thermoresponsive surface and a reactive-oxygen-species (ROS)-generating core. In this work, the CPMs exhibited a strong capability to capture the toxic Aβ aggregates at physiological temperature. Under white-light irradiation, ROS was generated in the CPMs, and the toxic Aβ aggregates were efficiently disaggregated through the oxidation of ROS, leading to appropriate Aβ homeostasis between aggregation and disaggregation and reduced the Aβ-induced cytotoxicity. Therefore, the multifunctional micelles of CPMs with both capturing shells and ROS functional cores present a promising strategy to reduce Aβ fibrillation-induced cytotoxicity.

Graphical abstract: Inhibition and disaggregation of amyloid β protein fibrils through conjugated polymer–core thermoresponsive micelles

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Supplementary files

Article information


Submitted
31 Jul 2020
Accepted
14 Sep 2020
First published
21 Sep 2020

J. Mater. Chem. B, 2020, Advance Article
Article type
Paper

Inhibition and disaggregation of amyloid β protein fibrils through conjugated polymer–core thermoresponsive micelles

H. Geng, H. Yuan, L. Qiu, D. Gao, Y. Cheng and C. Xing, J. Mater. Chem. B, 2020, Advance Article , DOI: 10.1039/D0TB01863E

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