Chemical Research in Chinese Universities ›› 2022, Vol. 38 ›› Issue (2): 522-528.doi: 10.1007/s40242-021-1372-3

• Articles • Previous Articles     Next Articles

Nanocomposites Facilitate the Removal of Aβ Fibrils for Neuroprotection

CHAI Jingshan, LI Qiushi, ZHAO Yu, LIU Yang   

  1. Key Laboratory of Functional Polymer Materials, Ministry of Education, State Key Laboratory of Medicinal Chemical Biology, College of Chemistry, Nankai University, Tianjin 300071, P. R. China
  • Received:2021-09-16 Revised:2021-11-09 Online:2022-04-01 Published:2021-11-12
  • Contact: ZHAO Yu, LIU Yang E-mail:chemyzhao@nankai.edu.cn;yliu@nankai.edu.cn
  • Supported by:
    This work was supported by the National Key Research and Development Programs of China(No.2018YFA0209700), the Fund of the Frontiers Science Center for New Organic Matter, Nankai University, China(No.63181206), the National Natural Science Foundation of China(Nos. 22077073, 22007051), the Fundamental Research Funds for the Central Universities, Nankai University, China(No.63206015) and the China Postdoctoral Science Foundation (No.2019M660975).

Abstract: Accumulation of β-amyloid(Aβ) fibrils in the brain is one of the main culprits in Alzheimer’s disease(AD) progression, which initiates the neuronal damage and subsequent neurodegeneration. Various anti-Aβ agents have shown the potentials to dissociate Aβ fibrils. However, these approaches can’t facilitate the removal of Aβ fibrils, resulting in a disappointing therapeutic effect. Herein, we demonstrate an integrated polymer nanocomposite(NP-GLVFF-IgG) that can dissociate Aβ fibrils into fragments and activate microglia to remove the fragments via Fc receptors-mediated phagocytosis. NP-GLVFF-IgG is constructed by an albumin/polymer hybrid nanoparticle with Gly-Leu-Val-Phe-Phe (GLVFF) peptides and Immunoglobulin G(IgG) molecules on the surface. In this design, NP-GLVFF-IgG achieves to dissociate the Aβ fibrils by the strong hydrogen-bonding interactions between Aβ fibrils and GLVFF peptides. Then, NP-GLVFF-IgG activates the microglial phagocytosis, thereby achieving an enhanced phagocytic removal of Aβ fibrils for neuroprotection. Moreover, NP-GLVFF-IgG achieves to trigger the effective removal of Aβ fibrils even under inflammatory condition that usually suppressed phagocytosis. Therefore, NP-GLVFF-IgG has great potential as a novel therapeutic platform for effective AD therapy.

Key words: Alzheimer’s disease, Aβ fibril, Nanocomposite, Hydrogen-bonding interaction, Microglia

Copyright © 2019 Editorial office of 《Chemical Research in Chinese Universities》
Communication address:Editorial Department of Chemical Journal of Chinese Universities, 2699 Qianjin Street, Changchun 130012 
Tel.:(86)0431-88499867  Fax:(86)0431-88499216 
E-mail: cjcu@jlu.edu.cn https://crcu.jlu.edu.cn