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Self‐Assembled Peptide–Polyoxometalate Hybrid Nanospheres: Two in One Enhances Targeted Inhibition of Amyloid β‐Peptide Aggregation Associated with Alzheimer's Disease
Author(s) -
Li Meng,
Xu Can,
Wu Li,
Ren Jinsong,
Wang Enbo,
Qu Xiaogang
Publication year - 2013
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201202612
Subject(s) - bifunctional , peptide , polyoxometalate , amyloid (mycology) , biophysics , fibril , chemistry , fluorescence , amyloid fibril , nanoparticle , materials science , nanotechnology , biochemistry , amyloid β , medicine , disease , pathology , biology , inorganic chemistry , physics , quantum mechanics , catalysis
Amyloid fibril formation is a critical step in Alzheimer's disease (AD) pathogenesis. Inhibition of Aβ aggregation has shown promising against AD and has been used in clinic trials. Here, a novel strategy is reported for the self‐assembly of polyoxometalate–peptide (POM@P) hybrid particles as bifunctional Aβ inhibitors. The two‐in‐one bifunctional POM@P nanoparticles show an enhanced inhibition effect on amyloid aggregation in mice cerebrospinal fluid. Incorporating a clinically used Aβ fibril‐staining dye, congo red (CR), into the hybrid colloidal spheres, the nanoparticles can also act as an effective fluorescent probe to monitor the inhibition process of POM@P via CR fluorescence change in real time. It is believed that such flexible organic–inorganic hybrid systems may prompt the design of new multifunctional materials for AD treatment.