Self-assembled peptide-polyoxometalate hybrid nanospheres: two in one enhances targeted inhibition of amyloid β-peptide aggregation associated with Alzheimer's disease.

Abstract

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.

• Authors: Meng Li, Can Xu, Li Wu, Jinsong Ren, Enbo Wang, Xiaogang Qu
• Journal: Small (Weinheim an der Bergstrasse, Germany) (Small) Vol. 9 Issue 20 Pg. 3455-61 (Oct 25 2013) ISSN: 1613-6829 [Electronic] Germany
• PMID: 23650245 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Chemical References

• Amyloid beta-Peptides
• Colloids
• Tungsten Compounds
• polyoxometalate I
• Congo Red

Topics

• Alzheimer Disease (pathology)
• Amyloid beta-Peptides (antagonists & inhibitors, chemistry, toxicity)
• Animals
• Cell Death (drug effects)
• Colloids (chemistry)
• Congo Red (metabolism)
• Kinetics
• Mice
• Microscopy, Fluorescence
• Nanospheres (chemistry, ultrastructure)
• PC12 Cells
• Protein Structure, Quaternary
• Rats
• Tungsten Compounds (pharmacology)