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Maintenance of Amyloid β Peptide Homeostasis by Artificial Chaperones Based on Mixed-Shell Polymeric Micelles
- Source :
- Angewandte Chemie International Edition. 53:8985-8990
- Publication Year :
- 2014
- Publisher :
- Wiley, 2014.
-
Abstract
- The disruption of Aβ homeostasis, which results in the accumulation of neurotoxic amyloids, is the fundamental cause of Alzheimer's disease (AD). Molecular chaperones play a critical role in controlling undesired protein misfolding and maintaining intricate proteostasis in vivo. Inspired by a natural molecular chaperone, an artificial chaperone consisting of mixed-shell polymeric micelles (MSPMs) has been devised with tunable surface properties, serving as a suppressor of AD. Taking advantage of biocompatibility, selectivity toward aberrant proteins, and long blood circulation, these MSPM-based chaperones can maintain Aβ homeostasis by a combination of inhibiting Aβ fibrillation and facilitating Aβ aggregate clearance and simultaneously reducing Aβ-mediated neurotoxicity. The balance of hydrophilic/hydrophobic moieties on the surface of MSPMs is important for their enhanced therapeutic effect.
- Subjects :
- Biocompatibility
Polymers
Catalysis
law.invention
Microscopy, Electron, Transmission
law
medicine
Homeostasis
Micelles
Amyloid beta-Peptides
biology
Chemistry
Circular Dichroism
Neurotoxicity
P3 peptide
General Medicine
General Chemistry
medicine.disease
Kinetics
Proteostasis
Biochemistry
Chaperone (protein)
biology.protein
Biophysics
Suppressor
Spectrophotometry, Ultraviolet
Protein folding
Molecular Chaperones
Subjects
Details
- ISSN :
- 14337851
- Volume :
- 53
- Database :
- OpenAIRE
- Journal :
- Angewandte Chemie International Edition
- Accession number :
- edsair.doi.dedup.....6f0f8750b8a873d3323babf2edb0c499