Nanochaperone‐Based Strategies to Control Protein Aggregation Linked to Conformational Diseases

The generation of highly organized amyloid fibrils is associated with a wide range of conformational pathologies, including primarily neurodegenerative diseases. Such disorders are characterized by misfolded proteins that lose their normal physiological roles and acquire toxicity. Recent findings su...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2021-01, Vol.60 (1), p.41-52
Main Authors: Caballero, Ana B., Gamez, Patrick
Format: Article
Language:English
Subjects:
Agglomeration
Amyloid
chaperone
Chaperones
conformational disease
Disorders
Drug development
Fibrils
Humans
misfolding
Molecular Chaperones - chemistry
Molecular Conformation
nanoparticle
Nanoparticles
Neurodegenerative diseases
Protein Aggregates - genetics
Protein Folding
Protein interaction
Proteins
Proteostasis Deficiencies - genetics
Proteostasis Deficiencies - pathology
Toxicity
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Summary:The generation of highly organized amyloid fibrils is associated with a wide range of conformational pathologies, including primarily neurodegenerative diseases. Such disorders are characterized by misfolded proteins that lose their normal physiological roles and acquire toxicity. Recent findings suggest that proteostasis network impairment may be one of the causes leading to the accumulation and spread of amyloids. These observations are certainly contributing to a new focus in anti‐amyloid drug design, whose efforts are so far being centered on single‐target approaches aimed at inhibiting amyloid aggregation. Chaperones, known to maintain proteostasis, hence represent interesting targets for the development of novel therapeutics owing to their potential protective role against protein misfolding diseases. In this minireview, research on nanoparticles that can either emulate or help molecular chaperones in recognizing and/or correcting protein misfolding is discussed. The nascent concept of “nanochaperone” may indeed set future directions towards the development of cost‐effective, disease‐modifying drugs to treat several currently fatal disorders. Nanoparticles with chaperone‐like activity may be considered as potential therapeutic agents to treat conformational diseases. This Minireview aims at emphasising the essential features required by nanomaterials to deal with toxic protein misfolding and accumulation.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.202007924