Nanochaperones: Potential therapeutic approach for 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 (amyloids) that lose their normal physiological roles and acquire toxicity.  Recent findings suggest that the accumulation and spread of amyloids arises from proteostasis network impairment. These observations are certainly contributing to the current change of focus in anti-amyloid drug design, whose efforts are so far centered on single-target approaches aimed at inhibiting amyloid aggregation. Chaperones, known to maintain proteostasis, hence represent ideal therapeutic targets owing to their potential protective role against conformational 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.