Angew. Chem. Int. Ed. http://doi.org/f2ss49 (2014)
The formation of cerebral amyloid fibrils as a result of the aggregation of amyloid β peptides is indicative of Alzheimer's disease. Now, Linqi Shi and colleagues demonstrate the inhibition of amyloid β fibrillation using mixed-shell polymeric micelles (MSPM). The micelles, formed from the self-assembly of two amphiphilic copolymers, have a poly(caprolactone) core and a mixed shell of polyethylene oxide and poly(N-isopropylacrylamide) (PNIPAM). At physiological temperature, the PNIPAM chains collapse and form hydrophobic domains. These domains interact with the hydrophobic amyloid β peptides and their oligomeric aggregates, and hence, inhibit the formation of fibrils. The ratio of polymers within the shell can be altered to tune the surface properties and influence amyloid β fibrillation. Shi and colleagues also report that the proteolytic degradation of MSPM–amyloid β peptide complexes is greater than that of mature amyloid fibrils. This combination of prevention of fibril formation by the binding of amyloid β peptides and oligomeric species with the ability to degrade amyloid β aggregates, results in the reduction of amyloid-β-mediated neurotoxicity in in vitro studies.
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Stoddart, A. Aggregate prevention. Nature Mater 13, 769 (2014). https://doi.org/10.1038/nmat4053