Amyloid protein fibrillation is responsible for variety of neurological disorders and thus inhibition of fibrillation is a potential therapeutic strategy for these diseases. Recent study shows that nanoparticles can significantly influence the kinetics of amyloid fibrillation, depending on their surface chemistry. Here we demonstrate that amyloid fibril formation can be completely inhibited by nanoparticles coated with histidine-based polymer. We have designed nanoparticles with modular surface chemistry and found that the presence of cationic and anionic surface charge, along with weakly hydrophobic functional groups, is essential in inhibiting the amyloid fibrillation processes. This work shows that the appropriate nanoprobe can be designed for controlling the amyloid fibrillation kinetics and for complete inhibition of fibrillation.
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Palmal et al. (2014) studied this question.
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