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A resorcinarene for inhibition of A? fibrillation.


ABSTRACT: Amyloid-? peptides (A?) fibrillation is the hallmark of Alzheimer's disease (AD). However, it has been challenging to discover potent agents in order to inhibit A? fibrillation. Herein, we demonstrated the effect of resorcinarene on inhibiting A? fibrillation in vitro via experimental and computational methods. A? were incubated with different concentrations of resorcinarene so as to monitor the kinetics by using thioflavin T binding assay. The results, which were further confirmed by far-UV CD spectroscopy and atomic force microscopy, strongly indicated that the higher concentration of resorcinarene, the more effective the inhibition of A? fibrillation. A cytotoxicity study showed that when sea urchin embryos were exposed to the resorcinarene, the majority survived due to the resorcinarene low toxicity. In addition, when the resorcinarene was added, the formation of toxic A? 42 species was delayed. Computational studies of A? fibrillation, including docking simulations and MD simulations, illustrated that the interaction between inhibitor resorcinarene and A? is driven by the non-polar interactions. These studies display a novel strategy for the exploration of promising antiamyloiddogenic agents for AD treatments.

PROVIDER: S-EPMC5398272 | BioStudies | 2017-01-01T00:00:00Z

REPOSITORIES: biostudies

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