Abstract
The Alzheimer’s disease (AD) therapeutic research is yielding large number of potent molecules. The nanoparticle-based therapeutics against the protein aggregation in AD is also taking a lead especially with amyloid beta as a primary target. In this work, we have screened for first time, the protein capped (PC) metal nanoparticles for their potency in inhibiting Tau aggregation in vitro. We present a novel function of PC-CdS nanoparticles as a potent Tau aggregation inhibitor by fluorescence spectrometry, SDS-PAGE and Electron microscopy. We demonstrate that the biologically synthesized PC-metal nanoparticles, iron oxide and cadmium sulphide do not affect the viability of neuroblastoma cells. Moreover, PC-CdS nanoparticles show dual property of inhibition as well as disaggregation of Tau. Thus, the nanoparticles can take a lead as potent Tau aggregation inhibitors and can be modified for specific drug delivery due to very small size. This current work presents unprecedented strategy to design anti-Tau aggregation drugs, which provides interesting insights to understand the role of biological nanostructures in Alzheimer’s disease.
Supplementary materials
Title
SI-Tau-NPs-2019
Description
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