Protein Capped Metal Nanoparticles Inhibits Tau Aggregation in Alzheimer’s Disease

31 May 2019, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

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.

Keywords

tau aggregation inhibitor
Tauopathies
Nanoparticles Conjugated
Alzheimer's disease

Supplementary materials

Title
Description
Actions
Title
SI-Tau-NPs-2019
Description
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