These are preliminary reports that have not been peer-reviewed. They should not be regarded as conclusive, guide clinical practice/health-related behavior, or be reported in news media as established information. For more information, please see our FAQs.
Preprints are manuscripts made publicly available before they have been submitted for formal peer review and publication. They might contain new research findings or data. Preprints can be a draft or final version of an author's research but must not have been accepted for publication at the time of submission.
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.