@article {46242,
	title = {Protein-capped metal nanoparticles inhibit tau aggregation in alzheimer{\textquoteright}s disease},
	journal = {Acs Omega},
	volume = {4},
	year = {2019},
	month = {JULY},
	pages = {12833-12840},
	type = {Article},
	abstract = {<p>The Alzheimer{\textquoteright}s disease (AD) therapeutic research is yielding a 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 the first time protein-capped (PC) metal nanoparticles for their potency in inhibiting Tau aggregation in vitro. We present a novel function of PC-Fe3O4 and PC-CdS nanoparticles as potent Tau aggregation inhibitors by fluorescence spectrometry, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and electron microscopy. We demonstrate that the biologically synthesized PC-metal nanoparticles, especially iron oxide do not affect the viability of neuroblastoma cells. Moreover, PC-CdS nanoparticles show dual properties of inhibition and 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 their very small size. The current work presents unprecedented strategy to design anti-Tau aggregation drugs, which provides interesting insights to understand the role of biological nanostructures in Alzheimer{\textquoteright}s disease.<br />
	\&nbsp;</p>
},
	doi = {10.1021/acsomega.9b01411},
	author = {Sonawane, Shweta Kishor and Ahmad, Absar and Chinnathambi, Subashchandrabose}
}
