01813nas a2200157   4500008004100000245008600041210006900127260000900196300001600205490000600221520122900227100002901456700001701485700003601502856011701538       2019                        eng d00aProtein-capped metal nanoparticles inhibit tau aggregation in alzheimer's disease0 aProteincapped metal nanoparticles inhibit tau aggregation in alz  cJULY  a12833-128400 v43 a<p>The Alzheimer'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's disease.<br />
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1 aSonawane, Shweta, Kishor1 aAhmad, Absar1 aChinnathambi, Subashchandrabose  uhttps://library.ncl.res.in/content/protein-capped-metal-nanoparticles-inhibit-tau-aggregation-alzheimers-disease