Nanobiocatalyst facilitated aglycosidic quercetin as a potent inhibitor of tau protein aggregation

Sanjay Kumar, V. Guru Krishnakumar, Vinod Morya, Sharad Gupta, Bhaskar Datta*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Polyphenols have been suggested as potential therapeutic agents for the treatment of amyloidogenic diseases. In this work, we evaluate quercetin-rich onion extract for its ability to inhibit tau fibrillization. Considering the presence of polyphenols in multiple glycosidic and aglycosidic forms, a nanobiocatalyst-mediated approach has been used to extract quercetin from onion skins. The nanobiocatalysts facilitate greater release of quercetin compared to the use of free enzymes. Atomic force microscopy and fluorescence microscopy show that quercetin possesses a novel inhibitory character on tau-fibril aggregation. In contrast, quercetin-diglucoside does not have an inhibitory effect. Molecular Dynamics simulations reveal conformational changes in tau protein upon interaction with quercetin due to specific hydrogen bonding and hydrophobic interactions. The resulting conformational stability of tau monomer reduces propensity of the protein to aggregate. The ability of quercetin to inhibit tau fibrillization expands the paradigm for application of bioactive polyphenols.

Original languageEnglish
Pages (from-to)168-180
Number of pages13
JournalInternational Journal of Biological Macromolecules
Volume138
DOIs
StatePublished - 1 Oct 2019
Externally publishedYes

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